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https://en.wikipedia.org/wiki/Protein%20N-acetylglucosaminyltransferase | In enzymology, a protein N-acetylglucosaminyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-N-acetyl-D-glucosamine + protein UDP + 4-N-(N-acetyl-D-glucosaminyl)-protein
Thus, the two substrates of this enzyme are UDP-N-acetyl-D-glucosamine and protein, whereas its two products are UDP and 4-N-(N-acetyl-D-glucosaminyl)-protein.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:protein beta-N-acetyl-D-glucosaminyl-transferase. Other names in common use include uridine diphosphoacetylglucosamine-protein, acetylglucosaminyltransferase, uridine diphospho-N-acetylglucosamine:polypeptide, beta-N-acetylglucosaminyltransferase, and O-GlcNAc transferase.
References
External links
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pyridoxine%205%27-O-beta-D-glucosyltransferase | In enzymology, a pyridoxine 5'-O-beta-D-glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + pyridoxine UDP + 5'-O-beta-D-glucosylpyridoxine
Thus, the two substrates of this enzyme are UDP-glucose and pyridoxine, whereas its two products are UDP and 5'-O-beta-D-glucosylpyridoxine.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:pyridoxine 5'-O-beta-D-glucosyltransferase. Other names in common use include UDP-glucose:pyridoxine 5'-O-beta-glucosyltransferase, uridine diphosphoglucose-pyridoxine 5'-beta-glucosyltransferase, and UDP-glucose-pyridoxine glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pyrimidine-nucleoside%20phosphorylase | In enzymology, a pyrimidine-nucleoside phosphorylase () is an enzyme that catalyzes the chemical reaction
a pyrimidine nucleoside + phosphate a pyrimidine base + alpha-D-ribose 1-phosphate
Thus, the two substrates of this enzyme are pyrimidine nucleoside and phosphate, whereas its two products are pyrimidine base and alpha-D-ribose 1-phosphate.
This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is pyrimidine-nucleoside:phosphate alpha-D-ribosyltransferase. This enzyme is also called Py-NPase. This enzyme participates in pyrimidine metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 5, Academic Press, New York, 1961, p. 237-255.
EC 2.4.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Queuine%20tRNA-ribosyltransferase | In enzymology, a queuine tRNA-ribosyltransferase () is an enzyme that catalyzes the chemical reaction
[tRNA]-guanine + queuine [tRNA]-queuine + guanine
Thus, the two substrates of this enzyme are tRNA-guanine and queuine, whereas its two products are [tRNA]-queuine and guanine.
This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is [tRNA]-guanine:queuine tRNA-D-ribosyltransferase. Other names in common use include tRNA-guanine transglycosylase, guanine insertion enzyme, tRNA transglycosylase, Q-insertase, queuine transfer ribonucleate ribosyltransferase, transfer ribonucleate glycosyltransferase, tRNA guanine transglycosidase, guanine, queuine-tRNA transglycosylase, and tRNA-guanine:queuine tRNA-D-ribosyltransferase.
Structural studies
As of late 2007, 36 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , and .
References
EC 2.4.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Raffinose%E2%80%94raffinose%20alpha-galactosyltransferase | In enzymology, a raffinose-raffinose alpha-galactosyltransferase () is an enzyme that catalyzes the chemical reaction
2 raffinose 1F-alpha-D-galactosylraffinose + sucrose
Hence, this enzyme has one substrate, raffinose, and two products, 1F-alpha-D-galactosylraffinose and sucrose.
This enzyme belongs to the family of glycosyltransferases, to be specific the hexosyltransferases. The systematic name of this enzyme class is raffinose:raffinose alpha-D-galactosyltransferase. Other names in common use include raffinose (raffinose donor) galactosyltransferase, raffinose:raffinose alpha-galactosyltransferase, and raffinose-raffinose alpha-galactotransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Salicyl-alcohol%20beta-D-glucosyltransferase | In enzymology, a salicyl-alcohol beta-D-glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + salicyl alcohol UDP + salicin
Thus, the two substrates of this enzyme are UDP-glucose and salicyl alcohol, whereas its two products are UDP and salicin.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:salicyl-alcohol beta-D-glucosyltransferase. Other names in common use include uridine diphosphoglucose-salicyl alcohol 2-glucosyltransferase, and UDPglucose:salicyl alcohol phenyl-glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sarsasapogenin%203%CE%B2-glucosyltransferase | In enzymology, a sarsasapogenin 3β-glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + sarsasapogenin UDP + sarsasapogenin 3-O-β-D-glucoside
Thus, the two substrates of this enzyme are UDP-glucose and sarsasapogenin [(3β,5β,25S)-spirostan-3-ol], whereas its two products are UDP and sarsasapogenin 3-O-β-D-glucoside.
The enzyme was first isolated from the root of the common asparagus (Asparagus officinalis). It is specific for substrate sterols with the uncommon 5β-configuration (sarsasapogenin and smilagenin), that is with a cis-linkage between the A and B rings of the steroid nucleus.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:(3β,5β,25S)-spirostan-3-ol 3-O-β-D-glucosyltransferase. This enzyme is also called uridine diphosphoglucose-sarsasapogenin glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Scopoletin%20glucosyltransferase | In enzymology, a scopoletin glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + scopoletin UDP + scopolin
Thus, the two substrates of this enzyme are UDP-glucose and scopoletin, whereas its two products are UDP and scopolin.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:scopoletin O-beta-D-glucosyltransferase. Other names in common use include uridine diphosphoglucose-scopoletin glucosyltransferase, UDP-glucose:scopoletin glucosyltransferase, and SGTase. This enzyme participates in phenylpropanoid biosynthesis.
References
EC 2.4.1
Enzymes of unknown structure
Coumarins metabolism |
https://en.wikipedia.org/wiki/Part-based%20models | Part-based models refers to a broad class of detection algorithms used on images, in which various parts of the image are used separately in order to determine if and where an object of interest exists. Amongst these methods a very popular one is the constellation model which refers to those schemes which seek to detect a small number of features and their relative positions to then determine whether or not the object of interest is present.
These models build on the original idea of Fischler and Elschlager of using the relative position of a few template matches and evolve in complexity in the work of Perona and others. These models will be covered in the constellation models section. To get a better idea of what is meant by constellation model an example may be more illustrative. Say we are trying to detect faces. A constellation model would use smaller part detectors, for instance mouth, nose and eye detectors and make a judgment about whether an image has a face based on the relative positions in which the components fire.
Non-constellation models
Many overlapping ideas are included under the title part-based models even after having excluded those models of the constellation variety. The uniting thread is the use of small parts to build up to an algorithm that can detect/recognize an item (face, car, etc.)
Early efforts, such as those by Yuille, Hallinan and Cohen sought to detect facial features and fit deformable templates to them. These templates were math |
https://en.wikipedia.org/wiki/Carboxylesterase%20type%20B | Carboxylesterase, type B is a family of evolutionarily related proteins that belongs to the superfamily of proteins with the Alpha/beta hydrolase fold.
Higher eukaryotes have many distinct esterases. The different types include those that act on carboxylic esters (). Carboxyl-esterases have been classified into three categories (A, B and C) on the basis of differential patterns of inhibition by organophosphates. The sequence of a number of type-B carboxylesterases indicates that the majority are evolutionarily related. As is the case for lipases and serine proteases, the catalytic apparatus of esterases involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.
Subfamilies
Neuroligin
Cholinesterase
Examples
Human genes that encode proteins containing the carboxylesterase domain include:
ACHE
ARACHE
BCHE
CEL
CES1
CES2
CES3
CES4
CES7
CES8
NLGN1
NLGN2
NLGN3
NLGN4X
NLGN4Y
TG
See also
Carboxylesterase
References
External links
Carboxylesterases type-B in PROSITE
Protein families
Peripheral membrane proteins |
https://en.wikipedia.org/wiki/ATP%20synthase%20subunit%20C | ATPase, subunit C of Fo/Vo complex is the main transmembrane subunit of V-type, A-type and F-type ATP synthases. Subunit C (also called subunit 9, or proteolipid in F-ATPases, or the 16 kDa proteolipid in V-ATPases) was found in the Fo or Vo complex of F- and V-ATPases, respectively. The subunits form an oligomeric c ring that make up the Fo/Vo/Ao rotor, where the actual number of subunits vary greatly among specific enzymes.
ATPases (or ATP synthases) are membrane-bound enzyme complexes/ion transporters that combine ATP synthesis and/or hydrolysis with the transport of protons across a membrane. ATPases can harness the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. Some ATPases work in reverse,
using the energy from the hydrolysis of ATP to create a proton gradient. There are different types of ATPases, which can
differ in function (ATP synthesis and/or hydrolysis), structure (F-, V- and A-ATPases contain rotary motors) and in the type of ions they transport.
The F-ATPases (or F1Fo ATPases) and V-ATPases (or V1Vo ATPases) are each composed of two linked complexes: the F1 or V1 complex contains the catalytic core that synthesizes/hydrolyses ATP, and the Fo or Vo complex that forms the membrane-spanning pore. The F- and V-ATPases all contain rotary motors, one that drives proton translocation across the membrane and one that drives ATP synthesis/hydrolysis.
In F-ATPases, the flux of pro |
https://en.wikipedia.org/wiki/Sinapate%201-glucosyltransferase | In enzymology, a sinapate 1-glucosyltransferase () is an enzyme that catalyzes the chemical reaction:
UDP-glucose + sinapate UDP + 1-sinapoyl-D-glucose
Thus, the two substrates of this enzyme are UDP-glucose and sinapate, whereas its two products are UDP and 1-sinapoyl-D-glucose.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:sinapate D-glucosyltransferase. Other names in common use include uridine diphosphoglucose-sinapate glucosyltransferase, UDP-glucose:sinapic acid glucosyltransferase, uridine 5'-diphosphoglucose-hydroxycinnamic acid, and acylglucosyltransferase. This enzyme participates in phenylpropanoid biosynthesis.
References
EC 2.4.1
Enzymes of unknown structure
Hydroxycinnamic acids metabolism |
https://en.wikipedia.org/wiki/%28Skp1-protein%29-hydroxyproline%20N-acetylglucosaminyltransferase | In enzymology, a [Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-N-acetylglucosamine + [Skp-protein]-hydroxyproline UDP + [Skp-protein]-O-(N-acetyl-D-glucosaminyl)hydroxyproline
Thus, the two substrates of this enzyme are UDP-N-acetylglucosamine and Skp1-protein-hydroxyproline, whereas its two products are UDP and Skp1-protein-O-(N-acetyl-D-glucosaminyl)hydroxyproline.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:[Skp1-protein]-hydroxyproline N-acetyl-D-glucosaminyl-transferase. Other names in common use include Skp1-HyPro GlcNAc-transferase, UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide, GlcNAc-transferase, UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase, and UDP-GlcNAc:hydroxyproline polypeptide GlcNAc-transferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/S-methyl-5%27-thioadenosine%20phosphorylase | In enzymology, a S-methyl-5'-thioadenosine phosphorylase () is an enzyme that catalyzes the chemical reaction
S-methyl-5'-thioadenosine + phosphate adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
Thus, the two substrates of this enzyme are S-methyl-5'-thioadenosine and phosphate, whereas its two products are adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate.
This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is S-methyl-5-thioadenosine:phosphate S-methyl-5-thio-alpha-D-ribosyl-transferase. Other names in common use include 5'-methylthioadenosine nucleosidase, 5'-deoxy-5'-methylthioadenosine phosphorylase, MTA phosphorylase, MeSAdo phosphorylase, MeSAdo/Ado phosphorylase, methylthioadenosine phosphorylase, methylthioadenosine nucleoside phosphorylase, 5'-methylthioadenosine:phosphate methylthio-D-ribosyl-transferase, and S-methyl-5-thioadenosine phosphorylase. This enzyme participates in methionine metabolism.
Structural studies
As of late 2007, 20 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , and .
References
EC 2.4.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Aquapheresis | Aquapheresis is a medical technology designed to remove excess salt and water from the body safely, predictably, and effectively from patients with a condition called fluid overload. It removes the excess salt and water and helps to restore a patient's proper fluid balance, which is called euvolemia.
Uses
Aquapheresis is used to treat a condition called fluid overload or hypervolemia. Fluid overload can be caused by many reasons, including heart failure, liver cirrhosis, hypertension and certain kidney diseases. Fluid overload can also be experienced after certain surgical operations. Congestive heart failure is the most common reason for fluid overload.
How it works
Blood containing excess salt and water is withdrawn from a patient using peripheral or central venous catheters and passed through a special filter. Using a form of ultrafiltration, the filter separates the excess salt and water from the blood and the blood is returned to the patient while the fluid is collected in a bag for later disposal.
Anti-coagulation therapy is often used with aquapheresis to prevent blood from clotting the ultrafiltration filter. Patients must discontinue any anticoagulant medications before starting aquapheresis so they can be placed on intravenous heparin therapy. Once the Heparin therapy is initiated, the patient's PTT (partial thromboplastin time) levels will be monitored closely per hospital protocol to prevent excessive anti-coagulation. If a patient is allergic to Heparin or |
https://en.wikipedia.org/wiki/Sn-glycerol-3-phosphate%201-galactosyltransferase | In enzymology, a sn-glycerol-3-phosphate 1-galactosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-galactose + sn-glycerol 3-phosphate UDP + alpha-D-galactosyl-(1,1')-sn-glycerol 3-phosphate
Thus, the two substrates of this enzyme are UDP-galactose and sn-glycerol 3-phosphate, whereas its two products are UDP and alpha-D-galactosyl-(1,1')-sn-glycerol 3-phosphate.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:sn-glycerol-3-phosphate 1-alpha-D-galactosyltransferase. Other names in common use include isofloridoside-phosphate synthase, UDP-Gal:sn-glycero-3-phosphoric acid 1-alpha-galactosyl-transferase, UDPgalactose:sn-glycerol-3-phosphate alpha-D-galactosyltransferase, uridine diphosphogalactose-glycerol phosphate galactosyltransferase, and glycerol 3-phosphate 1alpha-galactosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sn-glycerol-3-phosphate%202-alpha-galactosyltransferase | In enzymology, a sn-glycerol-3-phosphate 2-alpha-galactosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-galactose + sn-glycerol 3-phosphate UDP + 2-(alpha-D-galactosyl)-sn-glycerol 3-phosphate
Thus, the two substrates of this enzyme are UDP-galactose and sn-glycerol 3-phosphate, whereas its two products are UDP and 2-(alpha-D-galactosyl)-sn-glycerol 3-phosphate.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:sn-glycerol-3-phosphate 2-alpha-D-galactosyltransferase. Other names in common use include floridoside-phosphate synthase, UDP-galactose:sn-glycerol-3-phosphate-2-D-galactosyl transferase, FPS, UDP-galactose, sn-3-glycerol phosphate:1->2' galactosyltransferase, floridoside phosphate synthetase, and floridoside phosphate synthase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sphingosine%20beta-galactosyltransferase | In enzymology, a sphingosine beta-galactosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-galactose + sphingosine UDP + psychosine
Thus, the two substrates of this enzyme are UDP-galactose and sphingosine, whereas its two products are UDP and psychosine.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:sphingosine 1-beta-galactosyltransferase. Other names in common use include psychosine-UDP galactosyltransferase, galactosyl-sphingosine transferase, psychosine-uridine diphosphate galactosyltransferase, UDP-galactose:sphingosine O-galactosyl transferase, uridine diphosphogalactose-sphingosine beta-galactosyltransferase, and UDP-galactose:sphingosine 1-beta-galactotransferase. This enzyme participates in sphingolipid metabolism.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Starch%20synthase | In enzymology, a starch synthase () is an enzyme that catalyzes the chemical reaction
ADP-glucose + (1,4-alpha-D-glucosyl)n ADP + (1,4-alpha-D-glucosyl)n+1
Thus, the two substrates of this enzyme are ADP-glucose and a chain of D-glucose residues joined by 1,4-alpha-glycosidic bonds, whereas its two products are ADP and an elongated chain of glucose residues. Plants use these enzymes in the biosynthesis of starch.
This enzyme belongs to the family of hexosyltransferases, specifically the glycosyltransferases. The systematic name of this enzyme class is ADP-glucose:1,4-alpha-D-glucan 4-alpha-D-glucosyltransferase. Other names in common use include ADP-glucose-starch glucosyltransferase, adenosine diphosphate glucose-starch glucosyltransferase, adenosine diphosphoglucose-starch glucosyltransferase, ADP-glucose starch synthase, ADP-glucose synthase, ADP-glucose transglucosylase, ADP-glucose-starch glucosyltransferase, ADPG starch synthetase, and ADPG-starch glucosyltransferase
Five isoforms seems to be present. GBSS which is linked to amylose synthesis. The others are SS1, SS2, SS3 and SS4. These have different roles in amylopectin synthesis. New work implies that SS4 is important for granule initiation. (Szydlowski et al., 2011)
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
Whelan, W.J. and Schultz, J. (Eds.), Miami Winter Symposia, vol. 1, North Holland, Utrecht, 19 |
https://en.wikipedia.org/wiki/Steroid%20N-acetylglucosaminyltransferase | In enzymology, a steroid N-acetylglucosaminyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-N-acetyl-D-glucosamine + estradiol-17alpha 3-D-glucuronoside UDP + 17alpha-(N-acetyl-D-glucosaminyl)-estradiol 3-D-glucuronoside
Thus, the two substrates of this enzyme are UDP-N-acetyl-D-glucosamine and estradiol-17alpha 3-D-glucuronoside, whereas its two products are UDP and 17alpha-(N-acetyl-D-glucosaminyl)-estradiol 3-D-glucuronoside.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:estradiol-17alpha-3-D-glucuronoside 17alpha-N-acetylglucosaminyltransferase. Other names in common use include hydroxy steroid acetylglucosaminyltransferase, steroid acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-steroid, and acetylglucosaminyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sterol%203beta-glucosyltransferase | In enzymology, a sterol 3beta-glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + a sterol UDP + a sterol 3-beta-D-glucoside
Thus, the two substrates of this enzyme are UDP-glucose and sterol, whereas its two products are UDP and sterol 3-beta-D-glucoside.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:sterol 3-O-beta-D-glucosyltransferase. Other names in common use include UDPG:sterol glucosyltransferase, UDP-glucose-sterol beta-glucosyltransferase, sterol:UDPG glucosyltransferase, UDPG-SGTase, uridine diphosphoglucose-poriferasterol glucosyltransferase, uridine diphosphoglucose-sterol glucosyltransferase, sterol glucosyltransferase, sterol-beta-D-glucosyltransferase, and UDP-glucose-sterol glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sucrose%E2%80%941%2C6-alpha-glucan%203%286%29-alpha-glucosyltransferase | In enzymology, a sucrose-1,6-alpha-glucan 3(6)-alpha-glucosyltransferase () is an enzyme that catalyzes the chemical reaction
sucrose + (1,6-alpha-D-glucosyl)n D-fructose + (1,6-alpha-D-glucosyl)n+1
Thus, the two substrates of this enzyme are sucrose and (1,6-alpha-D-glucosyl)n, whereas its two products are D-fructose and (1,6-alpha-D-glucosyl)n+1.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is sucrose:1,6-alpha-D-glucan 3(6)-alpha-D-glucosyltransferase. Other names in common use include water-soluble-glucan synthase, GTF-S, sucrose-1,6-alpha-glucan 3(6)-alpha-glucosyltransferase, sucrose:1,6-alpha-D-glucan 3-alpha- and 6-alpha-glucosyltransferase, sucrose:1,6-, 1,3-alpha-D-glucan 3-alpha- and, and 6-alpha-D-glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sucrose%206F-alpha-galactosyltransferase | In enzymology, a sucrose 6F-alpha-galactosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-galactose + sucrose UDP + 6F-alpha-D-galactosylsucrose
Thus, the two substrates of this enzyme are UDP-galactose and sucrose, whereas its two products are UDP and 6F-alpha-D-galactosylsucrose.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:sucrose 6F-alpha-D-galactosyltransferase. Other names in common use include uridine diphosphogalactose-sucrose 6F-alpha-galactosyltransferase, UDPgalactose:sucrose 6fru-alpha-galactosyltransferase, and sucrose 6F-alpha-galactotransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sucrose-phosphate%20synthase | Sucrose-phosphate synthase (SPS) is a plant enzyme involved in sucrose biosynthesis. Specifically, this enzyme catalyzes the transfer of a hexosyl group from uridine diphosphate glucose (UDP-glucose) to D-fructose 6-phosphate to form UDP and D-sucrose-6-phosphate. This reversible step acts as the key regulatory control point in sucrose biosynthesis, and is an excellent example of various key enzyme regulation strategies such as allosteric control and reversible phosphorylation.
This enzyme participates in starch and sucrose metabolism.
Nomenclature
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:D-fructose 6-phosphate 2-alpha-D-glucosyltransferase. Other names in common use include UDP-glucose-fructose-phosphate glucosyltransferase, sucrosephosphate-UDP glucosyltransferase, UDP-glucose-fructose-phosphate glucosyltransferase, SPS, uridine diphosphoglucose-fructose phosphate glucosyltransferase, sucrose 6-phosphate synthase, sucrose phosphate synthetase, and sucrose phosphate-uridine diphosphate glucosyltransferase.
Structure
X-ray diffraction studies have revealed that the structure of Halothermothrix orenii SPS belongs to the GT-B fold family. Like other GT-B proteins, SPS contains two Rossmann fold domains that are named the A domain and the B domain. Generally, the structure of these domains are somewhat similar, as both contain central beta sheets that are surro |
https://en.wikipedia.org/wiki/Sucrose%3Asucrose%20fructosyltransferase | In enzymology, a sucrose:sucrose fructosyltransferase () is an enzyme that catalyzes the chemical reaction
2 sucrose D-glucose + beta-D-fructofuranosyl-(2->1)-beta-D-fructofuranosyl + alpha-D-glucopyranoside
Hence, this enzyme has one substrate, sucrose, but 3 products: D-glucose, [[beta-D-fructofuranosyl-(2->1)-beta-D-fructofuranosyl]], and alpha-D-glucopyranoside.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is sucrose:sucrose 1'-beta-D-fructosyltransferase. Other names in common use include SST, sucrose:sucrose 1-fructosyltransferase, sucrose-sucrose 1-fructosyltransferase, sucrose 1F-fructosyltransferase, and sucrose:sucrose 1F-beta-D-fructosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sucrose%20synthase | In enzymology, a sucrose synthase () is an enzyme that catalyzes the chemical reaction
NDP-glucose + D-fructose NDP + sucrose
Thus, the two substrates of this enzyme are NDP-glucose and D-fructose, whereas its two products are NDP and sucrose.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is NDP-glucose:D-fructose 2-alpha-D-glucosyltransferase. Other names in common use include UDPglucose-fructose glucosyltransferase, sucrose synthetase, sucrose-UDP glucosyltransferase, sucrose-uridine diphosphate glucosyltransferase, and uridine diphosphoglucose-fructose glucosyltransferase. This enzyme participates in starch and sucrose metabolism.
References
Literature
EC 2.4.1 |
https://en.wikipedia.org/wiki/Thymidine%20phosphorylase | Thymidine phosphorylase () is an enzyme that is encoded by the TYMP gene and catalyzes the reaction:
thymidine + phosphate thymine + 2-deoxy-alpha-D-ribose 1-phosphate
Thymidine phosphorylase is involved in purine metabolism, pyrimidine metabolism, and other metabolic pathways. Variations in thymidine phosphorylase and the TYMP gene that encode it are associated with mitochondrial neurogastrointestinal encephalopathy (MNGIE) syndrome and bladder cancer.
Nomenclature
This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is thymidine:phosphate deoxy-alpha-D-ribosyltransferase. Other names in common use include pyrimidine phosphorylase, thymidine-orthophosphate deoxyribosyltransferase, animal growth regulators, blood platelet-derived endothelial cell, growth factors, blood platelet-derived endothelial cell growth factor, deoxythymidine phosphorylase, gliostatins, pyrimidine deoxynucleoside phosphorylase, and thymidine:phosphate deoxy-D-ribosyltransferase.
Mechanism
Thymidine phosphorylase catalyzes the reversible phosphorylation of thymidine, deoxyuridine, and their analogs (except deoxycytidine) to their respective bases (thymine/uracil) and 2-deoxyribose 1-phosphate. The enzyme follows a sequential mechanism, where phosphate binds before thymidine (or deoxyuridine, etc.) and 2-deoxyribose 1-phosphate leaves after the nitrogenous base. The thymidine is bound in a high-energy conforma |
https://en.wikipedia.org/wiki/Trans-zeatin%20O-beta-D-glucosyltransferase | In enzymology, a trans-zeatin O-beta-D-glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + trans-zeatin UDP + O-beta-D-glucosyl-trans-zeatin
Thus, the two substrates of this enzyme are UDP-glucose and trans-zeatin, whereas its two products are UDP and O-beta-D-glucosyl-trans-zeatin.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:trans-zeatin O-beta-D-glucosyltransferase. Other names in common use include zeatin O-beta-D-glucosyltransferase, uridine diphosphoglucose-zeatin O-glucosyltransferase, and zeatin O-glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Trehalose%206-phosphate%20phosphorylase | In enzymology, a trehalose 6-phosphate phosphorylase () is an enzyme that catalyzes the chemical reaction
alpha,alpha-trehalose 6-phosphate + phosphate glucose 6-phosphate + beta-D-glucose 1-phosphate
The two substrates of this enzyme are alpha,alpha'-trehalose 6-phosphate and phosphate. Its two products are glucose 6-phosphate and beta-D-glucose 1-phosphate.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is alpha,alpha-trehalose 6-phosphate:phosphate beta-D-glucosyltransferase. This enzyme is also called trehalose 6-phosphate:phosphate beta-D-glucosyltransferase.
References
External links
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/TRNA-queuosine%20beta-mannosyltransferase | In enzymology, a tRNA-queuosine beta-mannosyltransferase () is an enzyme that catalyzes the chemical reaction
GDP-mannose + tRNAAsp-queuosine GDP + tRNAAsp-O-5"-beta-D-mannosylqueuosine
Thus, the two substrates of this enzyme are GDP-mannose and tRNAAsp-queuosine, whereas its two products are GDP and tRNAAsp-O-5''-beta-D-mannosylqueuosine.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is GDP-mannose:tRNAAsp-queuosine O-5"-beta-D-mannosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Undecaprenyldiphospho-muramoylpentapeptide%20beta-N-acetylglucosaminyltransferase | In enzymology, an undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol UDP + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
The 2 substrates of this enzyme are UDP-N-acetylglucosamine and Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol, whereas its 2 products are UDP and Lipid II.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:N-acetyl-alpha-D-muramyl(oyl-L-Ala-gamma- D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol beta-1,4-N-acetylglucosaminlytransferase. Another name in common use is MurG transferase. This enzyme participates in peptidoglycan biosynthesis.
Variant reactions producing modified cell walls include (not muturally exclusive):
Replacement of lysine residue with meso-diaminopimelate combined with adjacent residues through its L-centre, as it is in Gram-negative and some Gram-positive organisms.
Use of mono-trans,octa-cis-decaprenyl instead of the conventional di-trans,octa-cis-undecaprenol moiety, as found in Mycobacterium.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Undecaprenyl-phosphate%20mannosyltransferase | In enzymology, an undecaprenyl-phosphate mannosyltransferase () is an enzyme that catalyzes the chemical reaction
GDP-mannose + undecaprenyl phosphate GDP + D-mannosyl-1-phosphoundecaprenol
Thus, the two substrates of this enzyme are GDP-mannose and undecaprenyl phosphate, whereas its two products are GDP and D-mannosyl-1-phosphoundecaprenol.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is GDP-mannose:undecaprenyl-phosphate D-mannosyltransferase. Other names in common use include guanosine diphosphomannose-undecaprenyl phosphate, mannosyltransferase, GDP mannose-undecaprenyl phosphate mannosyltransferase, and GDP-D-mannose:lipid phosphate transmannosylase. It employs one cofactor, phosphatidylglycerol. Sources of this enzyme includes Micrococcus luteus, Phaseolus aureus, Mycobacterium smegmatis and cotton fibers.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Urate-ribonucleotide%20phosphorylase | In enzymology, an urate-ribonucleotide phosphorylase () is an enzyme that catalyzes the chemical reaction
urate D-ribonucleotide + phosphate urate + alpha-D-ribose 1-phosphate
Thus, the two substrates of this enzyme are urate D-ribonucleotide and phosphate, whereas its two products are urate and alpha-D-ribose 1-phosphate.
This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is urate-ribonucleotide:phosphate alpha-D-ribosyltransferase. Other names in common use include UAR phosphorylase, and urate-ribonucleotide:phosphate D-ribosyltransferase. This enzyme participates in purine metabolism.
References
EC 2.4.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Uridine%20phosphorylase | In enzymology, an uridine phosphorylase () is an enzyme that catalyzes the chemical reaction
uridine + phosphate uracil + alpha-D-ribose 1-phosphate
Thus, the two substrates of this enzyme are uridine and phosphate, whereas its two products are uracil and alpha-D-ribose 1-phosphate.
This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is uridine:phosphate alpha-D-ribosyltransferase. Other names in common use include pyrimidine phosphorylase, UrdPase, UPH, and UPase. This enzyme participates in pyrimidine metabolism.
Structural studies
As of late 2007, 27 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , , , , , , , , and .
References
EC 2.4.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Vitexin%20beta-glucosyltransferase | In enzymology, a vitexin beta-glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + vitexin UDP + vitexin 2"-O-beta-D-glucoside
Thus, the two substrates of this enzyme are UDP-glucose and vitexin, whereas its two products are UDP and vitexin 2"-O-beta-D-glucoside.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:vitexin 2. This enzyme is also called uridine diphosphoglucose-vitexin 2"-glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Vomilenine%20glucosyltransferase | In enzymology, a vomilenine glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + vomilenine UDP + raucaffricine
Thus, the two substrates of this enzyme are UDP-glucose and vomilenine, whereas its two products are UDP and raucaffricine.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:vomilenine 21-O-beta-D-glucosyltransferase. This enzyme is also called UDPG:vomilenine 21-beta-D-glucosyltransferase. This enzyme participates in indole and ipecac alkaloid biosynthesis.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Bone%20remodeling | In osteology, bone remodeling or bone metabolism is a lifelong process where mature bone tissue is removed from the skeleton (a process called bone resorption) and new bone tissue is formed (a process called ossification or new bone formation). These processes also control the reshaping or replacement of bone following injuries like fractures but also micro-damage, which occurs during normal activity. Remodeling responds also to functional demands of the mechanical loading.
In the first year of life, almost 100% of the skeleton is replaced. In adults, remodeling proceeds at about 10% per year.
An imbalance in the regulation of bone remodeling's two sub-processes, bone resorption and bone formation, results in many metabolic bone diseases, such as osteoporosis.
Physiology
Bone homeostasis involves multiple but coordinated cellular and molecular events. Two main types of cells are responsible for bone metabolism: osteoblasts (which secrete new bone), and osteoclasts (which break bone down). The structure of bones as well as adequate supply of calcium requires close cooperation between these two cell types and other cell populations present at the bone remodeling sites (e.g. immune cells). Bone metabolism relies on complex signaling pathways and control mechanisms to achieve proper rates of growth and differentiation. These controls include the action of several hormones, including parathyroid hormone (PTH), vitamin D, growth hormone, steroids, and calcitonin, as well as sev |
https://en.wikipedia.org/wiki/Xanthine%20phosphoribosyltransferase | In enzymology, a xanthine phosphoribosyltransferase () is an enzyme that catalyzes the chemical reaction
XMP + diphosphate 5-phospho-alpha-D-ribose 1-diphosphate + xanthine
Thus, the two substrates of this enzyme are XMP and diphosphate, whereas its two products are 5-phospho-alpha-D-ribose 1-diphosphate and xanthine.
This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is XMP:diphosphate 5-phospho-alpha-D-ribosyltransferase. Other names in common use include Xan phosphoribosyltransferase, xanthosine 5'-phosphate pyrophosphorylase, xanthylate pyrophosphorylase, xanthylic pyrophosphorylase, XMP pyrophosphorylase, 5-phospho-alpha-D-ribose-1-diphosphate:xanthine, phospho-D-ribosyltransferase, 9-(5-phospho-beta-D-ribosyl)xanthine:diphosphate, and 5-phospho-alpha-D-ribosyltransferase. This enzyme participates in purine metabolism.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 2.4.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Xylosylprotein%204-beta-galactosyltransferase | In enzymology, a xylosylprotein 4-beta-galactosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-galactose + O-beta-D-xylosylprotein UDP + 4-beta-D-galactosyl-O-beta-D-xylosylprotein
Thus, the two substrates of this enzyme are UDP-galactose and O-beta-D-xylosylprotein, whereas its two products are UDP and 4-beta-D-galactosyl-O-beta-D-xylosylprotein.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:O-beta-D-xylosylprotein 4-beta-D-galactosyltransferase. Other names in common use include UDP-D-galactose:D-xylose galactosyltransferase, UDP-D-galactose:xylose galactosyltransferase, galactosyltransferase I, and uridine diphosphogalactose-xylose galactosyltransferase. This enzyme participates in chondroitin sulfate biosynthesis and glycan structures - biosynthesis 1. It employs one cofactor, manganese.
References
EC 2.4.1
Manganese enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Zeatin%20O-beta-D-xylosyltransferase | In enzymology, a zeatin O-beta-D-xylosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-D-xylose + zeatin UDP + O-beta-D-xylosylzeatin
Thus, the two substrates of this enzyme are UDP-D-xylose and zeatin, whereas its two products are UDP and O-beta-D-xylosylzeatin.
This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is UDP-D-xylose:zeatin O-beta-D-xylosyltransferase. Other names in common use include uridine diphosphoxylose-zeatin xylosyltransferase, and zeatin O-xylosyltransferase.
References
EC 2.4.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Harris%20affine%20region%20detector | In the fields of computer vision and image analysis, the Harris affine region detector belongs to the category of feature detection. Feature detection is a preprocessing step of several algorithms that rely on identifying characteristic points or interest points so to make correspondences between images, recognize textures, categorize objects or build panoramas.
Overview
The Harris affine detector can identify similar regions between images that are related through affine transformations and have different illuminations. These affine-invariant detectors should be capable of identifying similar regions in images taken from different viewpoints that are related by a simple geometric transformation: scaling, rotation and shearing. These detected regions have been called both invariant and covariant. On one hand, the regions are detected invariant of the image transformation but the regions covariantly change with image transformation. Do not dwell too much on these two naming conventions; the important thing to understand is that the design of these interest points will make them compatible across images taken from several viewpoints. Other detectors that are affine-invariant include Hessian affine region detector, Maximally stable extremal regions, Kadir–Brady saliency detector, edge-based regions (EBR) and intensity-extrema-based regions (IBR).
Mikolajczyk and Schmid (2002) first described the Harris affine detector as it is used today in An Affine Invariant Interest Point |
https://en.wikipedia.org/wiki/Tracer%20use%20in%20the%20oil%20industry | Tracers are used in the oil industry in order to qualitatively or quantitatively gauge how fluid flows through the reservoir, as well as being a useful tool for estimating residual oil saturation. Tracers can be used in either interwell tests or single well tests. In interwell tests, the tracer is injected at one well along with the carrier fluid (water in a waterflood or gas in a gasflood) and detected at a producing well after some period of time, which can be anything from days to years. In single well tests, the tracer is injected into the formation from a well and then produced out the same well. The delay between a tracer that does not react with the formation (a conservative tracer) and one that does (a partitioning tracer) will give an indication of residual oil saturation, a piece of information that is difficult to acquire by other means.
Tracers can be radioactive or chemical, gas or liquid and have been used extensively in the oil industry and hydrology for decades.
References
Petroleum engineering |
https://en.wikipedia.org/wiki/Replication%20protein%20A | Replication protein A (RPA) is the major protein that binds to single-stranded DNA (ssDNA) in eukaryotic cells. In vitro, RPA shows a much higher affinity for ssDNA than RNA or double-stranded DNA. RPA is required in replication, recombination and repair processes such as nucleotide excision repair and homologous recombination. It also plays roles in responding to damaged DNA.
Structure
RPA is a heterotrimer, composed of the subunits RPA1 (RPA70) (70kDa subunit), RPA2 (RPA32) (32kDa subunit) and RPA3 (RPA14) (14kDa subunit). The three RPA subunits contain six OB-folds (oligonucleotide/oligosaccharide binding),with DNA-binding domains (DBD) designated DBDs A-F, that bind RPA to single-stranded DNA.
DBDs A, B, C and F are located on RPA1, DBD D is located on RPA2, and DBD E is located on RPA3. DBDs C, D, and E make up the trimerization core of the protein with flexible linker regions connecting them all together. Due to these flexible linker regions RPA is considered highly flexible and this supports the dynamic binding that RPA is able to achieve. Because of this dynamic binding, RPA is also capable of different conformations that leads to varied numbers of nucleotides that it can engage.
DBDs A, B, C and D are the sites that are involved in ssDNA binding. Protein-protein interactions between RPA and other proteins happen at the N-terminal of RPA1, specifically DBD F, along with the C-terminal of RPA2. Phosphorylation of RPA takes place at the N-terminus of RPA2.
RP |
https://en.wikipedia.org/wiki/Major%20intrinsic%20proteins | Major intrinsic proteins comprise a large superfamily of transmembrane protein channels that are grouped together on the basis of homology. The MIP superfamily includes three subfamilies: aquaporins, aquaglyceroporins and S-aquaporins.
The aquaporins (AQPs) are water selective.
The aquaglyceroporins are permeable to water, but also to other small uncharged molecules such as glycerol.
The third subfamily, with little conserved amino acid sequences around the NPA boxes, include 'superaquaporins' (S-aquaporins).
The phylogeny of insect MIP family channels has been published.
Families
There are two families that belong to the MIP Superfamily.
1.A.8 - The Major Intrinsic Protein (MIP) Family
1.A.16 - The Formate-Nitrite Transporter (FNT) Family
The Major Intrinsic Protein Family (TC# 1.A.8)
The MIP family is large and diverse, possessing thousands of members that form transmembrane channels. These channel proteins function in transporting water, small carbohydrates (e.g., glycerol), urea, NH3, CO2, H2O2 and ions by energy-independent mechanisms. For example, the glycerol channel, FPS1p of Saccharomyces cerevisiae mediates uptake of arsenite and antimonite. Ion permeability appears to occur through a pathway different than that used for water/glycerol transport and may involve a channel at the 4 subunit interface rather than the channels through the subunits. MIP family members are found ubiquitously in bacteria, archaea and eukaryotes. Phylogenetic clustering of the pro |
https://en.wikipedia.org/wiki/PlayStation%203%20cluster | A PlayStation 3 cluster is a distributed system computer composed primarily of PlayStation 3 video game consoles.
Before and during the console's production lifetime, its powerful IBM Cell CPU attracted interest in using multiple, networked PS3s for affordable high-performance computing.
Deployments
PlayStation 3 clusters have had different configurations. A distributed computing system utilizing PlayStation 3 consoles does not need to meet the strict definition of a computer cluster.
The National Center for Supercomputing Applications had already built a cluster based on the PlayStation 2. Terra Soft Solutions has a version of Yellow Dog Linux for the PlayStation 3, and sells PS3s with it pre-installed, in single units and in 8 and 32 node clusters. RapidMind developed a stream programming package for the PS3.
On January 3, 2007, Dr. Frank Mueller, Associate Professor of Computer Science at North Carolina State University, clustered 8 PS3s. Mueller commented that the 256 MB of system RAM is a limitation for this particular application, and considered attempting to retrofit more RAM. Software includes: Fedora Core 5 Linux ppc64,
MPICH2, OpenMP v2.5, GNU Compiler Collection, and CellSDK 1.1.
In mid-2007, Gaurav Khanna, a professor in the Physics Department of the University of Massachusetts Dartmouth, independently built a message-passing based cluster using 8 PS3s running Fedora Linux. It was built with support from Sony Computer Entertainment as the first PS3 cluster wi |
https://en.wikipedia.org/wiki/Pentatricopeptide%20repeat | The pentatricopeptide repeat (PPR) is a 35-amino acid sequence motif. Pentatricopeptide-repeat-containing proteins are a family of proteins commonly found in the plant kingdom. They are distinguished by the presence of tandem degenerate PPR motifs and by the relative lack of introns in the genes coding for them.
Approximately 450 such proteins have been identified in the Arabidopsis genome, and another 477 in the rice genome. Despite the large size of the protein family, genetic data suggest that there is little or no redundancy of function between the PPR proteins in Arabidopsis.
The purpose of PPR proteins is currently under dispute. It has been shown that a good deal of those in Arabidopsis interact (often essentially) with mitochondria and other organelles and that they are possibly involved in RNA editing. However many trans proteins are required for this editing to occur and research continues to look at which proteins are needed.
The structure of the PPR has been resolved. It folds into a helix-turn-helix structure similar to those found in the tetratricopeptide repeat. Several repeats of the protein forms a ring around a single-strand RNA molecule in a sequence-sensitive way reminiscent of TAL effectors.
Examples
Human genes encoding proteins containing this repeat include:
DENND4A, DENND4B, DENND4C
LRPPRC
PTCD1, PTCD2, PTCD3
MRPS27
References
Amino acid motifs |
https://en.wikipedia.org/wiki/Torovirus | Torovirus is a genus of enveloped, positive-strand RNA viruses in the order Nidovirales and family Tobaniviridae. They primarily infect vertebrates, especially cattle, pigs, and horses. Diseases associated with this genus include gastroenteritis, which commonly presents in mammals. Torovirus is the only genus in the monotypic subfamily Torovirinae. Torovirus is also a monotypic taxon, containing only one subgenus, Renitovirus.
The discovery of the first torovirus can be traced back to 1970s. Equine torovirus (EToV) was accidentally found in the rectal sample from a horse who was experiencing severe diarrhea. The 'Breda' bovine torovirus was later found in 1979 while investigation in a dairy farm in Breda. They had several calves experiencing severe diarrhea for months. In 1984, torovirus-like particles were detected with electron microscope (EM) technique in the human patients with gastroenteritis.
Virology
Structure
Toroviruses (ToV) are single-stranded RNA viruses that have a peplomer-bearing envelope that is often correlated with the enteric infections in cattle and possibly humans. These viruses appear to occur globally, occurrence of ToVs have been reported from countries in various continents like Europe, Americas, New Zealand and South Africa. Torovirus particles typically possess a helical and symmetrical nucleocapsid that is coiled into a hollow cylindrical shape. The diameter is approximately 23 nm with an average length of 104 nm, where every turn cycle is at i |
https://en.wikipedia.org/wiki/Glycoside%20hydrolase%20family%201 | Glycoside hydrolase family 1 is a family of glycoside hydrolases. Glycoside hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families. This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.
Glycoside hydrolase family 1 CAZY GH_1 comprises enzymes with a number of known activities; beta-glucosidase (); beta-galactosidase (); 6-phospho-beta-galactosidase (); 6-phospho-beta-glucosidase (); lactase-phlorizin hydrolase (), lactase (); beta-mannosidase (); myrosinase ().
Subfamilies
6-phospho-beta-galactosidase
Human proteins containing this domain
GBA3; KL; KLB; LCT; LCTL;
External links
GH1 in CAZypedia
References
Peripheral membrane proteins
EC 3.2.1
Glycoside hydrolase families
Protein families |
https://en.wikipedia.org/wiki/SecY%20protein | The SecY protein is the main transmembrane subunit of the bacterial Sec export pathway and of a protein-secreting ATPase complex, also known as a SecYEG translocon. Homologs of the SecYEG complex are found in eukaryotes and in archaea, where the subunit is known as Sec61α.
Secretion of some proteins carrying a signal-peptide across the inner membrane in Gram-negative bacteria occurs via the preprotein translocase pathway. Proteins are produced in the cytoplasm as precursors, and require a chaperone subunit to direct them to the translocase component within the membrane. From there, the mature proteins are either targeted to the outer membrane or remain as periplasmic proteins. The translocase protein subunits are encoded on the bacterial chromosome.
The translocase pathway comprises 7 proteins, including a chaperone protein (SecB), an ATPase (SecA), an integral membrane complex (SecY, SecE, and SecG), and two additional membrane proteins that promote the release of the mature peptide into the periplasm (SecD and SecF). The chaperone protein SecB is a highly acidic homotetrameric protein that exists as a "dimer of dimers" in the bacterial cytoplasm. SecB maintains preproteins in an unfolded state after translation and targets these to the peripheral membrane protein ATPase SecA for secretion.
Cytoplasmic regions 2 and 3, and TM domains 1, 2, 4, 5, 7, and 10 are well conserved: the conserved cytoplasmic regions are believed to interact with cytoplasmic secretion factors, whi |
https://en.wikipedia.org/wiki/Alternating-direction%20implicit%20method | In numerical linear algebra, the alternating-direction implicit (ADI) method is an iterative method used to solve Sylvester matrix equations. It is a popular method for solving the large matrix equations that arise in systems theory and control, and can be formulated to construct solutions in a memory-efficient, factored form. It is also used to numerically solve parabolic and elliptic partial differential equations, and is a classic method used for modeling heat conduction and solving the diffusion equation in two or more dimensions. It is an example of an operator splitting method.
ADI for matrix equations
The method
The ADI method is a two step iteration process that alternately updates the column and row spaces of an approximate solution to . One ADI iteration consists of the following steps:1. Solve for , where 2. Solve for , where .
The numbers are called shift parameters, and convergence depends strongly on the choice of these parameters. To perform iterations of ADI, an initial guess is required, as well as shift parameters, .
When to use ADI
If and , then can be solved directly in using the Bartels-Stewart method. It is therefore only beneficial to use ADI when matrix-vector multiplication and linear solves involving and can be applied cheaply.
The equation has a unique solution if and only if , where is the spectrum of . However, the ADI method performs especially well when and are well-separated, and and are normal matrices. These assumpti |
https://en.wikipedia.org/wiki/Spectrin%20repeat | Spectrin repeats are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin, dystrophin and more recently the plakin family. The spectrin repeat forms a three-helix bundle. These conform to the rules of the heptad repeat. Spectrin repeats give rise to linear proteins. This however may be due to sample bias in which linear and rigid structures are more amenable to crystallization. There are hints however, that some proteins harbouring spectrin repeats may also be flexible. This is most likely due to specifically evolved functional purposes.
Human proteins containing this domain
ACTN1; ACTN2; ACTN3; ACTN4; AKAP6; SYNE3; CATX-15; DMD;
DRP2; DST; KALRN; MACF1; MCF2L; SPTA1; SPTAN1;
SPTB; SPTBN1; SPTBN2; SPTBN4; SPTBN5; SYNE1; SYNE2;
TRIO; UTRN;
References
Further reading
Peripheral membrane proteins
Protein domains |
https://en.wikipedia.org/wiki/Barren%20vegetation | Barren vegetation describes an area of land where plant growth may be sparse, stunted, and/or contain limited biodiversity. Environmental conditions such as toxic or infertile soil, high winds, coastal salt-spray, and climatic conditions are often key factors in poor plant growth and development. Barren vegetation can be categorized depending on the climate, geology, and geographic location of a specific area.
Pine barrens, coastal barrens, and serpentine barrens are some of the more distinct ecoregions for barren vegetation and are the most commonly researched by scientists. Often referred to as "heathlands", barrens can be excellent environments for unique biological diversity and taxonomic compositions.
Serpentine Barrens
Biological diversity
Serpentine barren habitats include grasslands, chaparral, and woodlands as well as some areas that are very sparsely vegetated. Areas of sparse vegetation are often characterized by annual and perennial herbaceous plant species. The flora of the serpentines is recognized globally for its high level of biological diversity which includes over 1600 taxa of plants occurring in serpentine areas of the eastern U.S., with as many as 2000 taxa considered to be endemic to serpentine rich soils.
Geology
Serpentine barrens are distinct due to the serpentine-rich soil produced by the hydration weathering and metamorphic transformation of ultramafic igneous bedrock. Serpentine barrens are often characterized as high-stress environments with l |
https://en.wikipedia.org/wiki/Alec%20Reeves | Alec Harley Reeves (10 March 1902 – 13 October 1971) was an English scientist best known for his invention of pulse-code modulation (PCM). He was awarded 82 patents.
Early life
Alec Reeves was born in Redhill, Surrey in 1902 and was educated at the Reigate Grammar School, followed by a scholarship to the City and Guilds Engineering College in 1918, and then postgraduate studies at Imperial College London in 1921.
Career
Reeves joined the International Western Electric Company in 1923, and was part of a team of engineers responsible for the first commercial transatlantic telephone link. In 1925 Western Electric's European operations were acquired by ITT, and in 1927 Reeves was transferred to ITT's research laboratories in Paris. Whilst in Paris, he was responsible for a number of projects, including: a short-wave radio link between the telephone networks of Spain and South America, the world's first single-sideband radio telephone system, and for developing a multi-channel carrier system for UHF radio telephones. He was also responsible for innovations in the design of automatic frequency control circuits, digital delay lines and condenser microphones.
Pulse Code Modulation
Reeves recognised the potential that pulse-code modulation had for reducing noise when speech is transmitted over long distances. With an analogue signal, every time the signal is amplified, the noise contained in the signal is also amplified and new, additional noise is added. With pulse code modulatio |
https://en.wikipedia.org/wiki/Alpha/beta%20hydrolase%20superfamily | The alpha/beta hydrolase superfamily is a superfamily of hydrolytic enzymes of widely differing phylogenetic origin and catalytic function that share a common fold. The core of each enzyme is an alpha/beta-sheet (rather than a barrel), containing 8 beta strands connected by 6 alpha helices. The enzymes are believed to have diverged from a common ancestor, retaining little obvious sequence similarity, but preserving the arrangement of the catalytic residues. All have a catalytic triad, the elements of which are borne on loops, which are the best-conserved structural features of the fold.
The alpha/beta hydrolase fold includes proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases.
Database
The ESTHER database provides a large collection of information about this superfamily of proteins.
Subfamilies
3-oxoadipate enol-lactonase
Human proteins containing this domain
ABHD10; ABHD11; ABHD12; ABHD12B; ABHD13; ABHD2; ABHD3; ABHD4;
ABHD5; ABHD6; ABHD7; ABHD8; ABHD9; BAT5; BPHL; C20orf135;
EPHX1; EPHX2; FAM108B1; LIPA; LIPF; LIPJ; LIPK; LIPM;
LIPN; LYPLAL1; MEST; MGLL; PPME1; SERHL; SERHL2; SPG21; CES1; CES2; C4orf29
See also
Ecdysteroid-phosphate phosphatase - structure of a steroid phosphate phosphotase
Serine hydrolase - an enzyme family that is composed largely of proteins with alpha-beta hydrolase folds
External links
The ESTHER database
References
Protein domains
Peripheral membrane proteins
Hydrolases
Protein superfamilies |
https://en.wikipedia.org/wiki/Regulator%20of%20G%20protein%20signaling | Regulators of G protein signaling (RGS) are protein structural domains or the proteins that contain these domains, that function to activate the GTPase activity of heterotrimeric G-protein α-subunits.
RGS proteins are multi-functional, GTPase-accelerating proteins that promote GTP hydrolysis by the α-subunit of heterotrimeric G proteins, thereby inactivating the G protein and rapidly switching off G protein-coupled receptor signaling pathways. Upon activation by receptors, G proteins exchange GDP for GTP, are released from the receptor, and dissociate into a free, active GTP-bound α-subunit and βγ-dimer, both of which activate downstream effectors. The response is terminated upon GTP hydrolysis by the α-subunit (), which can then re-bind the βγ-dimer ( ) and the receptor. RGS proteins markedly reduce the lifespan of GTP-bound α-subunits by stabilising the G protein transition state. Whereas receptors stimulate GTP binding, RGS proteins stimulate GTP hydrolysis.
RGS proteins have been conserved in evolution. The first to be identified was Sst2 ("SuperSensiTivity to pheromone") in yeast (Saccharomyces cerevisiae). All RGS proteins contain an RGS-box (or RGS domain), which is required for activity. Some small RGS proteins such as RGS1 and RGS4 are little more than an RGS domain, while others also contain additional domains that confer further functionality.
RGS domains in the G protein-coupled receptor kinases are able to bind to Gq family α-subunits, but do not accelerate th |
https://en.wikipedia.org/wiki/Mark%E2%80%93Houwink%20equation | The Mark–Houwink equation, also known as the Mark–Houwink–Sakurada equation or the Kuhn–Mark–Houwink–Sakurada equation or the Landau–Kuhn–Mark–Houwink–Sakurada equation or the Mark-Chrystian equation gives a relation between intrinsic viscosity and molecular weight :
From this equation the molecular weight of a polymer can be determined from data on the intrinsic viscosity and vice versa.
The values of the Mark–Houwink parameters, and , depend on the particular polymer-solvent system. For solvents, a value of is indicative of a theta solvent. A value of is typical for good solvents. For most flexible polymers, . For semi-flexible polymers, . For polymers with an absolute rigid rod, such as Tobacco mosaic virus, .
It is named after Herman F. Mark and Roelof Houwink.
Applications
In size-exclusion chromatography, such as gel permeation chromatography, the intrinsic viscosity of a polymer is directly related to the elution volume of the polymer. Therefore, by running several monodisperse samples of polymer in a gel permeation chromatograph (GPC), the values of and can be determined graphically using a line of best fit. Then the molecular weight and intrinsic viscosity relationship is defined.
Also, the molecular weights of two different polymers in a particular solvent can be related using the Mark–Houwink equation when the polymer-solvent systems have the same intrinsic viscosity:
Knowing the Mark–Houwink parameters and the molecular weight of one of the polymers al |
https://en.wikipedia.org/wiki/ERC2 | ERC2 may refer to:
ERC2 (gene), a human protein-coding gene
European Referendum Campaign |
https://en.wikipedia.org/wiki/Santa%20Palomba%20transmitter | Santa Palomba transmitter is a facility of RAI, used for medium-wave broadcasting near Santa Palomba at . It works on 846 kHz and 1332 kHz. On the first frequency, it can be easily received throughout Europe at night time.
Santa Palomba transmitter uses three antennas: two free-standing lattice towers, 186 metres and 75 metres tall and an array of three 116-meter-tall guyed mast radiators. The 186-meter-tall main tower, which is a grounded structure equipped with two individually feedable cage antenna systems for effective skywave suppression, is used for broadcasting on 846 kHz, and the mast array is used for broadcasting on 1332 kHz. The 75-meter-tall lattice tower, which is also grounded and equipped with a cage antenna, serves as a backup antenna for both frequencies.
Santa Palomba transmitter, which belongs to the most important transmitters of RAI, got controversial after the power of the transmitter for 846 kHz was increased to 1500 kW.
External links
http://mediasuk.org/archive/palomba.html
Lattice towers
Towers in Italy |
https://en.wikipedia.org/wiki/Pietro%20De%20Camilli | Pietro De Camilli NAS, AAA&S, NAM is an Italian-American biologist and John Klingenstein Professor of Neuroscience and Cell Biology at Yale University School of Medicine. He is also an Investigator at Howard Hughes Medical Institute. De Camilli completed his M.D. degree from the University of Milan in Italy in 1972. He then went to the United States and did his postdoctoral studies at Yale University with Paul Greengard.
De Camilli is known for contributions that has been to demonstrate the crucial role of protein-lipid interactions and phosphoinositide metabolism in the control of membrane traffic at the synapse.
He has received several awards and honors for his work. He was elected to the European Molecular Biology Organization in 1987. In 2001, he was elected to the National Academy of Sciences and to the American Academy of Arts and Sciences. In 1990 he received the together with Reinhard Jahn (at this time at the Max Planck Institute of Psychiatry). In 2019 he was awarded the Ernst Jung Gold Medal for Medicine for lifetime achievement.
References
External links
Personal lab page of Pietro De Camilli
HHMI Bio
PNAS Bio
Year of birth missing (living people)
Living people
21st-century American biologists
University of Milan alumni
Members of the United States National Academy of Sciences
Howard Hughes Medical Investigators
Yale University faculty
Members of the National Academy of Medicine |
https://en.wikipedia.org/wiki/Centrin | Centrins, also known as caltractins, are a family of calcium-binding phosphoproteins found in the centrosome of eukaryotes. Centrins are small calcium binding proteins that are ubiquitous centrosome components. There are about 350 “signature” proteins that are unique to eukaryotic cells but have no significant homology to proteins in archaea and bacteria. They are a type of protein that is essential and present in almost all eukaryotic cells and are found in the centrioles and pericentriolar lattice. Human centrin genes are CETN1, CETN2 and CETN3.
Humans and mice have three centrin genes: Cetn-1, which is typically only expressed in male germ cells, and Cetn-2 and Cetn-3, which are typically only expressed in somatic cells. Centrin-2 is a recombinant GFP-centrin-2 and centriole protein that localizes to centrioles throughout the cell cycle, while centrin-3 seems to stick to the pericentriolar material that surrounds the centrioles.
History
Centrin was first isolated and characterized from the flagellar roots of the green alga Tetraselmis striata in 1984. Jeffrey Salisbury, who discovered centrin in the green algae, and his colleagues used RNA interference (RNAi) to reduce the levels of centrin-2 in human tissue culture cells. The RNAi of centrin-2 from HeLa cells had led to progressive losses in the centrioles and was consistent with full blocks in the centriole replication. He had proved that centrin was involved in centriole duplication in animal cells like seen in his p |
https://en.wikipedia.org/wiki/Payment%20for%20ecosystem%20services | Payments for ecosystem services (PES), also known as payments for environmental services (or benefits), are incentives offered to farmers or landowners in exchange for managing their land to provide some sort of ecological service. They have been defined as "a transparent system for the additional provision of environmental services through conditional payments to voluntary providers". These programmes promote the conservation of natural resources in the marketplace.
Concept overview
Ecosystem services have no standardized definition but might broadly be called "the benefits of nature to households, communities, and economies" or, more simply, "the good things nature does". Twenty-four specific ecosystem services were identified and assessed by the Millennium Ecosystem Assessment, a 2005 UN-sponsored report designed to assess the state of the world's ecosystems. The report defined the broad categories of ecosystem services as food production (in the form of crops, livestock, capture fisheries, aquaculture, and wild foods), fiber (in the form of timber, cotton, hemp, and silk), genetic resources (biochemicals, natural medicines, and pharmaceuticals), fresh water, air quality regulation, climate regulation, water regulation, erosion regulation, water purification and waste treatment, disease regulation, pest regulation, pollination, natural hazard regulation, and cultural services (including spiritual, religious, and aesthetic values, recreation and ecotourism). Notably, how |
https://en.wikipedia.org/wiki/NPR1 | Natriuretic peptide receptor A/guanylate cyclase A (atrionatriuretic peptide receptor A), also known as NPR1, is an atrial natriuretic peptide receptor. In humans it is encoded by the NPR1 gene.
Function
NPR1 is a membrane-bound guanylate cyclase that serves as the receptor for both atrial and brain natriuretic peptides (ANP and BNP, respectively).
It is localized in the kidney where it results in natriuresis upon binding to natriuretic peptides. However, it is found in even greater quantity in the lungs and adipocytes.
See also
Atrial natriuretic peptide receptor
References
Further reading
External links
EC 4.6.1 |
https://en.wikipedia.org/wiki/NPR2 | Natriuretic peptide receptor B/guanylate cyclase B (atrionatriuretic peptide receptor B), also known as NPR2, is an atrial natriuretic peptide receptor. In humans it is encoded by the NPR2 gene.
A mutation of the NPR2 gene can result in disproportionate dwarfism with short limbs.
See also
Atrial natriuretic peptide receptor
Dwarfism
References
Further reading
External links
EC 4.6.1 |
https://en.wikipedia.org/wiki/NPR3 | Natriuretic peptide receptor C/guanylate cyclase C (atrionatriuretic peptide receptor C), also known as NPR3, is an atrial natriuretic peptide receptor. In humans it is encoded by the NPR3 gene.
Function
The family of natriuretic peptides elicit a number of vascular, renal, and endocrine effects that are important in the maintenance of blood pressure and extracellular fluid volume. These effects are mediated by specific binding of the peptides to cell surface receptors in the vasculature, kidney, adrenal, and brain.
See also
Atrial natriuretic peptide receptor
References
Further reading
External links |
https://en.wikipedia.org/wiki/Birkhoff%E2%80%93Grothendieck%20theorem | In mathematics, the Birkhoff–Grothendieck theorem classifies holomorphic vector bundles over the complex projective line. In particular every holomorphic vector bundle over is a direct sum of holomorphic line bundles. The theorem was proved by , and is more or less equivalent to Birkhoff factorization introduced by .
Statement
More precisely, the statement of the theorem is as the following.
Every holomorphic vector bundle on is holomorphically isomorphic to a direct sum of line bundles:
The notation implies each summand is a Serre twist some number of times of the trivial bundle. The representation is unique up to permuting factors.
Generalization
The same result holds in algebraic geometry for algebraic vector bundle over for any field .
It also holds for with one or two orbifold points, and for chains of projective lines meeting along nodes.
Applications
One application of this theorem is it gives a classification of all coherent sheaves on . We have two cases, vector bundles and coherent sheaves supported along a subvariety, so where n is the degree of the fat point at . Since the only subvarieties are points, we have a complete classification of coherent sheaves.
See also
Algebraic geometry of projective spaces
Euler sequence
Splitting principle
K-theory
Jumping line
References
Further reading
External links
Roman Bezrukavnikov. 18.725 Algebraic Geometry (LEC # 24 Birkhoff–Grothendieck, Riemann-Roch, Serre Duality) Fall 2015. Massachusetts Instit |
https://en.wikipedia.org/wiki/SP%20Chemicals | SP Chemicals, a Singapore-based company, is one of the largest ion-membrane chlor-alkali producer and aniline producer in the PRC. It was listed on the Main Board of SGX-ST on 6 August 2003.
Products
SP Chemicals engages in the manufacture and sale of the chemical industry's basic building blocks - caustic soda, chlorine, hydrogen and its related downstream products. Their products are materials widely used in various applications across a diverse range of industries.
Products include: aniline, caustic soda, chlorine, chlorobenzene, nitrochlorobenzene, nitrobenzene, vinyl chloride monomer (VCM). To further drive its growth, SP Chemicals plans to invest approximately RMB1.1 billion in facilities for the production of styrene monomer, an intermediate raw chemical used in making polystyrene plastics, protective coatings, polyesters and resins.
Vietnam Petrochemical Industrial Park
SP Chemicals is planning to build an integrated petrochemical park of 1,300 hectares and a naphtha cracking plant in the Vietnam Petrochemical Industrial Park, with a production capacity of 800,000 tpa of ethylene annum, to supply raw materials to their own facilities in the PRC, and Hoa Tam Petrochemical Park, and, to a lesser extent, for export.
This mammoth project is targeted to be completed within 15 years in 2 development phases:
Phase One – To build a naphtha cracking and utility plant; targeted to be completed in 2014 at an investment of US$1.5 billion.
Phase Two – To promote the Hoa T |
https://en.wikipedia.org/wiki/1-alkenyl-2-acylglycerol%20choline%20phosphotransferase | In enzymology, a 1-alkenyl-2-acylglycerol choline phosphotransferase () is an enzyme that catalyzes the chemical reaction
CDP-choline + 1-alkenyl-2-acylglycerol CMP + plasmenylcholine
Thus, the two substrates of this enzyme are CDP-choline and 1-alkenyl-2-acylglycerol, whereas its two products are CMP and plasmenylcholine.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is CDP-choline:1-alkenyl-2-acylglycerol cholinephosphotransferase. This enzyme is also called CDP-choline-1-alkenyl-2-acyl-glycerol phosphocholinetransferase. This enzyme participates in ether lipid metabolism.
References
EC 2.7.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/1-phosphatidylinositol-3-phosphate%205-kinase | In enzymology, a 1-phosphatidylinositol-3-phosphate 5-kinase () is an enzyme that catalyzes the chemical reaction
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate ⇌ ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
Thus, the two substrates of this enzyme are ATP and 1-phosphatidyl-1D-myo-inositol 3-phosphate, whereas its two products are ADP and 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:1-phosphatidyl-1D-myo-inositol-3-phosphate 5-phosphotransferase. Other names in common use include type III PIP kinase, and phosphatidylinositol 3-phosphate 5-kinase. This enzyme participates in phosphatidylinositol signaling system and regulation of actin cytoskeleton.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/1-phosphatidylinositol%204-kinase | In enzymology, a 1-phosphatidylinositol 4-kinase () is an enzyme that catalyzes the chemical reaction
ATP + 1-phosphatidyl-1D-myo-inositol ADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
Thus, the two substrates of this enzyme are ATP and 1-phosphatidyl-1D-myo-inositol, whereas its two products are ADP and 1-phosphatidyl-1D-myo-inositol 4-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:1-phosphatidyl-1D-myo-inositol 4-phosphotransferase. Other names in common use include phosphatidylinositol kinase (phosphorylating), phosphatidylinositol 4-kinase, phosphatidylinositol kinase, type II phosphatidylinositol kinase, PI kinase, and PI 4-kinase. This enzyme participates in inositol phosphate metabolism and phosphatidylinositol signaling system.
Structural studies
As of late 2007, the structure has only been solved for this enzyme. Part of the enzyme was crystallized with its activating partner frequenin.
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/1-phosphatidylinositol-4-phosphate%205-kinase | In enzymology, 1-phosphatidylinositol-4-phosphate 5-kinase () is an enzyme that catalyzes the chemical reaction
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
Thus, the two substrates of this enzyme are ATP and 1-phosphatidyl-1D-myo-inositol 4-phosphate, whereas its two products are ADP and 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:1-phosphatidyl-1D-myo-inositol-4-phosphate 5-phosphotransferase. Other names in common use include diphosphoinositide kinase, PIP kinase, phosphatidylinositol 4-phosphate kinase, phosphatidylinositol-4-phosphate 5-kinase, and type I PIP kinase. This enzyme participates in 3 metabolic pathways: inositol phosphate metabolism, phosphatidylinositol signaling system, and regulation of the actin cytoskeleton.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/1-phosphatidylinositol-5-phosphate%204-kinase | In enzymology, a 1-phosphatidylinositol-5-phosphate 4-kinase () is an enzyme that catalyzes the chemical reaction
ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
Thus, the two substrates of this enzyme are ATP and 1-phosphatidyl-1D-myo-inositol 5-phosphate, whereas its two products are ADP and 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:1-phosphatidyl-1D-myo-inositol-5-phosphate 4-phosphotransferase. This enzyme is also called type II PIP kinase. This enzyme participates in 3 metabolic pathways: inositol phosphate metabolism, phosphatidylinositol signaling system, and regulation of actin cytoskeleton.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/1-phosphofructokinase | In enzymology, 1-phosphofructokinase () is an enzyme that catalyzes the chemical reaction
ATP + D-fructose 1-phosphate → ADP + D-fructose 1,6-bisphosphate
Thus, the two substrates of this enzyme are ATP and D-fructose 1-phosphate, whereas its two products are ADP and D-fructose 1,6-bisphosphate. The enzyme was first described and characterized in the 1960s.
This enzyme belongs to the phosphofructokinase B (PfkB) or Ribokinase family of sugar kinases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-fructose-phosphate 6-phosphotransferase. Other names in common use include fructose-1-phosphate kinase, 1-phosphofructokinase (phosphorylating), D-fructose-1-phosphate kinase, fructose 1-phosphate kinase, and 1-phosphofructokinase. This enzyme participates in fructose and mannose metabolism. The members of the PfkB/RK family are identified by the presence of three conserved sequence motifs and their enzymatic activity generally shows a dependence on the presence of pentavalent ions.
Structure
As of 2021, two structures have been solved for this class of enzymes, with the PDB accession codes and , both from structural genomics efforts. The protein is a homodimer.
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/%282%2C3-dihydroxybenzoyl%29adenylate%20synthase | In enzymology, a (2,3-dihydroxybenzoyl)adenylate synthase () is an enzyme that catalyzes the chemical reaction ATP + 2,3-dihydroxybenzoate diphosphate + (2,3-dihydroxybenzoyl)adenylate.
Thus, the two substrates of this enzyme are ATP and 2,3-dihydroxybenzoate, whereas its two products are diphosphate and (2,3-dihydroxybenzoyl)adenylate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:2,3-dihydroxybenzoate adenylyltransferase. This enzyme is also called 2,3-dihydroxybenzoate-AMP ligase. This enzyme participates in biosynthesis of siderophore group nonribosomal.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-amino-4-hydroxy-6-hydroxymethyldihydropteridine%20diphosphokinase | In enzymology, a 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase () is an enzyme that catalyzes the chemical reaction
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
Thus, the two substrates of this enzyme are ATP and 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine, whereas its two products are AMP and (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring two phosphorus-containing groups (diphosphotransferases). The systematic name of this enzyme class is ATP:2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine 6'-diphosphotransferase. Other names in common use include 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase, H2-pteridine-CH2OH pyrophosphokinase, 7,8-dihydroxymethylpterin-pyrophosphokinase, HPPK, 7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase, and hydroxymethyldihydropteridine pyrophosphokinase. This enzyme participates in folate biosynthesis.
This enzyme catalyses the first step in a three-step pathway leading to 7,8 dihydrofolate. Bacterial HPPK (gene folK or sulD) is a protein of 160 to 270 amino acids. In the lower eukaryote Pneumocystis carinii, HPPK is the central domain of a multifunctional folate synthesis enzyme (gene fas).
Structural studies
As of late 2007, 23 structures have been solved for this class of enzymes, with PDB ac |
https://en.wikipedia.org/wiki/Perineuronal%20net | Perineuronal nets (PNNs) are specialized extracellular matrix structures responsible for synaptic stabilization in the adult brain. PNNs are found around certain neuron cell bodies and proximal neurites in the central nervous system. PNNs play a critical role in the closure of the childhood critical period, and their digestion can cause restored critical period-like synaptic plasticity in the adult brain. They are largely negatively charged and composed of chondroitin sulfate proteoglycans, molecules that play a key role in development and plasticity during postnatal development and in the adult.
PNNs appear to be mainly present in the cortex, hippocampus, thalamus, brainstem, and the spinal cord. Studies of the rat brain have shown that the cortex contains high numbers of PNNs in the motor and primary sensory areas and relatively fewer in the association and limbic cortices. In the cortex, PNNs are associated mostly with inhibitory interneurons and are thought to be responsible for maintaining the excitatory/inhibitory balance in the adult brain.
History
The existence of PNNs has been inferred by Golgi, Lugaro, Donaggio, Martinotti, Ramón y Cajal and Meyer. However, Ramón y Cajal credits Golgi with the discovery of PNNs because he was the first to draw attention to them and gave the first precise description in 1893. Moreover, Golgi brought interest to the subject due to his opinion that the PNN was not a neuronal structure but rather a "kind of corset of neurokeratin whi |
https://en.wikipedia.org/wiki/2-C-methyl-D-erythritol%204-phosphate%20cytidylyltransferase | In enzymology, a 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase () is an enzyme that catalyzes the chemical reaction:
2-C-methyl-D-erythritol 4-phosphate + CTP diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
Thus, the two substrates of this enzyme are CTP and 2-C-methyl-D-erythritol 4-phosphate, whereas its two products are diphosphate and 4-diphosphocytidyl-2-C-methylerythritol.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases).
This enzyme participates in isoprenoid biosynthesis and stenvenosim. It catalyzes the third step of the MEP pathway; the formation of CDP-ME (4-diphosphocytidyl-2C-methyl-D-erythritol) from CTP and MEP (2C-methyl-D-erythritol 4-phosphate). The isoprenoid pathway is a well known target for anti-infective drug development.
Nomenclature
The systematic name of this enzyme class is CTP:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase. This enzyme is also called:
MEP cytidylyltransferase
CDP-ME synthetase
It is normally abbreviated IspD. It is also referenced by the open reading frame YgbP.
Structural studies
The crystal structure of the E. coli 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase , & , reported by Richard et al. (2001), was the first one for an enzyme involved in the MEP pathway.
As of February 2010, 13 other structures have been solved for this class of enzymes, with PDB accession codes |
https://en.wikipedia.org/wiki/2-dehydro-3-deoxygalactonokinase | In enzymology, a 2-dehydro-3-deoxygalactonokinase () is an enzyme that catalyzes the chemical reaction
ATP + 2-dehydro-3-deoxy-D-galactonate ADP + 2-dehydro-3-deoxy-D-galactonate 6-phosphate
Thus, the two substrates of this enzyme are ATP and 2-dehydro-3-deoxy-D-galactonate, whereas its two products are ADP and 2-dehydro-3-deoxy-D-galactonate 6-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:2-dehydro-3-deoxy-D-galactonate 6-phosphotransferase. Other names in common use include 2-keto-3-deoxygalactonokinase, 2-keto-3-deoxygalactonate kinase (phosphorylating), and 2-oxo-3-deoxygalactonate kinase. This enzyme participates in galactose metabolism.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-dehydro-3-deoxygluconokinase | In enzymology, a 2-dehydro-3-deoxygluconokinase () is an enzyme that catalyzes the chemical reaction
ATP + 2-dehydro-3-deoxy-D-gluconate ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
Thus, the two substrates of this enzyme are ATP and 2-dehydro-3-deoxy-D-gluconate, whereas its two products are ADP and 6-phospho-2-dehydro-3-deoxy-D-gluconate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:2-dehydro-3-deoxy-D-gluconate 6-phosphotransferase. Other names in common use include 2-keto-3-deoxygluconokinase, 2-keto-3-deoxy-D-gluconic acid kinase, 2-keto-3-deoxygluconokinase (phosphorylating), 2-keto-3-deoxygluconate kinase, and ketodeoxygluconokinase. This enzyme participates in pentose phosphate pathway and pentose and glucuronate interconversions.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/2%27-phosphotransferase | In enzymology, a 2'-phosphotransferase () is an enzyme that catalyzes the chemical reaction
2'-phospho-[ligated tRNA] + NAD+ mature tRNA + ADP-ribose 1,2-phosphate + nicotinamide + H2O
Thus, the two substrates of this enzyme are [[2'-phospho-[ligated tRNA]]] and NAD+, whereas its 4 products are mature tRNA, ADP-ribose 1,2-phosphate, nicotinamide, and H2O.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is 2'-phospho-[ligated tRNA]:NAD+ phosphotransferase. Other names in common use include yeast 2'-phosphotransferase, Tpt1, Tpt1p, and 2'-phospho-tRNA:NAD+ phosphotransferase.
References
EC 2.7.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-deoxy-manno-octulosonate%20cytidylyltransferase | In enzymology, a 3-deoxy-manno-octulosonate cytidylyltransferase () is an enzyme that catalyzes the chemical reaction
CTP + 3-deoxy-D-manno-octulosonate diphosphate + CMP-3-deoxy-D-manno-octulosonate
Thus, the two substrates of this enzyme are CTP and 3-deoxy-D-manno-octulosonate, whereas its two products are diphosphate and CMP-3-deoxy-D-manno-octulosonate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is CTP:3-deoxy-D-manno-octulosonate cytidylyltransferase. Other names in common use include CMP-3-deoxy-D-manno-octulosonate pyrophosphorylase, 2-keto-3-deoxyoctonate cytidylyltransferase, 3-Deoxy-D-manno-octulosonate cytidylyltransferase, CMP-3-deoxy-D-manno-octulosonate synthetase, CMP-KDO synthetase, CTP:CMP-3-deoxy-D-manno-octulosonate cytidylyltransferase, and cytidine monophospho-3-deoxy-D-manno-octulosonate pyrophosphorylase. This enzyme participates in lipopolysaccharide biosynthesis.
Structural studies
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , and .
References
EC 2.7.7
Enzymes of known structure |
https://en.wikipedia.org/wiki/Don%20Shroyer | Donald Gene Shroyer (November 24, 1925 – July 7, 2013) was an American football and baseball coach. He served as the head football coach at Millikin University in Decatur, Illinois from 1956 to 1961 and at Southern Illinois University Carbondale from 1964 to 1965, compiling a career college football coaching record of 32–35–1. Shroyer was also the head baseball coach at Millikin from 1957 to 1959, tallying a mark of 28–15. From 1962 to 1963, he was an assistant coach for St. Louis Cardinals of the National Football League (NFL).
Playing career
As a player at Millikin University, Shroyer was all-conference halfback in football for three consecutive years and all-conference champion in track in the broad jump.
Coaching career
Millikin
After a brief stint in the high school ranks, Shoyer returned to his alma mater, Millikin University, for his first college head coaching job and led the team from 1956 until 1961, accumulating a record of 28–19–1 with an undefeated season in 1961.
Southern Illinois
After Millikin, Shoyer became the tenth head football coach at Southern Illinois University Carbondale and he held that position for two seasons, from 1964 until 1965. His record at Southern Illinois was 4–16.
Head coaching record
College football
References
1925 births
2013 deaths
American football halfbacks
American male long jumpers
Millikin Big Blue baseball coaches
Millikin Big Blue football coaches
Millikin Big Blue football players
Southern Illinois Salukis football |
https://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate%20dehydrogenase%20%28acetyl-transferring%29%20kinase | In enzymology, a [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] () is an enzyme that catalyzes the chemical reaction
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate
Thus, the two substrates of this enzyme are ATP and 3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring), whereas its 3 products are ADP, 3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring), and phosphate.
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is ATP:[3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphotransferase. Other names in common use include kinase, BCK, BCKD kinase, BCODH kinase, branched-chain alpha-ketoacid dehydrogenase kinase, branched-chain 2-oxo acid dehydrogenase kinase, branched-chain keto acid dehydrogenase kinase, branched-chain oxo acid dehydrogenase kinase (phosphorylating), and STK2.
In 2012, it was suggested that mutations in the gene which expresses this enzyme could be the cause of a rare form of autism.
References
Literature
EC 2.7.11
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-phosphoglyceroyl-phosphate%E2%80%94polyphosphate%20phosphotransferase | In enzymology, a 3-phosphoglyceroyl-phosphate—polyphosphate phosphotransferase () is an enzyme that catalyzes the chemical reaction
3-phospho-D-glyceroyl phosphate + (phosphate)n 3-phosphoglycerate + (phosphate)n+1
Thus, the two substrates of this enzyme are 3-phospho-D-glyceroyl phosphate and (phosphate)n, whereas its two products are 3-phosphoglycerate and (phosphate)n+1.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is 3-phospho-D-glyceroyl-phosphate:polyphosphate phosphotransferase. Other names in common use include diphosphoglycerate-polyphosphate phosphotransferase, and 1,3-diphosphoglycerate-polyphosphate phosphotransferase.
References
EC 2.7.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-%28cytidine%205%27-diphospho%29-2-C-methyl-D-erythritol%20kinase | In enzymology, a 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase () is an enzyme that catalyzes the chemical reaction
ATP + 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate ADP + 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate
Thus, the two substrates of this enzyme are ATP and 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME), whereas its two products are ADP and 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-MEP).
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol 2-phosphotransferase. This enzyme is also called CDP-ME kinase, and IspE. This enzyme participates in the MEP pathway (non-mevalonate pathway) of isoprenoid precursor biosynthesis.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/5-dehydro-2-deoxygluconokinase | In enzymology, a 5-dehydro-2-deoxygluconokinase () is an enzyme that catalyzes the chemical reaction
ATP + 5-dehydro-2-deoxy-D-gluconate ADP + 6-phospho-5-dehydro-2-deoxy-D-gluconate
Thus, the two substrates of this enzyme are ATP and 5-dehydro-2-deoxy-D-gluconate, whereas its two products are ADP and 6-phospho-5-dehydro-2-deoxy-D-gluconate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:5-dehydro-2-deoxy-D-gluconate 6-phosphotransferase. Other names in common use include 5-keto-2-deoxygluconokinase, 5-keto-2-deoxyglucono kinase (phosphorylating), and DKH kinase. This enzyme participates in inositol metabolism.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/5-methyldeoxycytidine-5%27-phosphate%20kinase | In enzymology, a 5-methyldeoxycytidine-5'-phosphate kinase () is an enzyme that catalyzes the chemical reaction
ATP + 5-methyldeoxycytidine 5'-phosphate ADP + 5-methyldeoxycytidine diphosphate
Thus, the two substrates of this enzyme are ATP and 5-methyldeoxycytidine 5'-phosphate, whereas its two products are ADP and 5-methyldeoxycytidine diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:5-methyldeoxycytidine-5'-phosphate phosphotransferase.
References
EC 2.7.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acetate%20kinase%20%28diphosphate%29 | In enzymology, an acetate kinase (diphosphate) () is an enzyme that catalyzes the chemical reaction
diphosphate + acetate phosphate + acetyl phosphate
Thus, the two substrates of this enzyme are diphosphate and acetate, whereas its two products are phosphate and acetyl phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is diphosphate:acetate phosphotransferase. This enzyme is also called pyrophosphate-acetate phosphotransferase. This enzyme participates in pyruvate metabolism.
References
EC 2.7.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28acetyl-CoA%20carboxylase%29%20kinase | In enzymology, a [acetyl-CoA carboxylase] kinase () is an enzyme that catalyzes the chemical reaction
ATP + [acetyl-CoA carboxylase] ADP + [acetyl-CoA carboxylase] phosphate
Thus, the two substrates of this enzyme are ATP and acetyl-CoA carboxylase, whereas its two products are ADP and acetyl-CoA carboxylase phosphate.
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is ATP:[acetyl-CoA carboxylase] phosphotransferase. Other names in common use include acetyl coenzyme A carboxylase kinase (phosphorylating), acetyl-CoA carboxylase bound kinase, acetyl-CoA carboxylase kinase, acetyl-CoA carboxylase kinase (cAMP-independent), acetyl-CoA carboxylase kinase 2, acetyl-CoA carboxylase kinase-2, acetyl-CoA carboxylase kinase-3 (AMP-activated), acetyl-coenzyme A carboxylase kinase, ACK2, ACK3, AMPK, I-peptide kinase, and STK5.
References
EC 2.7.11
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acetylglutamate%20kinase | In enzymology, an acetylglutamate kinase () is an enzyme that catalyzes the chemical reaction:
ATP + N-acetyl-L-glutamate ADP + N-acetyl-L-glutamyl 5-phosphate
Thus, the two substrates of this enzyme are ATP and N-acetyl-L-glutamate, whereas its two products are ADP and N-acetyl-L-glutamyl 5-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. This enzyme participates in urea cycle and metabolism of amino groups.
Nomenclature
The systematic name of this enzyme class is ATP:N-acetyl-L-glutamate 5-phosphotransferase. Other names in common use include:
N-acetylglutamate 5-phosphotransferase,
acetylglutamate phosphokinase,
N-acetylglutamate phosphokinase,
N-acetylglutamate kinase, and
N-acetylglutamic 5-phosphotransferase.
Structural studies
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , and .
References
EC 2.7.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Acylglycerol%20kinase | In enzymology, an acylglycerol kinase () is an enzyme that catalyzes the chemical reaction
ATP + acylglycerol ADP + acyl-sn-glycerol 3-phosphate
The two substrates of this enzyme are ATP and acylglycerol, whereas its two products are ADP and acyl-sn-glycerol 3-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:acylglycerol 3-phosphotransferase. Other names in common use include monoacylglycerol kinase, monoacylglycerol kinase (phosphorylating), sn-2-monoacylglycerol kinase, MGK, monoglyceride kinase, and monoglyceride phosphokinase. This enzyme participates in glycerolipid metabolism.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acyl-phosphate%E2%80%94hexose%20phosphotransferase | In enzymology, an acyl-phosphate-hexose phosphotransferase () is an enzyme that catalyzes the chemical reaction
acyl phosphate + D-hexose an acid + D-hexose phosphate
Thus, the two substrates of this enzyme are acyl phosphate and D-hexose, whereas its two products are acid and D-hexose phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is acyl-phosphate:D-hexose phosphotransferase. This enzyme is also called hexose phosphate:hexose phosphotransferase.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Adenosine%20kinase | Adenosine kinase (AdK; EC 2.7.1.20) is an enzyme that catalyzes the transfer of gamma-phosphate from Adenosine triphosphate (ATP) to adenosine (Ado) leading to formation of Adenosine monophosphate (AMP). In addition to its well-studied role in controlling the cellular concentration of Ado, AdK also plays an important role in the maintenance of methylation reactions. All S-adenosylmethionine-dependent transmethylation reactions in cells lead to production of S-adenosylhomocysteine (SAH), which is cleaved by SAH hydrolase into Ado and homocysteine. The failure to efficiently remove these end products (Ado removed by phosphorylation by AdK) can result in buildup of SAH, which is a potent inhibitor of all transmethylation reactions. The disruption of AdK gene (-/-) in mice causes neonatal hepatic steatosis, a fatal condition characterized by rapid microvesicular fat infiltration, leading to early postnatal death. The liver was the main organ affected in these animals and in it the levels of adenine nucleotides were decreased, while those of SAH were elevated. Recently, missense mutations in the AdK gene in humans which result in AdK deficiency have also been shown to cause hypermethioninemia, encephalopathy and abnormal liver function.
Biochemical properties
AdK is a monomeric protein (~ 38-40 kDa), which works via an ordered Bi-Bi reaction mechanism. It belongs to the phosphofructokinase B (PfkB) family of sugar kinases. Other members of this family (also known as the RK famil |
https://en.wikipedia.org/wiki/Adenosylcobinamide%20kinase | In enzymology, an adenosylcobinamide kinase () is an enzyme that catalyzes the chemical reaction
RTP + adenosylcobinamide adenosylcobinamide phosphate + RDP
Thus, the two substrates of this enzyme are RTP and adenosylcobinamide, whereas its two products are adenosylcobinamide phosphate and RDP.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is RTP:adenosylcobinamide phosphotransferase. Other names in common use include CobU, adenosylcobinamide kinase/adenosylcobinamide-phosphate, guanylyltransferase, and AdoCbi kinase/AdoCbi-phosphate guanylyltransferase. This enzyme participates in porphyrin and chlorophyll metabolism.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Adenosylcobinamide-phosphate%20guanylyltransferase | In enzymology, an adenosylcobinamide-phosphate guanylyltransferase () is an enzyme that catalyzes the chemical reaction
GTP + adenosylcobinamide phosphate diphosphate + adenosylcobinamide-GDP
The two substrates of this enzyme are GTP and adenosylcobinamide phosphate; its two products are diphosphate and adenosylcobinamide-GDP.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is GTP:adenosylcobinamide-phosphate guanylyltransferase. Other names in common use include CobU, adenosylcobinamide kinase/adenosylcobinamide-phosphate, guanylyltransferase, and AdoCbi kinase/AdoCbi-phosphate guanylyltransferase. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in bacteria.
See also
Cobalamin biosynthesis
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Adenylylsulfate%E2%80%94ammonia%20adenylyltransferase | In enzymology, an adenylylsulfate-ammonia adenylyltransferase () is an enzyme that catalyzes the chemical reaction adenylyl sulfate + NH3 adenosine 5'-phosphoramidate + sulfate.
Thus, the two substrates of this enzyme are adenylyl sulfate and NH3, whereas its two products are adenosine 5'-phosphoramidate and sulfate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is adenylyl-sulfate:ammonia adenylyltransferase. Other names in common use include APSAT, and adenylylsulfate:ammonia adenylyltransferase.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Adenylyl-sulfate%20kinase | In enzymology, an adenylyl-sulfate kinase () is an enzyme that catalyzes the chemical reaction
ATP + adenylyl sulfate ADP + 3'-phosphoadenylyl sulfate
Thus, the two substrates of this enzyme are ATP and adenylyl sulfate, whereas its two products are ADP and 3'-phosphoadenylyl sulfate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:adenylyl-sulfate 3'-phosphotransferase. Other names in common use include adenylylsulfate kinase (phosphorylating), 5'-phosphoadenosine sulfate kinase, adenosine 5'-phosphosulfate kinase, adenosine phosphosulfate kinase, adenosine phosphosulfokinase, adenosine-5'-phosphosulfate-3'-phosphokinase, and APS kinase. This enzyme participates in 3 metabolic pathways: purine metabolism, selenoamino acid metabolism, and sulfur metabolism.
This enzyme contains an ATP binding P-loop motif.
Structural studies
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , and .
References
Further reading
Protein domains
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/ADP-specific%20glucokinase | In enzymology, an ADP-specific glucokinase () also known as ADP-dependent glucokinase is an enzyme that catalyzes the chemical reaction
ADP + D-glucose AMP + D-glucose 6-phosphate
Thus, the two substrates of this enzyme are ADP and D-glucose, whereas its two products are AMP and D-glucose 6-phosphate.
This enzyme belongs to the family of transferases, to be specific those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor.
In humans, the ADP-dependent glucokinase is encoded by the ADPGK gene.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
External links
Further reading
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/ADP-specific%20phosphofructokinase | In enzymology, an ADP-specific phosphofructokinase () is an enzyme that catalyzes the chemical reaction
ADP + D-fructose 6-phosphate AMP + D-fructose 1,6-bisphosphate
Thus, the two substrates of this enzyme are ADP and D-fructose 6-phosphate, whereas its two products are AMP and D-fructose 1,6-bisphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ADP:D-fructose-6-phosphate 1-phosphotransferase. This enzyme is also called ADP-6-phosphofructokinase, ADP-dependent phosphofructokinase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/ADP%E2%80%94thymidine%20kinase | In enzymology, an ADP—thymidine kinase () is an enzyme that catalyzes the chemical reaction
ADP + thymidine AMP + thymidine 5'-phosphate
Thus, the two substrates of this enzyme are ADP and thymidine, whereas its two products are AMP and thymidine 5'-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ADP:thymidine 5'-phosphotransferase. Other names in common use include ADP:dThd phosphotransferase, and adenosine diphosphate-thymidine phosphotransferase.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Agmatine%20kinase | In enzymology, an agmatine kinase () is an enzyme that catalyzes the chemical reaction
ATP + agmatine ADP + N4-phosphoagmatine
Thus, the two substrates of this enzyme are ATP and agmatine, whereas its two products are ADP and N4-phosphoagmatine.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:agmatine N4-phosphotransferase. Other names in common use include phosphagen phosphokinase, and ATP:agmatine 4-N-phosphotransferase.
References
EC 2.7.3
Enzymes of unknown structure |
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