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https://en.wikipedia.org/wiki/RX%20meter | An RX meter is used to measure the separate resistive and reactive components of reactive parallel Z network.
The two variable frequency oscillators track each other at frequencies 100 kHz apart. The output of a 0.5-250 MHz oscillator, F1, is fed into a bridge. When the impedance network to be measured is connected one arm across the bridge, the equivalent parallel resistance and reactance (capacitive or inductive) unbalances the bridge and the resulting voltage is fed to the mixer. The output of the 0.6-250.1 MHz oscillator F2, tracking 100 kHz above F1, is also fed to the mixer. This results in a 100 kHz difference frequency proportional in level to the bridge unbalance. The difference frequency signal is amplified by a filter amplifier combination and is applied to a null meter. When the bridge resistive and reactive controls are nulled, their respective dials accurately indicate the parallel impedance components of the network under test.
The best-known RX Meter was the RX250-A, developed in the early 1950s by Boonton Radio Corporation. After acquiring BRC, Hewlett-Packard continued to sell versions of the meter (both the original and the improved 250B) into the late 1960s.
References
Electrical engineering
Impedance measurements |
https://en.wikipedia.org/wiki/Cytochrome%20c%20oxidase%20subunit%20I | Cytochrome c oxidase I (COX1) also known as mitochondrially encoded cytochrome c oxidase I (MT-CO1) is a protein that is encoded by the MT-CO1 gene in eukaryotes. The gene is also called COX1, CO1, or COI. Cytochrome c oxidase I is the main subunit of the cytochrome c oxidase complex. In humans, mutations in MT-CO1 have been associated with Leber's hereditary optic neuropathy (LHON), acquired idiopathic sideroblastic anemia, Complex IV deficiency, colorectal cancer, sensorineural deafness, and recurrent myoglobinuria.
Structure
In humans, the MT-CO1 gene is located from nucleotide pairs 5904 to 7444 on the guanine-rich heavy (H) section of mtDNA. The gene product is a 57 kDa protein composed of 513 amino acids.
Function
Cytochrome c oxidase subunit I (CO1 or MT-CO1) is one of three mitochondrial DNA (mtDNA) encoded subunits (MT-CO1, MT-CO2, MT-CO3) of respiratory complex IV. Complex IV is the third and final enzyme of the electron transport chain of mitochondrial oxidative phosphorylation.
Cytochrome c oxidase () is a key enzyme in aerobic metabolism. Proton pumping heme-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-heme a3 (or heme o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plas |
https://en.wikipedia.org/wiki/Piskacek%27s%20sign | In medicine, Piskacek's sign is an indication of pregnancy. This sign, however, may or may not be a concrete probability of pregnancy along with other signs of early pregnancy. Other signs of early pregnancy include Goodell, Hegar, von Braun Fernwald, Hartman sign and Chadwick.
Implantation of Zygote is eccentric so that growth of uterus is unequal in early pregnancy known as Piskacek's sign.
Specifically, Piskacek's sign consists noting a palpable lateral bulge or soft prominence one of the locations where the fallopian tube meets the uterus. Piskacek's sign can be noted in the seventh to eight week of gestation. Non pregnant uterus is pyriform in shape. By 12 weeks of gestation it becomes globular. In lateral implantation, there is asymmetrical enlargement of the uterus. One half of the uterus where the implantation occurred is firm while the other half is soft. This is known as Piskacek's sign.
The sign is named after Ludwig Piskaçek.
References
Medical signs
Obstetrics
Midwifery |
https://en.wikipedia.org/wiki/Planta%20Solar%20de%20Salamanca | Planta Solar de Salamanca is a 13.8 peak MW photovoltaic power plant located in Salamanca, Spain. The plant consists of approximately 70,000 Kyocera solar panels, occupying approximately 36-hectare (89-acre) site.
The plant was opened for operation on September 18, 2007.
See also
Photovoltaic power stations
References
Photovoltaic power stations in Spain |
https://en.wikipedia.org/wiki/1953%20Green%20Bay%20Packers%20season | The 1953 Green Bay Packers season was their 35th season overall and their 33rd in the National Football League. The team finished with a 2–9–1 record under head coach Gene Ronzani and interim co-coaches Ray McLean, and Hugh Devore, and finished last in the newly named Western Conference.
Fourth-year head coach Ronzani led the team for the first ten games, but resigned after a nationally televised Thanksgiving Day loss, his eighth loss to the Detroit Lions in four seasons; McLean and Devore co-coached the last two games of the season, both losses.
It was the only in-season coaching change in Packers history, until 2018. This season also marked the first season that the Packers played at the recently completed Milwaukee County Stadium.
Offseason
NFL draft
Yellow indicates a future Pro Bowl selection
Green indicates a future Pro Football Hall of Fame inductee
Regular season
Schedule
Standings
Roster
References
Sportsencyclopedia.com
Green Bay Packers seasons
Green Bay Packers
Green |
https://en.wikipedia.org/wiki/Kernelization | In computer science, a kernelization is a technique for designing efficient algorithms that achieve their efficiency by a preprocessing stage in which inputs to the algorithm are replaced by a smaller input, called a "kernel". The result of solving the problem on the kernel should either be the same as on the original input, or it should be easy to transform the output on the kernel to the desired output for the original problem.
Kernelization is often achieved by applying a set of reduction rules that cut away parts of the instance that are easy to handle. In parameterized complexity theory, it is often possible to prove that a kernel with guaranteed bounds on the size of a kernel (as a function of some parameter associated to the problem) can be found in polynomial time. When this is possible, it results in a fixed-parameter tractable algorithm whose running time is the sum of the (polynomial time) kernelization step and the (non-polynomial but bounded by the parameter) time to solve the kernel. Indeed, every problem that can be solved by a fixed-parameter tractable algorithm can be solved by a kernelization algorithm of this type. This is also true for approximate kernelization.
Example: vertex cover
A standard example for a kernelization algorithm is the kernelization of the vertex cover problem by S. Buss.
In this problem, the input is an undirected graph together with a number . The output is a set of at most vertices that includes an endpoint of every edge in the g |
https://en.wikipedia.org/wiki/SRBC | SRBC can stand for:
CD2, a cell adhesion molecule found on the surface of T cells and natural killer (NK) cells
Southern Railway of British Columbia, a Canadian short line railway branded as SRY Rail Link
Susquehanna River Basin Commission, a water management agency in the United States created by interstate compact |
https://en.wikipedia.org/wiki/Carboxypeptidase%20B2 | Carboxypeptidase B2 (CPB2), also known as carboxypeptidase U (CPU), plasma carboxypeptidase B (pCPB) or thrombin-activatable fibrinolysis inhibitor (TAFI), is an enzyme that, in humans, is encoded by the gene CPB2.
Function
CPB2 is synthesized by the liver and circulates in the plasma as a plasminogen-bound zymogen. When it is activated by proteolysis at residue Arg92 by the thrombin/thrombomodulin complex, CPB2 exhibits carboxypeptidase activity. Activated CPB2 reduces fibrinolysis by removing the fibrin C-terminal residues that are important for the binding and activation of plasminogen.
Carboxypeptidases are enzymes that hydrolyze C-terminal peptide bonds. The carboxypeptidase family includes metallo-, serine, and cysteine carboxypeptidases. According to their substrate specificity, these enzymes are referred to as carboxypeptidase A (cleaving aliphatic residues) or carboxypeptidase B (cleaving basic amino residues). The protein encoded by this gene is activated by thrombin and acts on carboxypeptidase B substrates. After thrombin activation, the mature protein downregulates fibrinolysis.
Isozymes
Polymorphisms have been described for this gene and its promoter region. Available sequence data analyses indicate splice variants that encode different isoforms.
See also
Carboxypeptidase B
References
Further reading
Fibrinolytic system |
https://en.wikipedia.org/wiki/CTBP1 | C-terminal-binding protein 1 also known as CtBP1 is a protein that in humans is encoded by the CTBP1 gene. CtBP1 is one of two CtBP proteins, the other protein being CtBP2.
Function
The CtBP1 protein was originally identified as a human protein that bound a PLDLS motif in the C-terminus of adenovirus E1A proteins. It and the related protein CTBP2 were later shown to function as transcriptional corepressors. That is, regulatory proteins that bind to sequence-specific DNA-binding proteins and help turn genes off. CtBPs do this by recruiting histone modifying enzymes that add repressive histone marks and remove activating marks. CtBP proteins can also self-associate and presumably bring together gene regulatory complexes.
CtBP1 is broadly expressed from embryo to adult, while CtBP2 has a somewhat more restricted pattern of expression. CtBPs have multiple biological roles and appear to be most important in regulating the epithelial to mesenchymal transition, as well as influencing metabolism. They do the latter by binding NADH in preference to NAD+, thereby sensing the NADH/NAD+ ratio. When bound, it undergoes a conformational change that allows it to dimerize and associate with its partner proteins and silence specific genes.
During skeletal and T cell development, CtBP1 and CtBP2 associate with the PLDLSL domain of δEF1, a cellular zinc finger-homeodomain protein, and thereby enhances δEF1-induced transcriptional silencing. CtBP also binds the Kruppel-like factors family of |
https://en.wikipedia.org/wiki/The%20Crystal%20Cube | The Crystal Cube was a mockumentary television pilot written by and starring Stephen Fry and Hugh Laurie, broadcast on 7 July 1983 on BBC2 at 22:10. The pilot was one of Fry and Laurie's first television appearances and the first show they had written themselves. However, the BBC chose not to take it to a full series, and Fry and Laurie did not get a chance to make their own programme for the BBC until 1989, when they produced their first full series of the more conventional sketch show A Bit of Fry and Laurie, after a pilot in 1987.
Plot
The Crystal Cube was a spoof science programme, based on shows such as Tomorrow's World. The show was hosted by Jackie Meld (Emma Thompson). In each episode, a different topic of science was to be discussed. In the pilot, it was genetics. Two guest scientists discussed the issue of genetics to a live studio audience and viewers at home. The scientists were Dr. Adrian Cowlacey (Fry), a practicing clinician at St. Thomas' Hospital, London, and Max Belhaven (Laurie) of the Bastard Institute in California. Cowlacey and Belhaven commented positively on the prospects that in the future, society would be divided into a genetic caste system with people divided into "Alphas", "Betas" and "Gammas" based on their genetic background (terminology used in Huxley's Brave New World). They also showed an example of a genetically engineered human, Gareth Gamma 0001 (Arthur Bostrom), who was designed to carry out menial tasks without complaint. The show later |
https://en.wikipedia.org/wiki/Dilruba | The dilruba (also spelt dilrupa) is a bowed musical instrument originating in India. It is slightly larger than an esraj and has a larger, square resonance box. The dilruba holds particular importance in Sikh history.
It became more widely known outside India in the 1960s through use in songs by Western artists, such as the Beatles during their psychedelic phase (most notably in the song "Within You Without You").
Etymology
The name of the instrument derives from the Persianized Hindustani word دلربا/दिलरुबा (dilrubā), literally meaning "that which ravishes or steals the heart."
History
The traditional story is that the dilruba was invented around 300 years ago by the 10th Sikh Guru, Guru Gobind Singh, who based it on the much older and much heavier taus. His innovations made it more convenient for the Sikh army (the khalsa) to carry the instrument on horseback.
There is some doubt in the research community about the truth of the traditional origin story described above. Some traditional kirtan bearers, such as Bhai Avtar Singh Raagi, have clarified the history of the dilruba's creation being tied to the patronage of Maharaja Bhupinder Singh and created by Mahant Gajja Singh.
After the introduction of the harmonium to the Indian Subcontinent by the British Raj, the dilruba fell out of use due to its comparatively steeper learning curve. In more recent times, it has had a resurgence, accompanying ragis in the Harmandir Sahib (Golden Temple) since 2006, and becoming more |
https://en.wikipedia.org/wiki/ELAV-like%20protein%201 | ELAV-like protein 1 or HuR (human antigen R) is a protein that in humans is encoded by the ELAVL1 gene.
The protein encoded by this gene is a member of the ELAVL protein family. This encoded protein contains 3 RNA-binding domains and binds cis-acting AU-rich elements. One of its best-known functions is to stabilize mRNAs in order to regulate gene expression.
See also
RNA-Binding Protein
Y box binding protein 1 (YBX1), may form complex with ELAVL1 affecting mRNA stability during muscle-fiber formation
References
Further reading
External links
PDBe-KB provides an overview of all the structure information available in the PDB for Human ELAV-like protein 1 |
https://en.wikipedia.org/wiki/Igor%20Talankin | Igor Vasilyevich Talankin () (3 October 1927 – 24 July 2010) was a Soviet and Russian film director and screenwriter. His film Splendid Days (1960, co-directed with Georgiy Daneliya) won the Crystal Globe (the main award) at the Karlovy Vary International Film Festival, and Tchaikovsky (1969) was nominated for the Academy Award for Best Foreign Language Film.
Selected filmography
Splendid Days (1960)
Introduction to Life (1962)
Day Stars (1968)
Tchaikovsky (1969)
Take Aim (1974)
Father Sergius (1978)
Starfall (1981)
Time for Rest from Saturday to Monday (1984)
References
External links
1927 births
2010 deaths
People from Noginsk
Academic staff of the Gerasimov Institute of Cinematography
People's Artists of the RSFSR
People's Artists of the USSR
Recipients of the Order "For Merit to the Fatherland", 4th class
Recipients of the Order of the Red Banner of Labour
Russian film directors
20th-century Russian screenwriters
Russian male screenwriters
20th-century Russian male writers
Soviet film directors
Soviet screenwriters |
https://en.wikipedia.org/wiki/HBE1 | Hemoglobin subunit epsilon is a protein that in humans is encoded by the HBE1 gene.
Function
The epsilon globin gene (HBE) is normally expressed in the embryonic yolk sac: two epsilon chains together with two zeta chains (an alpha-like globin) constitute the embryonic hemoglobin Hb Gower I; two epsilon chains together with two alpha chains form the embryonic Hb Gower II. Both of these embryonic hemoglobins are normally supplanted by fetal, and later, adult hemoglobin. The five beta-like globin genes are found within a 45 kb cluster on chromosome 11 in the following order: 5' - epsilon – gamma-G – gamma-A – delta – beta - 3'.
See also
Hemoglobin
Human β-globin locus
Hemoglobin alpha chains (two genes, same sequence):
HBA1
HBA2
References
Further reading
Hemoglobins |
https://en.wikipedia.org/wiki/Moesin | Moesin is a protein that in humans is encoded by the MSN gene.
Moesin (for membrane-organizing extension spike protein) is a member of the ERM protein family which includes ezrin and radixin. ERM proteins appear to function as cross-linkers between plasma membranes and actin-based cytoskeletons.
Moesin is localized to filopodia and other membranous protrusions that are important for cell–cell recognition and signaling and for cell movement.
Interactions
Moesin has been shown to interact with:
CD43
ICAM3
Neutrophil cytosolic factor 1,
Neutrophil cytosolic factor 4
VCAM-1
EZR
References
Further reading
Human proteins |
https://en.wikipedia.org/wiki/PLA2G2A | Phospholipase A2, membrane associated is an enzyme that in humans is encoded by the PLA2G2A gene.
See also
Phospholipase A2
References
Further reading |
https://en.wikipedia.org/wiki/Trypsin%201 | Trypsin-1, also known as cationic trypsinogen, is a protein that in humans is encoded by the PRSS1 gene. Trypsin-1 is the main isoform of trypsinogen secreted by pancreas, the others are trypsin-2 (anionic trypsinogen), and trypsin-3 (meso-trypsinogen).
Function
This gene encodes a trypsinogen, which is a member of the trypsin family of serine proteases. This enzyme is secreted by the pancreas and cleaved to its active form in the small intestine. It is active on peptide linkages involving the carboxyl group of lysine or arginine. Mutations in this gene are associated with hereditary pancreatitis. This gene and several other trypsinogen genes are localized to the T cell receptor beta locus on chromosome 7.
Clinical significance
Its malfunction acts in an autosomal dominant manner to cause pancreatitis. Many mutations that can lead to pancreatitis have been found. An example is a mutation at Arg 117. Arg 117 is a trypsin-sensitive site which can be cleaved by another trypsin and becomes inactivated. This site may be a fail-safe mechanism by which trypsin, when activated within the pancreas, may become inactivated. Mutation at this cleavage site would result in a loss of control and permit autodigestion, causing pancreatitis.
See also
Trypsin
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on PRSS1-Related Hereditary Pancreatitis
EC 3.4.21 |
https://en.wikipedia.org/wiki/Khaled%20Saad | Khaled Saad Salem Al-Malta'ah () is a Jordanian former footballer.
Career statistics
International
Scores and results list Oman's goal tally first.
References
External links
1981 births
Living people
Jordanian men's footballers
Jordan men's international footballers
Jordanian expatriate men's footballers
Men's association football defenders
2004 AFC Asian Cup players
Nejmeh SC players
Expatriate men's footballers in Lebanon
Jordanian expatriate sportspeople in Lebanon
Zamalek SC players
Expatriate men's footballers in Egypt
Jordanian expatriate sportspeople in Egypt
Salalah SC players
Fanja SC players
Expatriate men's footballers in Oman
Jordanian expatriate sportspeople in Oman
Al-Faisaly SC players
Egyptian Premier League players
Lebanese Premier League players |
https://en.wikipedia.org/wiki/Heteroglycan%20alpha-mannosyltransferase | In enzymology, a heteroglycan alpha-mannosyltransferase () is an enzyme that catalyzes the chemical reaction
GDP-mannose + heteroglycan GDP + 2(or 3)-alpha-D-mannosyl-heteroglycan
Thus, the two substrates of this enzyme are GDP-mannose and heteroglycan, whereas its 3 products are GDP, 2-alpha-D-mannosyl-heteroglycan, and 3-alpha-D-mannosyl-heteroglycan.
This enzyme belongs to the family of glycosyltransferases, to be specific the hexosyltransferases. The systematic name of this enzyme class is GDP-mannose:heteroglycan 2-(or 3-)-alpha-D-mannosyltransferase. Other names in common use include GDP mannose alpha-mannosyltransferase, and guanosine diphosphomannose-heteroglycan alpha-mannosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hydroquinone%20glucosyltransferase | In enzymology, a hydroquinone glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + hydroquinone UDP + hydroquinone-O-beta-D-glucopyranoside
Thus, the two substrates of this enzyme are UDP-glucose and hydroquinone, whereas its two products are UDP and hydroquinone-O-beta-D-glucopyranoside.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:hydroquinone-O-beta-D-glucosyltransferase. Other names in common use include arbutin synthase, and hydroquinone:O-glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hydroxyanthraquinone%20glucosyltransferase | In enzymology, a hydroxyanthraquinone glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + an hydroxyanthraquinone UDP + a glucosyloxyanthraquinone
Thus, the two substrates of this enzyme are UDP-glucose and hydroxyanthraquinone, whereas its two products are UDP and glucosyloxyanthraquinone.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:hydroxyanthraquinone O-glucosyltransferase. Other names in common use include uridine diphosphoglucose-anthraquinone glucosyltransferase, and anthraquinone-specific glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hydroxycinnamate%204-beta-glucosyltransferase | In enzymology, a hydroxycinnamate 4-beta-glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + trans-4-hydroxycinnamate UDP + 4-O-beta-D-glucosyl-4-hydroxycinnamate
Thus, the two substrates of this enzyme are UDP-glucose and trans-4-hydroxycinnamate (p-coumaric acid), whereas its two products are UDP and 4-O-beta-D-glucosyl-4-hydroxycinnamate.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:trans-4-hydroxycinnamate 4-O-beta-D-glucosyltransferase. Other names in common use include uridine diphosphoglucose-hydroxycinnamate glucosyltransferase, UDP-glucose-hydroxycinnamate glucosyltransferase, and hydroxycinnamoyl glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure
Hydroxycinnamic acids metabolism |
https://en.wikipedia.org/wiki/Hydroxymandelonitrile%20glucosyltransferase | In enzymology, a hydroxymandelonitrile glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + 4-hydroxymandelonitrile UDP + taxiphyllin
Thus, the two substrates of this enzyme are UDP-glucose and 4-hydroxymandelonitrile, whereas its two products are UDP and taxiphyllin.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:4-hydroxymandelonitrile glucosyltransferase. Other names in common use include cyanohydrin glucosyltransferase, and uridine diphosphoglucose-cyanohydrin glucosyltransferase. This enzyme participates in tyrosine metabolism.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Torsin%20A | Torsin-1A (TorA) also known as dystonia 1 protein (DYT1) is a protein that in humans is encoded by the TOR1A gene (also known as DQ2 or DYT1). TorA localizes to the endoplasmic reticulum and contiguous perinuclear space, where its ATPase activity is activated by either LULL1 or LAP1, respectively.
Function
The protein encoded by this gene is a member of the AAA family of adenosine triphosphatases (ATPases), is related to the Clp protease/heat shock family.
Clinical significance
Mutations in this gene result in the autosomal dominant disorder, torsion dystonia 1.
References
Further reading
External links
GeneReview/NIH/UW entry on Early-Onset Primary Dystonia |
https://en.wikipedia.org/wiki/Indole-3-acetate%20beta-glucosyltransferase | In enzymology, an indole-3-acetate beta-glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + (indol-3-yl)acetate UDP + 1-O-(indol-3-yl)acetyl-beta-D-glucose
Thus, the two substrates of this enzyme are UDP-glucose and (indol-3-yl)acetate, whereas its two products are UDP and 1-O-(indol-3-yl)acetyl-beta-D-glucose.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:(indol-3-yl)acetate beta-D-glucosyltransferase. Other names in common use include uridine diphosphoglucose-indoleacetate glucosyltransferase, UDPG-indol-3-ylacetyl glucosyl transferase, UDP-glucose:indol-3-ylacetate glucosyltransferase, indol-3-ylacetylglucose synthase, UDP-glucose:indol-3-ylacetate glucosyl-transferase, IAGlu synthase, IAA-glucose synthase, and UDP-glucose:indole-3-acetate beta-D-glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Geometallurgy | Geometallurgy relates to the practice of combining geology or geostatistics with metallurgy, or, more specifically, extractive metallurgy, to create a spatially or geologically based predictive model for mineral processing plants. It is used in the hard rock mining industry for risk management and mitigation during mineral processing plant design. It is also used, to a lesser extent, for production planning in more variable ore deposits.
There are four important components or steps to developing a geometallurgical program,:
the geologically informed selection of a number of ore samples
laboratory-scale test work to determine the ore's response to mineral processing unit operations
the distribution of these parameters throughout the orebody using an accepted geostatistical technique
the application of a mining sequence plan and mineral processing models to generate a prediction of the process plant behavior
Sample selection
The sample mass and size distribution requirements are dictated by the kind of mathematical model that will be used to simulate the process plant, and the test work required to provide the appropriate model parameters. Flotation testing usually requires several kg of sample and grinding/hardness testing can required between 2 and 300 kg.
The sample selection procedure is performed to optimize granularity, sample support, and cost. Samples are usually core samples composited over the height of the mining bench. For hardness parameters, the variog |
https://en.wikipedia.org/wiki/Indolylacetylinositol%20arabinosyltransferase | In enzymology, an indolylacetylinositol arabinosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-L-arabinose + (indol-3-yl)acetyl-1D-myo-inositol UDP + (indol-3-yl)acetyl-myo-inositol 3-L-arabinoside
Thus, the two substrates of this enzyme are UDP-L-arabinose and indol-3-ylacetyl-1D-myo-inositol, whereas its two products are UDP and (indol-3-yl)acetyl-myo-inositol 3-L-arabinoside.
This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is UDP-L-arabinose:(indol-3-yl)acetyl-myo-inositol L-arabinosyltransferase. Other names in common use include arabinosylindolylacetylinositol synthase, UDP-L-arabinose:indol-3-ylacetyl-myo-inositol, and L-arabinosyltransferase.
References
EC 2.4.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Indolylacetyl-myo-inositol%20galactosyltransferase | In enzymology, an indolylacetyl-myo-inositol galactosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-galactose + (indol-3-yl)acetyl-myo-inositol UDP + 5-O-(indol-3-yl)acetyl-myo-inositol D-galactoside
Thus, the two substrates of this enzyme are UDP-galactose and indol-3-ylacetyl-myo-inositol, whereas its two products are UDP and 5-O-(indol-3-yl)acetyl-myo-inositol D-galactoside.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:(indol-3-yl)acetyl-myo-inositol 5-O-D-galactosyltransferase. Other names in common use include uridine diphosphogalactose-indolylacetylinositol, galactosyltransferase, indol-3-ylacetyl-myo-inositol galactoside synthase, UDP-galactose:indol-3-ylacetyl-myo-inositol, and 5-O-D-galactosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cyclomaltodextrin%20glucanotransferase | In enzymology, a cyclomaltodextrin glucanotransferase (also cyclodextrin glycosyl transferase or CGTase for short) () is an enzyme that catalyzes the chemical reaction of cyclizing part of a 1,4-alpha-D-glucan molecule through the formation of a 1,4-alpha-D-glucosidic bond. They are bacterial enzymes belonging to the same family of the α-amylase specifically known as glycosyl-hydrolase family 13. This peculiar enzyme is capable of catalyzing more than one reaction with the most important being the synthesis of non-reducing cyclic dextrins known as cyclodextrins starting from starch, amylose, and other polysaccharides.
CGTase is an enzyme common to many bacterial species, in particular of the Bacillus genus (e.g. B. circulans, B. macerans and B. stearothermophilus) and Brevibacillus brevis.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is 1,4-alpha-D-glucan 4-alpha-D-(1,4-alpha-D-glucano)-transferase (cyclizing). Other names in common use include Bacillus macerans amylase, cyclodextrin glucanotransferase, alpha-cyclodextrin glucanotransferase, alpha-cyclodextrin glycosyltransferase, beta-cyclodextrin glucanotransferase, beta-cyclodextrin glycosyltransferase, gamma-cyclodextrin glycosyltransferase, cyclodextrin glycosyltransferase, cyclomaltodextrin glucotransferase, cyclomaltodextrin glycosyltransferase, konchizaimu, alpha-1,4-glucan 4-glycosyltransferase, cyclizing, BMA, CGTase, and |
https://en.wikipedia.org/wiki/Indoxyl-UDPG%20glucosyltransferase | In enzymology, an indoxyl-UDPG glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + indoxyl UDP + indican
Thus, the two substrates of this enzyme are UDP-glucose and indoxyl, whereas its two products are UDP and indican.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:indoxyl 3-O-beta-D-glucosyltransferase. This enzyme is also called indoxyl-UDPG-glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Inositol%203-alpha-galactosyltransferase | In enzymology, an inositol 3-alpha-galactosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-galactose + myo-inositol UDP + O-alpha-D-galactosyl-(1->3)-1D-myo-inositol
Thus, the two substrates of this enzyme are UDP-galactose and myo-inositol, whereas its two products are UDP and [[O-alpha-D-galactosyl-(1->3)-1D-myo-inositol]].
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:myo-inositol 3-alpha-D-galactosyltransferase. Other names in common use include UDP-D-galactose:inositol galactosyltransferase, UDP-galactose:myo-inositol 1-alpha-D-galactosyltransferase, UDPgalactose:myo-inositol 1-alpha-D-galactosyltransferase, galactinol synthase, inositol 1-alpha-galactosyltransferase, and uridine diphosphogalactose-inositol galactosyltransferase. This enzyme participates in galactose metabolism.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/DNA%20alpha-glucosyltransferase | In enzymology, a DNA alpha-glucosyltransferase () is an enzyme that catalyzes the chemical reaction in which an alpha-D-glucosyl residue is transferred from UDP-glucose to a hydroxymethylcytosine residue in DNA.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:DNA alpha-D-glucosyltransferase. Other names in common use include uridine diphosphoglucose-deoxyribonucleate, alpha-glucosyltransferase, UDP-glucose-DNA alpha-glucosyltransferase, uridine diphosphoglucose-deoxyribonucleate, alpha-glucosyltransferase, T2-HMC-alpha-glucosyl transferase, T4-HMC-alpha-glucosyl transferase, and T6-HMC-alpha-glucosyl transferase.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
EC 2.4.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Inulosucrase | In enzymology, an inulosucrase () is an enzyme that catalyzes the chemical reaction
sucrose + (2,1-beta-D-fructosyl)n glucose + (2,1-beta-D-fructosyl)n+1
Thus, the two substrates of this enzyme are sucrose and (2,1-beta-D-fructosyl)n, whereas its two products are glucose and (2,1-beta-D-fructosyl)n+1.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is sucrose:2,1-beta-D-fructan 1-beta-D-fructosyltransferase. This enzyme is also called sucrose 1-fructosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Isoflavone%207-O-glucosyltransferase | In enzymology, an isoflavone 7-O-glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + an isoflavone UDP + an isoflavone 7-O-beta-D-glucoside
Thus, the two substrates of this enzyme are UDP-glucose and isoflavone, whereas its two products are UDP and isoflavone 7-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:isoflavone 7-O-beta-D-glucosyltransferase. Other names in common use include uridine diphosphoglucose-isoflavone 7-O-glucosyltransferase, UDPglucose-favonoid 7-O-glucosyltransferase, and UDPglucose:isoflavone 7-O-glucosyltransferase. This enzyme participates in isoflavonoid biosynthesis.
References
EC 2.4.1
Enzymes of unknown structure
Isoflavonoids metabolism |
https://en.wikipedia.org/wiki/Isovitexin%20beta-glucosyltransferase | In enzymology, an isovitexin beta-glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + isovitexin UDP + isovitexin 2"-O-beta-D-glucoside
Thus, the two substrates of this enzyme are UDP-glucose and isovitexin, whereas its two products are UDP and isovitexin 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:isovitexin 2"-O-beta-D-glucosyltransferase. This enzyme is also called uridine diphosphoglucose-isovitexin 2"-glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/DNA%20beta-glucosyltransferase | In enzymology, a DNA beta-glucosyltransferase () is an enzyme that catalyzes the chemical reaction in which a beta-D-glucosyl residue is transferred from UDP-glucose to an hydroxymethylcytosine residue in DNA. It is analogous to the enzyme DNA alpha-glucosyltransferase.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:DNA beta-D-glucosyltransferase. Other names in common use include T4-HMC-beta-glucosyl transferase, T4-beta-glucosyl transferase, T4 phage beta-glucosyltransferase, UDP glucose-DNA beta-glucosyltransferase, and uridine diphosphoglucose-deoxyribonucleate beta-glucosyltransferase.
Structural studies
As of late 2007, 20 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , and .
Bacteriophage T4 beta-glucosyltransferase
In molecular biology, Bacteriophage T4 beta-glucosyltransferase refers to a protein domain found in a virus of Escherichia coli named bacteriophage T4. Members of this family are enzymes encoded by bacteriophage T4, which modify DNA by transferring glucose from uridine diphosphoglucose to 5-hydroxymethyl cytosine bases of phage T4 DNA.
Function
Beta-glucosyltransferase is an enzyme, or more specifically an inverting glycosyltransferase (GT). In other words, it transfers glucose from uridine diphospho-glucose (UDPglucose) to an acceptor, modified DNA through beta-Glycosidic bon |
https://en.wikipedia.org/wiki/Kaempferol%203-O-galactosyltransferase | In enzymology, a kaempferol 3-O-galactosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-galactose + kaempferol UDP + kaempferol 3-O-beta-D-galactoside
Thus, the two substrates of this enzyme are UDP-galactose and kaempferol, whereas its two products are UDP and trifolin.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:kaempferol 3-O-beta-D-galactosyltransferase. This enzyme is also called F3GalTase.
References
EC 2.4.1
Enzymes of unknown structure
Kaempferol |
https://en.wikipedia.org/wiki/Kojibiose%20phosphorylase | In enzymology, a kojibiose phosphorylase () is an enzyme that catalyzes the chemical reaction
2-alpha-D-glucosyl-D-glucose + phosphate D-glucose + beta-D-glucose 1-phosphate
Thus, the two substrates of this enzyme are kojibiose and phosphate, whereas its two products are D-glucose 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 2-alpha-D-glucosyl-D-glucose:phosphate beta-D-glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lactosylceramide%201%2C3-N-acetyl-beta-D-glucosaminyltransferase | In enzymology, a lactosylceramide 1,3-N-anning-beta-D-glrofelucosaminyltlolferase () is an enzyme that catalyzes the chemical reaction
UDP-N-acetyl-D-glucosamine + D-galactosyl-1,4-beta-D-glucosylceramide UDP + N-acetyl-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D- glucosylceramide
Thus, the two substrates of this enzyme are UDP-N-acetyl-D-glucosamine and D-galactosyl-1,4-beta-D-glucosylceramide, whereas its 3 products are UDP, N-acetyl-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-, and glucosylceramide.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:D-galactosyl-1,4-beta-D-glucosylceramide beta-1,3-acetylglucosaminyltransferase. Other names in common use include LA2 synthase, beta1->3-N-acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-lactosylceramide, beta-acetylglucosaminyltransferase, and lactosylceramide beta-acetylglucosaminyltransferase. This enzyme participates in 3 metabolic pathways: glycosphingolipid biosynthesis - lactoseries, glycosphingolipid biosynthesis - neo-lactoseries, and glycan structures - biosynthesis 2.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lactosylceramide%204-alpha-galactosyltransferase | In enzymology, a lactosylceramide 4-alpha-galactosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-galactose + beta-D-galactosyl-(1->4)-D-glucosylceramide UDP + alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-D- glucosylceramide
Thus, the two substrates of this enzyme are UDP-galactose and [[beta-D-galactosyl-(1->4)-D-glucosylceramide]], whereas its 3 products are UDP, [[alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-D-]], and glucosylceramide.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:lactosylceramide 4II-alpha-D-galactosyltransferase. Other names in common use include Galbeta1-4Glcbeta1-Cer alpha1,4-galactosyltransferase, globotriaosylceramide/CD77 synthase, and histo-blood group Pk UDP-galactose. This enzyme participates in glycosphingolipid biosynthesis - globoseries and glycan structures - biosynthesis 2.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lactosylceramide%20alpha-2%2C3-sialyltransferase | In enzymology, a lactosylceramide alpha-2,3-sialyltransferase () is an enzyme that catalyzes the chemical reaction
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-beta-D-glucosylceramide CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-beta-D- glucosylceramide
Thus, the two substrates of this enzyme are CMP-N-acetylneuraminate and beta-D-galactosyl-1,4-beta-D-glucosylceramide, whereas its 3 products are CMP, alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-beta-D-, and glucosylceramide.
This enzyme belongs to the family of transferases, specifically those glycosyltransferases that do not transfer hexosyl or pentosyl groups. The systematic name of this enzyme class is CMP-N-acetylneuraminate:lactosylceramide alpha-2,3-N-acetylneuraminyltransferase. Other names in common use include cytidine monophosphoacetylneuraminate-lactosylceramide alpha2,3-, sialyltransferase, CMP-acetylneuraminate-lactosylceramide-sialyltransferase, CMP-acetylneuraminic acid:lactosylceramide sialyltransferase, CMP-sialic acid:lactosylceramide-sialyltransferase, cytidine monophosphoacetylneuraminate-lactosylceramide, sialyltransferase, ganglioside GM3 synthetase, GM3 synthase, GM3 synthetase, and SAT 1. This enzyme participates in glycosphingolipid biosynthesis - ganglioseries and glycan structures - biosynthesis 2.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.4.99
Enzymes of known |
https://en.wikipedia.org/wiki/Lactosylceramide%20alpha-2%2C6-N-sialyltransferase | In enzymology, a lactosylceramide alpha-2,6-N-sialyltransferase () is an enzyme that catalyzes the chemical reaction
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-beta-D-glucosylceramide CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-beta-D- glucosylceramide
Thus, the two substrates of this enzyme are CMP-N-acetylneuraminate and beta-D-galactosyl-1,4-beta-D-glucosylceramide, whereas its 3 products are CMP, alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-beta-D-, and glucosylceramide.
This enzyme belongs to the family of transferases, specifically those glycosyltransferases that do not transfer hexosyl or pentosyl groups. The systematic name of this enzyme class is CMP-N-acetylneuraminate:lactosylceramide alpha-2,6-N-acetylneuraminyltransferase. Other names in common use include cytidine monophosphoacetylneuraminate-lactosylceramide, sialyltransferase, CMP-acetylneuraminate-lactosylceramide-sialyltransferase, CMP-N-acetylneuraminic acid:lactosylceramide sialyltransferase, CMP-sialic acid:lactosylceramide sialyltransferase, cytidine monophosphoacetylneuraminate-lactosylceramide, and sialyltransferase.
References
EC 2.4.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lactosylceramide%20beta-1%2C3-galactosyltransferase | In enzymology, a lactosylceramide beta-1,3-galactosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-galactose + D-galactosyl-1,4-beta-D-glucosyl-R UDP + D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosyl-R
Thus, the two substrates of this enzyme are UDP-galactose and D-galactosyl-1,4-beta-D-glucosyl-R, whereas its two products are UDP and D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosyl-R.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:D-galactosyl-1,4-beta-D-glucosyl-R beta-1,3-galactosyltransferase. Other names in common use include uridine diphosphogalactose-lactosylceramide, and beta1->3-galactosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glucosyl-DNA%20beta-glucosyltransferase | In enzymology, a glucosyl-DNA beta-glucosyltransferase () is an enzyme that catalyzes the chemical reaction in which a beta-D-glucosyl residue is transferred from UDP-glucose to a glucosylhydroxymethylcytosine residue in DNA. This enzyme resembles DNA beta-glucosyltransferase in that respect.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:D-glucosyl-DNA beta-D-glucosyltransferase. Other names in common use include T6-glucosyl-HMC-beta-glucosyl transferase, T6-beta-glucosyl transferase, uridine diphosphoglucose-glucosyldeoxyribonucleate, and beta-glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure
Viral enzymes |
https://en.wikipedia.org/wiki/Laminaribiose%20phosphorylase | In enzymology, a laminaribiose phosphorylase () is an enzyme that catalyzes the chemical reaction
3-beta-D-glucosyl-D-glucose + phosphate D-glucose + alpha-D-glucose 1-phosphate
Thus, the two substrates of this enzyme are 3-beta-D-glucosyl-D-glucose and phosphate, whereas its two products are D-glucose and alpha-D-glucose 1-phosphate.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is 3-beta-D-glucosyl-D-glucose:phosphate alpha-D-glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Levansucrase | Levansucrase () is an enzyme that catalyzes the chemical reaction
sucrose + (2,6-beta-D-fructosyl)n glucose + (2,6-beta-D-fructosyl)n+1
Thus, the two substrates of this enzyme are sucrose and (2,6-beta-D-fructosyl)n, whereas its two products are glucose and (2,6-beta-D-fructosyl)n+1.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is sucrose:2,6-beta-D-fructan 6-beta-D-fructosyltransferase. Other names in common use include sucrose 6-fructosyltransferase, beta-2,6-fructosyltransferase, and beta-2,6-fructan:D-glucose 1-fructosyltransferase. This enzyme participates in starch and sucrose metabolism and two-component system - general.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
SacB counter-selection relies on the toxic product produced by the SacB gene. sacB comes from the gram-positive bacteria Bacillus subtilis and encodes the enzyme levansucrase that converts sucrose into a toxic metabolite in gram-negative bacteria. Plating on sucrose medium will select for cells that contain constructs that have lost the sacB gene.
EC 2.4.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Limonoid%20glucosyltransferase | In enzymology, a limonoid glucosyltransferase () is an enzyme that catalyzes the chemical reaction.
UDP-glucose + limonin glucosyl-limonin + UDP
Thus, the two substrates of this enzyme are UDP-glucose and limonin, whereas its two products are glucosyl-limonin and UDP.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is uridine diphosphoglucose-limonoid glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/BSIM | BSIM (Berkeley Short-channel IGFET Model) refers to a family of MOSFET transistor models for integrated circuit design. It also refers to the BSIM group located in the Department of Electrical Engineering and Computer Sciences (EECS) at the University of California, Berkeley, that develops these models. Accurate transistor models are needed for electronic circuit simulation, which in turn is needed for integrated circuit design. As the devices become smaller each process generation (see Moore's law), new models are needed to accurately reflect the transistor's behavior.
Commercial and industrial analog simulators (such as SPICE) have added many other device models as technology advanced and earlier models became inaccurate. To attempt standardization of these models so that a set of model parameters may be used in different simulators, an industry working group was formed, the Compact Model Coalition, to choose, maintain, and promote the use of standard models. BSIM models, developed at UC Berkeley, are one of these standards. Other models supported by the council are PSP, HICUM, and MEXTRAM .
BSIM models
The transistor models developed and currently maintained by UC Berkeley are:
BSIM-CMG (Common Multi-Gate),
BSIM-IMG (Independent Multi-Gate), the only model published without source-code (whose publication is foreseen for July 13, 2021)
BSIM-SOI (Silicon-on-Insulator),
BSIM-BULK, formerly BSIM6,
BSIM4, used for 0.13 μm to 20 nm nodes,
BSIM3, a predecessor of BSIM4 |
https://en.wikipedia.org/wiki/Linamarin%20synthase | In enzymology, a linamarin synthase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + 2-hydroxy-2-methylpropanenitrile UDP + linamarin
Thus, the two substrates of this enzyme are UDP-glucose and 2-hydroxy-2-methylpropanenitrile, whereas its two products are UDP and linamarin.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:2-hydroxy-2-methylpropanenitrile beta-D-glucosyltransferase. Other names in common use include uridine diphosphoglucose-ketone glucosyltransferase, uridine diphosphate-glucose-ketone cyanohydrin, beta-glucosyltransferase, UDP glucose ketone cyanohydrin glucosyltransferase, UDP-glucose:ketone cyanohydrin beta-glucosyltransferase, and uridine diphosphoglucose-ketone cyanohydrin glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lipid-A-disaccharide%20synthase | In enzymology, a lipid-A-disaccharide synthase () is an enzyme that catalyzes the chemical reaction
UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + 2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate UDP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate
Thus, the two substrates of this enzyme are UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine and 2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate, whereas its 2 products are UDP and 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine:2,3-bis(3-hydroxytet radecanoyl)-beta-D-glucosaminyl-1-phosphate 2,3-bis(3-hydroxytetradecanoyl)-glucosaminyltransferase. This enzyme participates in lipopolysaccharide biosynthesis.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lipopolysaccharide%203-alpha-galactosyltransferase | In enzymology, a lipopolysaccharide 3-alpha-galactosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-galactose + lipopolysaccharide UDP + 3-alpha-D-galactosyl-[lipopolysaccharide glucose]
Thus, the two substrates of this enzyme are UDP-galactose and lipopolysaccharide, whereas its two products are UDP and [[3-alpha-D-galactosyl-[lipopolysaccharide glucose]]].
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:lipopolysaccharide 3-alpha-D-galactosyltransferase. Other names in common use include UDP-galactose:lipopolysaccharide alpha,3-galactosyltransferase, UDP-galactose:polysaccharide galactosyltransferase, uridine diphosphate galactose:lipopolysaccharide, alpha-3-galactosyltransferase, uridine diphosphogalactose-lipopolysaccharide, and alpha,3-galactosyltransferase. This enzyme participates in lipopolysaccharide biosynthesis and glycan structures - biosynthesis 2.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.4.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Lipopolysaccharide%20glucosyltransferase%20I | In enzymology, a lipopolysaccharide glucosyltransferase I () is an enzyme that catalyzes the chemical reaction
UDP-glucose + lipopolysaccharide UDP + D-glucosyl-lipopolysaccharide
Thus, the two substrates of this enzyme are UDP-glucose and lipopolysaccharide, whereas its two products are UDP and D-glucosyl-lipopolysaccharide.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:lipopolysaccharide glucosyltransferase. Other names in common use include UDP-glucose:lipopolysaccharide glucosyltransferase I, lipopolysaccharide glucosyltransferase, uridine diphosphate glucose:lipopolysaccharide glucosyltransferase, I, and uridine diphosphoglucose-lipopolysaccharide glucosyltransferase. This enzyme participates in lipopolysaccharide biosynthesis and glycan structures - biosynthesis 2.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lipopolysaccharide%20glucosyltransferase%20II | In enzymology, a lipopolysaccharide glucosyltransferase II () is an enzyme that catalyzes the chemical reaction
UDP-glucose + lipopolysaccharide UDP + alpha-D-glucosyl-lipopolysaccharide
Thus, the two substrates of this enzyme are UDP-glucose and lipopolysaccharide, whereas its two products are UDP and alpha-D-glucosyl-lipopolysaccharide.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:galactosyl-lipopolysaccharide alpha-D-glucosyltransferase. Other names in common use include uridine diphosphoglucose-galactosylpolysaccharide, and glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lipopolysaccharide%20N-acetylglucosaminyltransferase | In enzymology, a lipopolysaccharide N-acetylglucosaminyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-N-acetyl-D-glucosamine + lipopolysaccharide UDP + N-acetyl-D-glucosaminyllipopolysaccharide
Thus, the two substrates of this enzyme are UDP-N-acetyl-D-glucosamine and lipopolysaccharide, whereas its two products are UDP and N-acetyl-D-glucosaminyllipopolysaccharide.
This enzyme participates in lipopolysaccharide biosynthesis and glycan structures - biosynthesis 2.
Nomenclature
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:lipopolysaccharide N-acetyl-D-glucosaminyltransferase. Other names in common use include UDP-N-acetylglucosamine-lipopolysaccharide, N-acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-lipopolysaccharide, and acetylglucosaminyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lipopolysaccharide%20N-acetylmannosaminouronosyltransferase | In enzymology, a lipopolysaccharide N-acetylmannosaminouronosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-N-acetyl-beta-D-mannosaminouronate + lipopolysaccharide UDP + N-acetyl-beta-D-mannosaminouronosyl-1,4-lipopolysaccharide
Thus, the two substrates of this enzyme are UDP-N-acetyl-beta-D-mannosaminouronate and lipopolysaccharide, whereas its two products are UDP and N-acetyl-beta-D-mannosaminouronosyl-1,4-lipopolysaccharide.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-N-acetyl-beta-D-mannosaminouronate:lipopolysaccharide N-acetyl-beta-D-mannosaminouronosyltransferase. Other names in common use include ManNAcA transferase, uridine-diphosphoacetylmannosaminuronatetranferase, N-acetylglucosaminylpyrophosphorylundecaprenol glucosyltransferase, and acetylmannosaminuronosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Luteolin-7-O-diglucuronide%204%27-O-glucuronosyltransferase | In enzymology, a luteolin-7-O-diglucuronide 4'-O-glucuronosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucuronate + luteolin 7-O-beta-D-diglucuronide UDP + luteolin 7-O-[beta-D-glucuronosyl-(1->2)-beta-D-glucuronide]-4'-O-beta-D- glucuronide
Thus, the two substrates of this enzyme are UDP-glucuronate and luteolin 7-O-beta-D-diglucuronide, whereas its 4 products are UDP, luteolin, [[7-O-[beta-D-glucuronosyl-(1->2)-beta-D-glucuronide]-4'-O-beta-D-]], and glucuronide.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucuronate:luteolin-7-O-beta-D-diglucuronide 4'-O-glucuronosyltransferase. Other names in common use include uridine diphosphoglucuronate-luteolin 7-O-diglucuronide, glucuronosyltransferase, UDP-glucuronate:luteolin 7-O-diglucuronide-glucuronosyltransferase, UDPglucuronate:luteolin, 7-O-diglucuronide-4'-O-glucuronosyl-transferase, and LDT.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Luteolin-7-O-glucuronide%202%22-O-glucuronosyltransferase | In enzymology, a luteolin-7-O-glucuronide 2"-O-glucuronosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucuronate + luteolin 7-O-beta-D-glucuronide UDP + luteolin 7-O-[beta-D-glucuronosyl-(1→2)-beta-D-glucuronide]
Thus, the two substrates of this enzyme are UDP-glucuronate and luteolin 7-O-beta-D-glucuronide, whereas its two products are UDP and luteolin 7-O-(beta-D-glucuronosyl-(1→2)-beta-D-glucuronide).
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucuronate:luteolin-7-O-beta-D-glucuronide 2''-O-glucuronosyltransferase. Other names in common use include uridine diphosphoglucuronate-luteolin 7-O-glucuronide, glucuronosyltransferase, LMT, and UDP-glucuronate:luteolin 7-O-glucuronide-glucuronosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Luteolin%207-O-glucuronosyltransferase | In enzymology, a luteolin 7-O-glucuronosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucuronate + luteolin UDP + luteolin 7-O-beta-D-glucuronide
Thus, the two substrates of this enzyme are UDP-glucuronate and luteolin, whereas its two products are UDP and luteolin 7-O-beta-D-glucuronide.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucuronate:luteolin 7-O-glucuronosyltransferase. Other names in common use include uridine diphosphoglucuronate-luteolin 7-O-glucuronosyltransferase, and LGT.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Maltose%20phosphorylase | In enzymology, a maltose phosphorylase () is an enzyme that catalyzes the chemical reaction
maltose + phosphate D-glucose + beta-D-glucose 1-phosphate
Thus, the two substrates of this enzyme are maltose and phosphate, whereas its two products are D-glucose 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 maltose:phosphate 1-beta-D-glucosyltransferase. This enzyme participates in starch and sucrose metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 5, Academic Press, New York, 1961, p. 229-236.
EC 2.4.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Maltose%20synthase | In enzymology, a maltose synthase () is an enzyme that catalyzes the chemical reaction
2 alpha-D-glucose 1-phosphate + H2O maltose + 2 phosphate
Thus, the two substrates of this enzyme are alpha-D-glucose 1-phosphate and H2O, whereas its two products are maltose and phosphate.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is alpha-D-glucose-1-phosphate:alpha-D-glucose-1-phosphate 4-alpha-D-glucosyltransferase (dephosphorylating).
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Mannosyl-3-phosphoglycerate%20synthase | In enzymology, a mannosyl-3-phosphoglycerate synthase () is an enzyme that catalyzes the chemical reaction
GDP-mannose + 3-phospho-D-glycerate GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Thus, the two substrates of this enzyme are GDP-mannose and 3-phospho-D-glycerate, whereas its two products are GDP and 2-(alpha-D-mannosyl)-3-phosphoglycerate.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is GDP-mannose:3-phosphoglycerate 3-alpha-D-mannosyltransferase. This enzyme is also called MPG synthase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Mannotetraose%202-alpha-N-acetylglucosaminyltransferase | In enzymology, a mannotetraose 2-alpha-N-acetylglucosaminyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-N-acetyl-D-glucosamine + 1,3-alpha-D-mannosyl-1,2-alpha-D-mannosyl-1,2-alpha-D-mannosyl-D-mannose UDP + 1,3-alpha-D-mannosyl-1,2-(N-acetyl-alpha-D-glucosaminyl-alpha-D-mannosyl)-1,2-alpha-D-mannosyl-D-mannose
The 2 substrates of this enzyme are UDP-N-acetyl-D-glucosamine and 1,3-alpha-D-mannosyl-1,2-alpha-D-mannosyl-1,2-alpha-D-mannosyl-D-mannose, whereas its 2 products are UDP and 1,3-alpha-D-mannosyl-1,2-(N-acetyl-alpha-D-glucosaminyl-alpha-D-mannosyl)-1,2-alpha-D-mannosyl-D-mannose.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:mannotetraose alpha-N-acetyl-D-glucosaminyltransferase. Other names in common use include alpha-N-acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine mannoside, and alpha1->2-alphacetylglucosaminyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Methyl-ONN-azoxymethanol%20beta-D-glucosyltransferase | In enzymology, a methyl-ONN-azoxymethanol beta-D-glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + methyl-ONN-azoxymethanol UDP + cycasin
Thus, the two substrates of this enzyme are UDP-glucose and methyl-ONN-azoxymethanol, whereas its two products are UDP and cycasin.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:methyl-ONN-azoxymethanol beta-D-glucosyltransferase. Other names in common use include cycasin synthase, uridine diphosphoglucose-methylazoxymethanol glucosyltransferase, and UDP-glucose-methylazoxymethanol glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Monogalactosyldiacylglycerol%20synthase | In enzymology, a monogalactosyldiacylglycerol synthase () is an enzyme that catalyzes the chemical reaction
UDP-galactose + 1,2-diacyl-sn-glycerol UDP + 3-beta-D-galactosyl-1,2-diacyl-sn-glycerol
Thus, the two substrates of this enzyme are UDP-galactose and 1,2-diacyl-sn-glycerol, whereas its two products are UDP and 3-beta-D-galactosyl-1,2-diacyl-sn-glycerol.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:1,2-diacyl-sn-glycerol 3-beta-D-galactosyltransferase. Other names in common use include uridine diphosphogalactose-1,2-diacylglycerol galactosyltransferase, UDP-galactose:diacylglycerol galactosyltransferase, MGDG synthase, UDP galactose-1,2-diacylglycerol galactosyltransferase, UDP-galactose-diacylglyceride galactosyltransferase, UDP-galactose:1,2-diacylglycerol 3-beta-D-galactosyltransferase, 1beta-MGDG, and 1,2-diacylglycerol 3-beta-galactosyltransferase. This enzyme participates in glycerolipid metabolism.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Monosialoganglioside%20sialyltransferase | In enzymology, a monosialoganglioside sialyltransferase () is an enzyme that catalyzes the chemical reaction
CMP-N-acetylneuraminate + D-galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide CMP + N-acetylneuraminyl-D-galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide
The 2 substrates of this enzyme are CMP-N-acetylneuraminate and D-galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide, whereas its 2 products are CMP and N-acetylneuraminyl-D-galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide.
This enzyme belongs to the family of transferases, specifically those glycosyltransferases that do not transfer hexosyl or pentosyl groups. The systematic name of this enzyme class is CMP-N-acetylneuraminate:D-galactosyl-N-acetyl-D-galactosaminyl-(N-ac etylneuraminyl)-D-galactosyl-D-glucosylceramide N-acetylneuraminyltransferase.
References
EC 2.4.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Monoterpenol%20beta-glucosyltransferase | In enzymology, a monoterpenol beta-glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + (-)-menthol UDP + (-)-menthyl O-beta-D-glucoside
Thus, the two substrates of this enzyme are UDP-glucose and (-)-menthol, whereas its two products are UDP and (-)-menthyl 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:(-)-menthol O-beta-D-glucosyltransferase. Other names in common use include uridine diphosphoglucose-monoterpenol glucosyltransferase, and UDPglucose:monoterpenol glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-acetylgalactosaminyl-proteoglycan%203-beta-glucuronosyltransferase | In enzymology, a N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-alpha-D-glucuronate + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl- proteoglycan UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)- beta-D-glucuronosyl-proteoglycan
The 3 substrates of this enzyme are UDP-alpha-D-glucuronate, [[N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-]], and proteoglycan, whereas its 3 products are UDP, [[beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)-]], and beta-D-glucuronosyl-proteoglycan.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is alpha-D-glucuronate:N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glu curonosyl-proteoglycan 3-beta-glucuronosyltransferase. This enzyme is also called chondroitin glucuronyltransferase II. This enzyme participates in chondroitin sulfate biosynthesis and glycan structures - biosynthesis 1.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-acetylglucosaminyldiphosphoundecaprenol%20glucosyltransferase | In enzymology, a N-acetylglucosaminyldiphosphoundecaprenol glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + N-acetyl-D-glucosaminyldiphosphoundecaprenol UDP + beta-D-glucosyl-1,4-N-acetyl-D-glucosaminyldiphosphoundecaprenol
Thus, the two substrates of this enzyme are UDP-glucose and N-acetyl-D-glucosaminyldiphosphoundecaprenol, whereas its two products are UDP and beta-D-glucosyl-1,4-N-acetyl-D-glucosaminyldiphosphoundecaprenol.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:N-acetyl-D-glucosaminyldiphosphoundecaprenol 4-beta-D-glucosyltransferase. Other names in common use include UDP-D-glucose:N-acetylglucosaminyl pyrophosphorylundecaprenol, glucosyltransferase, uridine, diphosphoglucose-acetylglucosaminylpyrophosphorylundecaprenol, and glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-acetylglucosaminyl-proteoglycan%204-beta-glucuronosyltransferase | In enzymology, a N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl- proteoglycan UDP + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-(1->4)- beta-D-glucuronosyl-proteoglycan
The 3 substrates of this enzyme are UDP-alpha-D-glucuronate, [[N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-]], and proteoglycan, whereas its 3 products are UDP, [[beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-(1->4)-]], and beta-D-glucuronosyl-proteoglycan.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-alpha-D-glucuronate:N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D- glucuronosyl-proteoglycan 4-beta-glucuronosyltransferase. Other names in common use include N-acetylglucosaminylproteoglycan beta-1,4-glucuronyltransferase, and heparan glucuronyltransferase II. This enzyme participates in heparan sulfate biosynthesis and glycan structures - biosynthesis 1.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-acetyllactosaminide%203-alpha-galactosyltransferase | In enzymology, a N-acetyllactosaminide 3-alpha-galactosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N- acetylglucosaminyl-R
Thus, the two substrates of this enzyme are UDP-galactose and [[beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R]], whereas its 3 products are UDP, [[alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-]], and acetylglucosaminyl-R.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:N-acetyllactosaminide 3-alpha-D-galactosyltransferase. Other names in common use include alpha-galactosyltransferase, UDP-Gal:beta-D-Gal(1,4)-D-GlcNAc alpha(1,3)-galactosyltransferase, UDP-Gal:N-acetyllactosaminide alpha(1,3)-galactosyltransferase, UDP-Gal:N-acetyllactosaminide alpha-1,3-D-galactosyltransferase, UDP-Gal:Galbeta1->4GlcNAc-R alpha1->3-galactosyltransferase, UDP-galactose-acetyllactosamine alpha-D-galactosyltransferase, UDPgalactose:beta-D-galactosyl-beta-1,4-N-acetyl-D-glucosaminyl-, glycopeptide alpha-1,3-D-galactosyltransferase, glucosaminylglycopeptide alpha-1,3-galactosyltransferase, uridine diphosphogalactose-acetyllactosamine, alpha1->3-galactosyltransferase, uridine diphosphogalactose-acetyllactosamine galactosyltransferase, uridine, diphosphogalactose-, galactosylacetylglucosaminyl |
https://en.wikipedia.org/wiki/N-acetyllactosaminide%20alpha-2%2C3-sialyltransferase | In enzymology, a N-acetyllactosaminide alpha-2,3-sialyltransferase () is an enzyme that catalyzes the chemical reaction
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N-acetyl-D- glucosaminyl-glycoprotein
Thus, the two substrates of this enzyme are CMP-N-acetylneuraminate and beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein, whereas its 3 products are CMP, alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N-acetyl-D-, and glucosaminyl-glycoprotein.
This enzyme belongs to the family of transferases, specifically those glycosyltransferases that do not transfer hexosyl or pentosyl groups. The systematic name of this enzyme class is CMP-N-acetylneuraminate:beta-D-galactosyl-1,4-N-acetyl-D-glucosaminy l-glycoprotein alpha-2,3-N-acetylneuraminyltransferase. Other names in common use include sialyltransferase, cytidine, monophosphoacetylneuraminate-beta-galactosyl(1-, >4)acetylglucosaminide alpha2->3-sialyltransferase, alpha2->3 sialyltransferase, and SiaT. This enzyme participates in 4 metabolic pathways: keratan sulfate biosynthesis, glycosphingolipid biosynthesis - lactoseries, glycan structures - biosynthesis 1, and glycan structures - biosynthesis 2.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.4.99
Enzymes of known structure |
https://en.wikipedia.org/wiki/N-acetyllactosaminide%20beta-1%2C3-N-acetylglucosaminyltransferase | In enzymology, a N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D- glucosaminyl-R
Thus, the two substrates of this enzyme are UDP-N-acetyl-D-glucosamine and beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R, whereas its 3 products are UDP, N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-, and glucosaminyl-R.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:beta-D-galactosyl-1,4-N-acetyl-D-glucosam ine beta-1,3-acetyl-D-glucosaminyltransferase. Other names in common use include uridine diphosphoacetylglucosamine-acetyllactosaminide, beta1->3-acetylglucosaminyltransferase, poly-N-acetyllactosamine extension enzyme, Galbeta1->4GlcNAc-R beta1->3 N-acetylglucosaminyltransferase, UDP-GlcNAc:GalR, beta-D-3-N-acetylglucosaminyltransferase, N-acetyllactosamine beta(1-3)N-acetylglucosaminyltransferase, UDP-GlcNAc:Galbeta1->4GlcNAcbeta-Rbeta1->3-N-, acetylglucosaminyltransferase, and GnTE. This enzyme participates in 4 metabolic pathways: keratan sulfate biosynthesis, glycosphingolipid biosynthesis - neo-lactoseries, glycan structures - biosynthesis 1, and glycan structures - biosynthesis 2.
References
EC 2.4.1
Enzymes of unknown |
https://en.wikipedia.org/wiki/N-acetyllactosaminide%20beta-1%2C6-N-acetylglucosaminyl-transferase | In enzymology, a N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase () is an enzyme that catalyzes the chemical reaction
UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R UDP + N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D- glucosaminyl-R
Thus, the two substrates of this enzyme are UDP-N-acetyl-D-glucosamine and beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R, whereas its 3 products are UDP, N-acetyl-beta-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-, and glucosaminyl-R.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:beta-D-galactosyl-1,4-N-acetyl-D-glucosaminide beta-1,6-N-acetyl-D-glucosaminyltransferase. Other names in common use include N-acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-acetyllactosaminide, beta1->6-acetylglucosaminyltransferase, Galbeta1->4GlcNAc-R beta1->6 N-acetylglucosaminyltransferase, and UDP-GlcNAc:Gal-R, beta-D-6-N-acetylglucosaminyltransferase. This enzyme participates in glycosphingolipid biosynthesis - neo-lactoseries and glycan structures - biosynthesis 2.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-acylsphingosine%20galactosyltransferase | In enzymology, a N-acylsphingosine galactosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-galactose + N-acylsphingosine UDP + D-galactosylceramide
Thus, the two substrates of this enzyme are UDP-galactose and N-acylsphingosine, whereas its two products are UDP and D-galactosylceramide.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:N-acylsphingosine D-galactosyltransferase. Other names in common use include UDP galactose-N-acylsphingosine galactosyltransferase, and uridine diphosphogalactose-acylsphingosine galactosyltransferase. This enzyme participates in sphingolipid metabolism.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/NAD%28%2B%29%E2%80%94dinitrogen-reductase%20ADP-D-ribosyltransferase | In enzymology, a NAD+-dinitrogen-reductase ADP-D-ribosyltransferase () is an enzyme that catalyzes the chemical reaction
NAD+ + [dinitrogen reductase] nicotinamide + ADP-D-ribosyl-[dinitrogen reductase]
Thus, the two substrates of this enzyme are NAD+ and dinitrogen reductase, whereas its two products are nicotinamide and ADP-D-ribosyl-[dinitrogen reductase].
This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is NAD+:[dinitrogen reductase] (ADP-D-ribosyl)transferase. Other names in common use include NAD-azoferredoxin (ADPribose)transferase, and NAD-dinitrogen-reductase ADP-D-ribosyltransferase.
References
EC 2.4.2
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/NAD%28%2B%29%E2%80%94diphthamide%20ADP-ribosyltransferase | In enzymology, a NAD+-diphthamide ADP-ribosyltransferase () is an enzyme that catalyzes the chemical reaction
NAD+ + peptide diphthamide nicotinamide + peptide N-(ADP-D-ribosyl)diphthamide
Thus, the two substrates of this enzyme are NAD+ and peptide diphthamide, whereas its two products are nicotinamide and peptide N-(ADP-D-ribosyl)diphthamide.
This enzyme belongs to the family of glycosyltransferases, to be specific, the pentosyltransferases. The systematic name of this enzyme class is NAD+:peptide-diphthamide N-(ADP-D-ribosyl)transferase. Other names in common use include ADP-ribosyltransferase, mono(ADPribosyl)transferase, and NAD-diphthamide ADP-ribosyltransferase.
Structural studies
As of late 2007, 15 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , and .
Clinical significance
The extracellular ADP-ribosyl-transferase ART2 is expressed only on T cells. T cell activation of P2X7 receptors can activate the T cells or cause T cell differentiation, can affect T cell migration or (at high extracellular levels of NAD+) can induce cell death by ART2.
References
See also
Diphtheria toxin
Pseudomonas exotoxin
ADP-ribosylation
EC 2.4.2
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/NDP-glucose%E2%80%94starch%20glucosyltransferase | In enzymology, a NDP-glucose—starch glucosyltransferase () is an enzyme that catalyzes the chemical reaction
NDP-glucose + (1,4-alpha-D-glucosyl)n NDP + (1,4-alpha-D-glucosyl)n+1
Thus, the two substrates of this enzyme are NDP-glucose and (1,4-alpha-D-glucosyl)n, whereas its two products are NDP and (1,4-alpha-D-glucosyl)n+1.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is NDP-glucose:1,4-alpha-D-glucan 4-alpha-D-glucosyltransferase. Other names in common use include granule-bound starch synthase, starch synthase II (ambiguous), waxy protein, starch granule-bound nucleoside diphosphate glucose-starch, glucosyltransferase, granule-bound starch synthase I, GBSSI, granule-bound starch synthase II, GBSSII, GBSS, and NDPglucose-starch glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Neolactotetraosylceramide%20alpha-2%2C3-sialyltransferase | In enzymology, a neolactotetraosylceramide alpha-2,3-sialyltransferase () is an enzyme that catalyzes the chemical reaction
CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D- galactosyl-1,4-D-glucosylceramide CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N-acetyl-beta-D- glucosaminyl-1,3-beta-D-galactosyl-1,4-D-glucosylceramide
The 3 substrates of this enzyme are CMP-N-acetylneuraminate, beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-, and galactosyl-1,4-D-glucosylceramide, whereas its 3 products are CMP, alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N-acetyl-beta-D-, and glucosaminyl-1,3-beta-D-galactosyl-1,4-D-glucosylceramide.
This enzyme belongs to the family of transferases, specifically those glycosyltransferases that do not transfer hexosyl or pentosyl groups. The systematic name of this enzyme class is CMP-N-acetylneuraminate:neolactotetraosylceramide alpha-2,3-sialyltransferase. Other names in common use include cytidine monophosphoacetylneuraminate-neolactotetraosylceramide, sialyltransferase, sialyltransferase 3, and SAT-3. This enzyme participates in glycosphingolipid biosynthesis - neo-lactoseries and glycan structures - biosynthesis 2.
References
EC 2.4.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-hydroxythioamide%20S-beta-glucosyltransferase | In enzymology, a N-hydroxythioamide S-beta-glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + N-hydroxy-2-phenylethanethioamide UDP + desulfoglucotropeolin
Thus, the two substrates of this enzyme are UDP-glucose and N-hydroxy-2-phenylethanethioamide, whereas its two products are UDP and desulfoglucotropeolin.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:N-hydroxy-2-phenylethanethioamide S-beta-D-glucosyltransferase. Other names in common use include desulfoglucosinolate-uridine diphosphate glucosyltransferase, uridine diphosphoglucose-thiohydroximate glucosyltransferase, thiohydroximate beta-D-glucosyltransferase, UDPG:thiohydroximate glucosyltransferase, thiohydroximate S-glucosyltransferase, thiohydroximate glucosyltransferase, and UDP-glucose:thiohydroximate S-beta-D-glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Nicotinamide%20phosphoribosyltransferase | Nicotinamide phosphoribosyltransferase (NAmPRTase or NAMPT), formerly known as pre-B-cell colony-enhancing factor 1 (PBEF1) or visfatin for its extracellular form (eNAMPT), is an enzyme that in humans is encoded by the NAMPT gene. The intracellular form of this protein (iNAMPT) is the rate-limiting enzyme in the nicotinamide adenine dinucleotide (NAD+) salvage pathway that converts nicotinamide to nicotinamide mononucleotide (NMN) which is responsible for most of the NAD+ formation in mammals. iNAMPT can also catalyze the synthesis of NMN from phosphoribosyl pyrophosphate (PRPP) when ATP is present. eNAMPT has been reported to be a cytokine (PBEF) that activates TLR4, that promotes B cell maturation, and that inhibits neutrophil apoptosis.
Reaction
iNAMPT catalyzes the following chemical reaction:
nicotinamide + 5-phosphoribosyl-1-pyrophosphate (PRPP) nicotinamide mononucleotide (NMN) + pyrophosphate (PPi)
Thus, the two substrates of this enzyme are nicotinamide and 5-phosphoribosyl-1-pyrophosphate (PRRP), whereas its two products are nicotinamide mononucleotide and pyrophosphate.
This enzyme belongs to the family of glycosyltransferases, to be specific, the pentosyltransferases. This enzyme participates in nicotinate and nicotinamide metabolism.
Expression and regulation
The liver has the highest iNAMPT activity of any organ, about 10-20 times greater activity than kidney, spleen, heart, muscle, brain or lung. iNAMPT is downregulated by an increase of miR-34a in obes |
https://en.wikipedia.org/wiki/Nicotinate%20glucosyltransferase | In enzymology, a nicotinate glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + nicotinate UDP + N-glucosylnicotinate
Thus, the two substrates of this enzyme are UDP-glucose and nicotinate, whereas its two products are UDP and N-glucosylnicotinate.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:nicotinate N-glucosyltransferase. Other names in common use include uridine diphosphoglucose-nicotinate N-glucosyltransferase, and UDP-glucose:nicotinic acid-N-glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Nicotinate-nucleotide%E2%80%94dimethylbenzimidazole%20phosphoribosyltransferase | In enzymology, a nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase () is an enzyme that catalyzes the chemical reaction
beta-nicotinate D-ribonucleotide + 5,6-dimethylbenzimidazole nicotinate + alpha-ribazole 5'-phosphate
Thus, the two substrates of this enzyme are beta-nicotinate D-ribonucleotide and 5,6-dimethylbenzimidazole, whereas its two products are nicotinate and alpha-ribazole 5'-phosphate.
This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is nicotinate-nucleotide:5,6-dimethylbenzimidazole phospho-D-ribosyltransferase. Other names in common use include CobT, nicotinate mononucleotide-dimethylbenzimidazole phosphoribosyltransferase, nicotinate ribonucleotide:benzimidazole (adenine) phosphoribosyltransferase, nicotinate-nucleotide:dimethylbenzimidazole phospho-D-ribosyltransferase, and nicotinate mononucleotide (NaMN):5,6-dimethylbenzimidazole phosphoribosyltransferase. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in bacteria.
Function
This enzyme plays a central role in the synthesis of alpha-ribazole-5'-phosphate, an intermediate for the lower ligand of cobalamin. It is one of the enzymes of the anaerobic pathway of cobalamin biosynthesis, and one of the four proteins (CobU, CobT, CobC, and CobS) involved in the synthesis of the lower ligand and the assembly of the nucleotide loop.
Biosynthesis of cobalamin
Vitamin B12 (c |
https://en.wikipedia.org/wiki/Nicotinate-nucleotide%20diphosphorylase%20%28carboxylating%29 | In enzymology, a nicotinate-nucleotide diphosphorylase (carboxylating) () is an enzyme that catalyzes the chemical reaction
nicotinate D-ribonucleotide + diphosphate + CO2 pyridine-2,3-dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate
The 3 substrates of this enzyme are nicotinate D-ribonucleotide, diphosphate, and CO2, whereas its two products are pyridine-2,3-dicarboxylate and 5-phospho-alpha-D-ribose 1-diphosphate.
This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is nicotinate-nucleotide:diphosphate phospho-alpha-D-ribosyltransferase (carboxylating). Other names in common use include quinolinate phosphoribosyltransferase (decarboxylating), quinolinic acid phosphoribosyltransferase, QAPRTase, NAD+ pyrophosphorylase, nicotinate mononucleotide pyrophosphorylase (carboxylating), and quinolinic phosphoribosyltransferase. This enzyme participates in nicotinate and nicotinamide metabolism.
Structural studies
As of late 2007, 9 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/Nicotinate%20phosphoribosyltransferase | In enzymology, a nicotinate phosphoribosyltransferase () is an enzyme that catalyzes the chemical reaction
nicotinate + 5-phospho-α-D-ribose 1-diphosphate + ATP + H2O nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
Thus, the four substrates of this enzyme are nicotinate, 5-phospho-alpha-D-ribose 1-diphosphate, ATP, and H2O, whereas its four products are nicotinate D-ribonucleotide, diphosphate, ADP, and phosphate.
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of this enzyme class is 5-phospho-alpha-D-ribose 1-diphosphate:nicotinate ligase (ADP, diphosphate-forming) .
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 6.3.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/Nuatigenin%203beta-glucosyltransferase | In enzymology, a nuatigenin 3beta-glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + (20S,22S,25S)-22,25-epoxyfurost-5-ene-3beta,26-diol UDP + (20S,22S,25S)-22,25-epoxyfurost-5-ene-3beta,26-diol 3-O-beta-D-glucoside
Thus, the two substrates of this enzyme are UDP-glucose and (20S,22S,25S)-22,25-epoxyfurost-5-ene-3beta,26-diol, whereas its 3 products are UDP, (20S,22S,25S)-22,25-epoxyfurost-5-ene-3beta,26-diol, and 3-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:(20S,22S,25S)-22,25-epoxyfurost-5-ene-3beta,26-diol 3-O-beta-D-glucosyltransferase. This enzyme is also called uridine diphosphoglucose-nuatigenin glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Nucleoside%20deoxyribosyltransferase | In enzymology, a nucleoside deoxyribosyltransferase () is an enzyme that catalyzes the chemical reaction
2-deoxy-D-ribosyl-base1 + base2 2-deoxy-D-ribosyl-base2 + base1
Thus, the two substrates of this enzyme are 2-deoxy-D-ribosyl-base1 and base2, whereas its two products are 2-deoxy-D-ribosyl-base2 and base1.
This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is nucleoside:purine(pyrimidine) deoxy-D-ribosyltransferase. Other names in common use include purine(pyrimidine) nucleoside:purine(pyrimidine) deoxyribosyl, transferase, deoxyribose transferase, nucleoside trans-N-deoxyribosylase, trans-deoxyribosylase, trans-N-deoxyribosylase, trans-N-glycosidase, nucleoside deoxyribosyltransferase I (purine nucleoside:purine, deoxyribosyltransferase: strictly specific for transfer between, purine bases), nucleoside deoxyribosyltransferase II [purine(pyrimidine), and nucleoside:purine(pyrimidine) deoxyribosyltransferase]. This enzyme participates in pyrimidine metabolism.
Structural studies
As of late 2007, 12 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/Cytochrome%20c%20oxidase%20subunit%202 | Cytochrome c oxidase II is a protein in eukaryotes that is encoded by the MT-CO2 gene. Cytochrome c oxidase subunit II, abbreviated COXII, COX2, COII, or MT-CO2, is the second subunit of cytochrome c oxidase. It is also one of the three mitochondrial DNA (mtDNA) encoded subunits (MT-CO1, MT-CO2, MT-CO3) of respiratory complex IV.
Structure
In humans, the MT-CO2 gene is located on the p arm of mitochondrial DNA at position 12 and it spans 683 base pairs. The MT-CO2 gene produces a 25.6 kDa protein composed of 227 amino acids. MT-CO2 is a subunit of the enzyme Cytochrome c oxidase () (Complex IV), an oligomeric enzymatic complex of the mitochondrial respiratory chain involved in the transfer of electrons from cytochrome c to oxygen. In eukaryotes this enzyme complex is located in the mitochondrial inner membrane; in aerobic prokaryotes it is found in the plasma membrane. The enzyme complex consists of 3-4 subunits (prokaryotes) to up to 13 polypeptides (mammals). The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices. The structure of MT-CO2 is known to contain one redox center and a binuclear copper A center (CuA). The CuA is located in a conserved cysteine loop at 196 and 200 amino acid positions and conserved histidine at 204. Several bacterial MT-CO2 have a C-terminal extension that contains a covalently bound haem c.
Function
The MT-CO2 gene encodes for the second subunit of cytochrome c oxidase (complex IV), a component of the mitochond |
https://en.wikipedia.org/wiki/Nucleoside%20ribosyltransferase | In enzymology, a nucleoside ribosyltransferase () is an enzyme that catalyzes the chemical reaction
D-ribosyl-base1 + base2 D-ribosyl-base2 + base1
Thus, the two substrates of this enzyme are D-ribosyl-base1 and base2, whereas its two products are D-ribosyl-base2 and base1.
This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is nucleoside:purine(pyrimidine) D-ribosyltransferase. This enzyme is also called nucleoside N-ribosyltransferase.
References
EC 2.4.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/O-dihydroxycoumarin%207-O-glucosyltransferase | In enzymology, an o-dihydroxycoumarin 7-O-glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + 7,8-dihydroxycoumarin UDP + daphnin
Thus, the two substrates of this enzyme are UDP-glucose and 7,8-dihydroxycoumarin, whereas its two products are UDP and daphnin.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:7,8-dihydroxycoumarin 7-O-beta-D-glucosyltransferase. Other names in common use include uridine diphosphoglucose-o-dihydroxycoumarin, 7-O-glucosyltransferase, and UDP-glucose:o-dihydroxycoumarin glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Peptidoglycan%20glycosyltransferase | Peptidoglycan glycosyltransferase () is an enzyme used in the biosynthesis of peptidoglycan. It transfers a disaccharide-peptide from a donor substrate to synthesize a glycan chain.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-(1->4)-(N-acetyl-D-mu ramoylpentapeptide):undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-( 1->4)-N-acetyl-D-muramoylpentapeptide) disaccharidetransferase. Other names in common use include PG-II, bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)-, pentapeptide:peptidoglycan, N-acetylmuramoyl-N-acetyl-D-glucosaminyltransferase, penicillin binding protein (3 or 1B), and peptidoglycan transglycosylase.
Function
Peptidoglycan glycosyltransferase couples Lipid II subunits to synthesize the peptidoglycan chains. Transpeptidases crosslink the carbohydrate chains to provide the framework for the cell wall.
It catalyzes the chemical reaction
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
⇌
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1- diphosphoundecaprenol + undecaprenyl diphosphate
The 2 substrates of this enzyme are
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol,
GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys |
https://en.wikipedia.org/wiki/Phenol%20beta-glucosyltransferase | In enzymology, a phenol beta-glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + a phenol UDP + an aryl beta-D-glucoside
Thus, the two substrates of this enzyme are UDP-glucose and phenol, whereas its two products are UDP and aryl beta-D-glucoside.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:phenol beta-D-glucosyltransferase. Other names in common use include UDPglucosyltransferase, phenol-beta-D-glucosyltransferase, UDP glucosyltransferase, UDP-glucose glucosyltransferase, and uridine diphosphoglucosyltransferase. This enzyme participates in starch and sucrose metabolism.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphatidylinositol%20N-acetylglucosaminyltransferase | In enzymology, a phosphatidylinositol N-acetylglucosaminyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-N-acetylglucosamine + phosphatidylinositol UDP + N-acetyl-D-glucosaminylphosphatidylinositol
Thus, the two substrates of this enzyme are UDP-N-acetylglucosamine and phosphatidylinositol, whereas its two products are UDP and N-acetyl-D-glucosaminylphosphatidylinositol.
The mammalian enzyme is composed of at least six subunits (PIG-A, PIG-H, PIG-C, PIG-P, PIG-Y, and GPI1). PIG-A is the catalytic subunit.
This enzyme belongs to the family of glycosyltransferases, to be specific the hexosyltransferases. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:1-phosphatidyl-1D-myo-inositol 6-(N-acetyl-alpha-D-glucosaminyl)transferase. Other names in common use include UDP-N-acetyl-D-glucosamine:phosphatidylinositol, N-acetyl-D-glucosaminyltransferase, uridine diphosphoacetylglucosamine, and alpha1,6-acetyl-D-glucosaminyltransferase. This enzyme participates in 3 metabolic pathways: glycosylphosphatidylinositol(gpi)-anchor, ???, and glycan structures - biosynthesis 2.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphopolyprenol%20glucosyltransferase | In enzymology, a phosphopolyprenol glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + polyprenyl phosphate UDP + polyprenylphosphate-glucose
Thus, the two substrates of this enzyme are UDP-glucose and polyprenyl phosphate, whereas its two products are UDP and polyprenylphosphate-glucose.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:phosphopolyprenol D-glucosyltransferase. Other names in common use include uridine diphosphoglucose-polyprenol monophosphate, glucosyltransferase, and UDP-glucose:polyprenol monophosphate glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Polygalacturonate%204-alpha-galacturonosyltransferase | In enzymology, a polygalacturonate 4-alpha-galacturonosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-D-galacturonate + (1,4-alpha-D-galacturonosyl)n UDP + (1,4-alpha-D-galacturonosyl)n+1
Thus, the two substrates of this enzyme are UDP-D-galacturonate and (1,4-alpha-D-galacturonosyl)n, whereas its two products are UDP and (1,4-alpha-D-galacturonosyl)n+1.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-D-galacturonate:1,4-alpha-poly-D-galacturonate 4-alpha-D-galacturonosyltransferase. Other names in common use include UDP galacturonate-polygalacturonate alpha-galacturonosyltransferase, uridine diphosphogalacturonate-polygalacturonate, and alpha-galacturonosyltransferase. This enzyme participates in starch and sucrose metabolism and nucleotide sugars metabolism.
Indications
Polygalacturonate salts can be used clinically to treat the GI reactions that are due to Quinidine.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Poly%28glycerol-phosphate%29%20alpha-glucosyltransferase | In enzymology, a poly(glycerol-phosphate) alpha-glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + poly(glycerol phosphate) UDP + O-(alpha-D-glucosyl)poly(glycerol phosphate)
Thus, the two substrates of this enzyme are UDP-glucose and poly(glycerol phosphate), whereas its two products are UDP and O-(alpha-D-glucosyl)poly(glycerol phosphate).
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:poly(glycerol-phosphate) alpha-D-glucosyltransferase. Other names in common use include UDP glucose-poly(glycerol-phosphate) alpha-glucosyltransferase, uridine diphosphoglucose-poly(glycerol-phosphate), and alpha-glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Polypeptide%20N-acetylgalactosaminyltransferase | In enzymology, a polypeptide N-acetylgalactosaminyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-N-acetyl-D-galactosamine + polypeptide UDP + N-acetyl-D-galactosaminyl-polypeptide
Thus, the two substrates of this enzyme are UDP-N-acetyl-D-galactosamine and polypeptide, whereas its two products are UDP and N-acetyl-D-galactosaminyl-polypeptide.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. This enzyme participates in o-glycan biosynthesis and glycan structures - biosynthesis 1. It has 2 cofactors: manganese, and calcium.
Nomenclature
The systematic name of this enzyme class is UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyl-transferase. Other names in common use include:
protein-UDP acetylgalactosaminyltransferase,
UDP-GalNAc:polypeptide N-acetylgalactosaminyl transferase,
UDP-N-acetylgalactosamine:kappa-casein polypeptide,
N-acetylgalactosaminyltransferase,
uridine diphosphoacetylgalactosamine-glycoprotein,
acetylgalactosaminyltransferase,
glycoprotein acetylgalactosaminyltransferase,
polypeptide-N-acetylgalactosamine transferase,
UDP-acetylgalactosamine-glycoprotein,
acetylgalactosaminyltransferase,
UDP-acetylgalactosamine:peptide-N-galactosaminyltransferase,
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase,
UDP-N-acetyl-alpha-D-galactosamine:polypeptide,
N-acetylgalactosaminyltransferase,
UDP-N-acetylgalactosamine-glycoprotein,
N-acetyl |
https://en.wikipedia.org/wiki/Poly%28ribitol-phosphate%29%20beta-glucosyltransferase | In enzymology, a poly(ribitol-phosphate) beta-glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + poly(ribitol phosphate) UDP + (beta-D-glucosyl)poly(ribitol phosphate)
Thus, the two substrates of this enzyme are UDP-glucose and poly(ribitol phosphate), whereas its two products are UDP and (beta-D-glucosyl)poly(ribitol phosphate).
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:poly(ribitol-phosphate) beta-D-glucosyltransferase. Other names in common use include UDP glucose-poly(ribitol-phosphate) beta-glucosyltransferase, uridine diphosphoglucose-poly(ribitol-phosphate), beta-glucosyltransferase, UDP-D-glucose polyribitol phosphate glucosyl transferase, and UDP-D-glucose:polyribitol phosphate glucosyl transferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Poly%28ribitol-phosphate%29%20N-acetylglucosaminyl-transferase | In enzymology, a poly(ribitol-phosphate) N-acetylglucosaminyl-transferase () is an enzyme that catalyzes the chemical reaction
UDP-N-acetyl-D-glucosamine + poly(ribitol phosphate) UDP + (N-acetyl-D-glucosaminyl)poly(ribitol phosphate)
Thus, the two substrates of this enzyme are UDP-N-acetyl-D-glucosamine and poly(ribitol phosphate), whereas its two products are UDP and (N-acetyl-D-glucosaminyl)poly(ribitol phosphate).
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:poly(ribitol-phosphate) N-acetyl-D-glucosaminyltransferase. Other names in common use include UDP acetylglucosamine-poly(ribitol phosphate), acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-poly(ribitol phosphate), and acetylglucosaminyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Procollagen%20galactosyltransferase | In enzymology, a procollagen galactosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-galactose + procollagen 5-hydroxy-L-lysine UDP + procollagen 5-(D-galactosyloxy)-L-lysine
Thus, the two substrates of this enzyme are UDP-galactose and procollagen 5-hydroxy-L-lysine, whereas its two products are UDP and procollagen 5-(D-galactosyloxy)-L-lysine.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:procollagen-5-hydroxy-L-lysine D-galactosyltransferase. Other names in common use include hydroxylysine galactosyltransferase, collagen galactosyltransferase, collagen hydroxylysyl galactosyltransferase, UDP galactose-collagen galactosyltransferase, uridine diphosphogalactose-collagen galactosyltransferase, and UDPgalactose:5-hydroxylysine-collagen galactosyltransferase. This enzyme participates in lysine degradation.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Procollagen%20glucosyltransferase | In enzymology, a procollagen glucosyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
Thus, the two substrates of this enzyme are UDP-glucose and 5-(D-galactosyloxy)-L-lysine-procollagen, whereas its two products are UDP and 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:5-(D-galactosyloxy)-L-lysine-procollagen D-glucosyltransferase. Other names in common use include galactosylhydroxylysine glucosyltransferase, collagen glucosyltransferase, collagen hydroxylysyl glucosyltransferase, galactosylhydroxylysyl glucosyltransferase, UDP-glucose-collagenglucosyltransferase, and uridine diphosphoglucose-collagen glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
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