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https://en.wikipedia.org/wiki/Inositol-tetrakisphosphate%205-kinase | In enzymology, an inositol-tetrakisphosphate 5-kinase () is an enzyme that catalyzes the chemical reaction
ATP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
Thus, the two substrates of this enzyme are ATP and 1D-myo-inositol 1,3,4,6-tetrakisphosphate, whereas its two products are ADP and 1D-myo-inositol 1,3,4,5,6-pentakisphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:1D-myo-inositol-1,3,4,6-tetrakisphosphate 5-phosphotransferase. This enzyme is also called 1D-myo-inositol-tetrakisphosphate 5-kinase. This enzyme participates in inositol phosphate metabolism and phosphatidylinositol signaling system.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Mass%20point | Mass point may refer to:
Mass point geometry
Point mass in physics
The values of a probability mass function in probability and statistics |
https://en.wikipedia.org/wiki/Inositol-trisphosphate%203-kinase | Inositol (1,4,5) trisphosphate 3-kinase (), abbreviated here as ITP3K, is an enzyme that facilitates a phospho-group transfer from adenosine triphosphate to 1D-myo-inositol 1,4,5-trisphosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:1D-myo-inositol-1,4,5-trisphosphate 3-phosphotransferase. ITP3K catalyzes the transfer of the gamma-phosphate from ATP to the 3-position of inositol 1,4,5-trisphosphate to form inositol 1,3,4,5-tetrakisphosphate. ITP3K is highly specific for the 1,4,5-isomer of IP3, and it exclusively phosphorylates the 3-OH position, producing Ins(1,3,4,5)P4, also known as inositol tetrakisphosphate or IP4.
In biology, the enzyme ITP3K is abbreviated a number of different ways, including 1D-myo-inositol-trisphosphate 3-kinase, ITP3K, ITPK, IP3-kinase, IP3-3-kinase, Ins(1,4,5)P3 3-kinase. In addition the enzyme may be named as the product of one of 3 genes in humans ITPKA, ITPKB, and ITPKC, or one of two in fruit flies, IP3K1 and IP3K2—a mutant known to geneticists as wavy. The nematode genome has one form of the enzyme, coded by the LFE-2 gene. ITP3K enzymes are expressed only in metazoans; they are not expressed in yeast or plants.
All ITP3Ks belong to a larger structural family, the inositol polyphosphate kinases, or IPKs. Note however, that the human genome also contains a gene fo |
https://en.wikipedia.org/wiki/Isocitrate%20dehydrogenase%20%28NADP%2B%29%20kinase | In enzymology, a [isocitrate dehydrogenase (NADP+)] kinase () is an enzyme that catalyzes the chemical reaction:
ATP + [isocitrate dehydrogenase (NADP+)] ADP + [isocitrate dehydrogenase (NADP+)] phosphate
Thus, the two substrates of this enzyme are ATP and isocitrate dehydrogenase (NADP+), whereas its two products are ADP and isocitrate dehydrogenase (NADP+) phosphate.
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases).
Other names
The systematic name of this enzyme class is ATP:[isocitrate dehydrogenase (NADP+)] phosphotransferase. Other names in common use include [isocitrate dehydrogenase (NADP+)] kinase, ICDH kinase/phosphatase, IDH kinase, IDH kinase/phosphatase, IDH-K/P, IDHK/P, isocitrate dehydrogenase kinase (phosphorylating), isocitrate dehydrogenase kinase/phosphatase, and STK3.
References
EC 2.7.11
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Kanamycin%20kinase | Aminoglycoside-3'-phosphotransferase (APH(3')), also known as aminoglycoside kinase, is an enzyme that primarily catalyzes the addition of phosphate from ATP to the 3'-hydroxyl group of a 4,6-disubstituted aminoglycoside, such as kanamycin. However, APH(3') has also been found to phosphorylate at the 5'-hydroxyl group in 4,5-disubstituted aminoglycosides, which lack a 3'-hydroxyl group, and to diphosphorylate hydroxyl groups in aminoglycosides that have both 3'- and 5'-hydroxyl groups. Primarily positively charged at biological conditions, aminoglycosides bind to the negatively charged backbone of nucleic acids to disrupt protein synthesis, effectively inhibiting bacterial cell growth. APH(3') mediated phosphorylation of aminoglycosides effectively disrupts their mechanism of action, introducing a phosphate group that reduces their binding affinity due to steric hindrances and unfavorable electrostatic interactions. APH(3') is primarily found in certain species of gram-positive bacteria.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:kanamycin 3'-O-phosphotransferase. This enzyme is also called neomycin-kanamycin phosphotransferase.
Structure
APH(3') thermodynamically favors a dimer form of two identical APH(3') monomers that are connected by two disulfide bonds between Cys19 and Cys156, with the active si |
https://en.wikipedia.org/wiki/L-arabinokinase | In enzymology, a L-arabinokinase () is an enzyme that catalyzes the chemical reaction
ATP + L-arabinose ADP + beta-L-arabinose 1-phosphate
Thus, the two substrates of this enzyme are ATP and L-arabinose, whereas its two products are ADP and beta-L-arabinose 1-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:L-arabinose 1-phosphotransferase. This enzyme is also called L-arabinokinase (phosphorylating). This enzyme participates in nucleotide sugars metabolism.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-Fuculokinase | {{DISPLAYTITLE:L-Fuculokinase}}
L-Fuculokinase () is an enzyme that catalyzes the chemical reaction
ATP + L-fuculose (L-fuculokinase) ADP + L-fuculose-1-phosphate
Thus, the two substrates of this enzyme are ATP and L-fuculose, whereas its two products are ADP and L-fuculose-1-phosphate.
The gene name used for the gene that encodes L-fuculokinase is fucK.
L-Fuculokinase belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:L-fuculose 1-phosphotransferase. Other names in common use include L-fuculokinase (phosphorylating), and L-fuculose kinase. This enzyme participates in fructose and mannose metabolism.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lombricine%20kinase | In enzymology, a lombricine kinase () is an enzyme that catalyzes the chemical reaction
ATP + lombricine ADP + N-phospholombricine
The two substrates of this enzyme are ATP and lombricine, and the two products are ADP and N-phospholombricine.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:lombricine N-phosphotransferase. This enzyme participates in glycine, serine and threonine metabolism.
References
EC 2.7.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Low-density-lipoprotein%20receptor%20kinase | In enzymology, a low-density-lipoprotein receptor kinase () is an enzyme that catalyzes the chemical reaction
ATP + [low-density-lipoprotein receptor]-L-serine ADP + [low-density-lipoprotein receptor]-O-phospho-L-serine
Thus, the two substrates of this enzyme are ATP and [[[low-density-lipoprotein receptor]-L-serine]], whereas its two products are ADP and [[[low-density-lipoprotein receptor]-O-phospho-L-serine]].
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is ATP:[low-density-lipoprotein receptor]-L-serine O-phosphotransferase. Other names in common use include ATP:low-density-lipoprotein-L-serine O-phosphotransferase, LDL receptor kinase, [low-density-lipoprotein] kinase, low-density lipoprotein kinase, low-density-lipoprotein receptor kinase (phosphorylating), and STK7.
References
EC 2.7.11
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-xylulokinase | In enzymology, a L-xylulokinase () is an enzyme that catalyzes the chemical reaction
ATP + L-xylulose ADP + L-xylulose 5-phosphate
Thus, the two substrates of this enzyme are ATP and L-xylulose, whereas its two products are ADP and L-xylulose 5-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:L-xylulose 5-phosphotransferase. This enzyme is also called L-xylulokinase (phosphorylating). This enzyme participates in pentose and glucuronate interconversions and ascorbate and aldarate metabolism.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Macrolide%202%27-kinase | In enzymology, a macrolide 2'-kinase () is an enzyme that catalyzes the chemical reaction
ATP + oleandomycin ADP + oleandomycin 2'-O-phosphate
Thus, the two substrates of this enzyme are ATP and oleandomycin, whereas its two products are ADP and oleandomycin 2'-O-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:macrolide 2'-O-phosphotransferase.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Mannokinase | In enzymology, a mannokinase () is an enzyme that catalyzes the chemical reaction
ATP + D-mannose ADP + D-mannose 6-phosphate
Thus, the two substrates of this enzyme are ATP and D-mannose, whereas its two products are ADP and D-mannose 6-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-mannose 6-phosphotransferase. Other names in common use include mannokinase (phosphorylating), and D-fructose (D-mannose) kinase. This enzyme participates in fructose and mannose metabolism.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Mannose-1-phosphate%20guanylyltransferase | In enzymology, a mannose-1-phosphate guanylyltransferase () is an enzyme that catalyzes the chemical reaction
GTP + alpha-D-mannose 1-phosphate diphosphate + GDP-mannose
Thus, the two substrates of this enzyme are GTP and alpha-D-mannose 1-phosphate, whereas its two products are diphosphate and GDP-mannose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is GTP:alpha-D-mannose-1-phosphate guanylyltransferase. Other names in common use include GTP-mannose-1-phosphate guanylyltransferase, PIM-GMP (phosphomannose isomerase-guanosine 5'-diphospho-D-mannose, pyrophosphorylase), GDP-mannose pyrophosphorylase, guanosine 5'-diphospho-D-mannose pyrophosphorylase, guanosine diphosphomannose pyrophosphorylase, guanosine triphosphate-mannose 1-phosphate guanylyltransferase, and mannose 1-phosphate guanylyltransferase (guanosine triphosphate). This enzyme participates in fructose and mannose metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 2.7.7
Enzymes of known structure |
https://en.wikipedia.org/wiki/Mannose-1-phosphate%20guanylyltransferase%20%28GDP%29 | In enzymology, a mannose-1-phosphate guanylyltransferase (GDP) () is an enzyme that catalyzes the chemical reaction
GDP + alpha-D-mannose 1-phosphate phosphate + GDP-mannose
Thus, the two substrates of this enzyme are GDP and alpha-D-mannose 1-phosphate, whereas its two products are phosphate and GDP-mannose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is GDP:alpha-D-mannose-1-phosphate guanylyltransferase. This enzyme participates in fructose and mannose metabolism.
Other common names
GDP mannose phosphorylase
Mannose 1-phosphate (guanosine diphosphate) guanylyltransferase
GDP mannose phosphorylase
GDP-mannose 1-phosphate guanylyltransferase
Guanosine diphosphate-mannose 1-phosphate guanylyltransferase
Guanosine diphosphomannose phosphorylase
Mannose 1-phosphate guanylyltransferase
GDP:D-mannose-1-phosphate guanylyltransferase
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Membrane-oligosaccharide%20glycerophosphotransferase | In enzymology, a membrane-oligosaccharide glycerophosphotransferase () is an enzyme that catalyzes the chemical reaction in which a glycerophospho group is transferred from one membrane-derived oligosaccharide to another.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is membrane-derived-oligosaccharide-6-(glycerophospho)-D-glucose:membra ne-derived-oligosaccharide-D-glucose glycerophosphotransferase. Other names in common use include periplasmic phosphoglycerotransferase, and phosphoglycerol cyclase.
References
EC 2.7.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/MRNA%20guanylyltransferase | In enzymology, a mRNA guanylyltransferase () is an enzyme that catalyzes the chemical reaction
GTP + (5')ppPur-mRNA diphosphate + G(5')pppPur-mRNA
Thus, the two substrates of this enzyme are GTP and (5')ppPur-mRNA, whereas its two products are diphosphate and G(5')pppPur-mRNA.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases).op The systematic name of this enzyme class is GTP:mRNA guanylyltransferase. Other names in common use include mRNA capping enzyme, messenger RNA guanylyltransferase, and Protein 2.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
mRNA guanylyltransferase
Enzymes of known structure |
https://en.wikipedia.org/wiki/Myosin-heavy-chain%20kinase | In enzymology, a myosin-heavy-chain kinase () is an enzyme that catalyzes the chemical reaction
ATP + [myosin heavy-chain] ADP + [myosin heavy-chain] phosphate
Thus, the two substrates of this enzyme are ATP and myosin heavy-chain, whereas its two products are ADP and myosin heavy-chain phosphate.
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is ATP:[myosin heavy-chain] O-phosphotransferase. Other names in common use include
ATP:myosin-heavy-chain O-phosphotransferase
calmodulin-dependent myosin heavy chain kinase
MHCK
MIHC kinase
myosin heavy chain kinase
myosin I heavy-chain kinase
myosin II heavy-chain kinase
[myosin-heavy-chain] kinase
myosin heavy chain kinase A
STK6.
References
EC 2.7.11
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-acetylgalactosamine%20kinase | In enzymology, a N-acetylgalactosamine kinase () is an enzyme that catalyzes the chemical reaction
ATP + N-acetyl-D-galactosamine ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
Thus, the two substrates of this enzyme are ATP and N-acetyl-D-galactosamine, whereas its two products are ADP and N-acetyl-alpha-D-galactosamine 1-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:N-acetyl-D-galactosamine 1-phosphotransferase. Other names in common use include GALK2, GK2, GalNAc kinase, and N-acetylgalactosamine (GalNAc)-1-phosphate kinase.
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/N-acetylglucosamine%20kinase | In enzymology, a N-acetylglucosamine kinase () is an enzyme that catalyzes the chemical reaction
ATP + N-acetyl-D-glucosamine ADP + N-acetyl-D-glucosamine 6-phosphate
Thus, the two substrates of this enzyme are ATP and N-acetyl-D-glucosamine, whereas its two products are ADP and N-acetyl-D-glucosamine 6-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:N-acetyl-D-glucosamine 6-phosphotransferase. Other names in common use include acetylglucosamine kinase (phosphorylating), ATP:2-acetylamino-2-deoxy-D-glucose 6-phosphotransferase, 2-acetylamino-2-deoxy-D-glucose kinase, and acetylaminodeoxyglucokinase. This enzyme participates in glutamate metabolism and aminosugars metabolism.
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/N-acylmannosamine%20kinase | In enzymology, a N-acylmannosamine kinase () is an enzyme that catalyzes the chemical reaction
ATP + N-acyl-D-mannosamine ADP + N-acyl-D-mannosamine 6-phosphate
Thus, the two substrates of this enzyme are ATP and N-acyl-D-mannosamine, whereas its two products are ADP and N-acyl-D-mannosamine 6-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:N-acyl-D-mannosamine 6-phosphotransferase. Other names in common use include acylmannosamine kinase (phosphorylating), acetylamidodeoxymannokinase, acetylmannosamine kinase, acylaminodeoxymannokinase, acylmannosamine kinase, N-acyl-D-mannosamine kinase, N-acetylmannosamine kinase, and ATP:N-acetylmannosamine 6-phosphotransferase. This enzyme participates in aminosugars metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/N-acylneuraminate%20cytidylyltransferase | In enzymology, a N-acylneuraminate cytidylyltransferase () is an enzyme that catalyzes the chemical reaction
CTP + N-acylneuraminate diphosphate + CMP-N-acylneuraminate
Thus, the two substrates of this enzyme are CTP and N-acylneuraminate, whereas its two products are diphosphate and CMP-N-acylneuraminate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is CTP:N-acylneuraminate cytidylyltransferase. Other names in common use include CMP-sialate pyrophosphorylase, CMP-sialate synthase, cytidine 5'-monophosphosialic acid synthetase, CMP-Neu5Ac synthetase, CMP-NeuAc synthetase, acylneuraminate cytidyltransferase, CMP-N-acetylneuraminate synthetase, CMP-N-acetylneuraminate synthase, CMP-N-acetylneuraminic acid synthase, CMP-NANA synthetase, CMP-sialate synthetase, CMP-sialic synthetase, cytidine 5'-monophospho-N-acetylneuraminic acid synthetase, cytidine 5-monophosphate N-acetylneuraminic acid synthetase, cytidine monophosphosialic acid synthetase, cytidine monophosphoacetylneuraminic synthetase, cytidine monophosphosialate pyrophosphorylase, cytidine monophosphosialate synthetase, and acetylneuraminate cytidylyltransferase. This enzyme participates in aminosugars metabolism.
Structural studies
As of late 2007, three structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 2.7.7
En |
https://en.wikipedia.org/wiki/NADH%20kinase | In enzymology, a NADH kinase () is an enzyme that catalyzes a chemical reaction.
Explanation
ATP + NADH ADP + NADPH
Thus, the two substrates of this enzyme are ATP and NADH, whereas its two products are ADP and NADPH.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:NADH 2'-phosphotransferase. Other names in common use include reduced nicotinamide adenine dinucleotide kinase (phosphorylating), DPNH kinase, reduced diphosphopyridine nucleotide kinase, and NADH kinase. This enzyme has at least one activator, acetate.
References
EC 2.7.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Nicotinamide-nucleotide%20adenylyltransferase | In enzymology, nicotinamide-nucleotide adenylyltransferase (NMNAT) () are enzymes that catalyzes the chemical reaction
ATP + nicotinamide mononucleotide diphosphate + NAD+
Thus, the two substrates of this enzyme are ATP and nicotinamide mononucleotide (NMN), whereas its two products are diphosphate and NAD+.
This enzyme participates in nicotinate and nicotinamide metabolism.
Humans have three protein isoforms: NMNAT1 (widespread), NMNAT2 (predominantly in brain), and NMNAT3 (highest in liver, heart, skeletal muscle, and erythrocytes). Mutations in the NMNAT1 gene lead to the LCA9 form of Leber congenital amaurosis. Mutations in NMNAT2 or NMNAT3 genes are not known to cause any human disease. NMNAT2 is critical for neurons: loss of NMNAT2 is associated with neurodegeneration. All NMNAT isoforms reportedly decline with age.
Belongs to
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:nicotinamide-nucleotide adenylyltransferase. Other names in common use include NAD+ pyrophosphorylase, adenosine triphosphate-nicotinamide mononucleotide transadenylase, ATP:NMN adenylyltransferase, diphosphopyridine nucleotide pyrophosphorylase, nicotinamide adenine dinucleotide pyrophosphorylase, nicotinamide mononucleotide adenylyltransferase, and NMN adenylyltransferase.
Structural studies
As of late 2007, 11 structures have been solved for |
https://en.wikipedia.org/wiki/Nicotinate-nucleotide%20adenylyltransferase | In enzymology, a nicotinate-nucleotide adenylyltransferase () is an enzyme that catalyzes the chemical reaction
ATP + nicotinate ribonucleotide diphosphate + deamido-NAD+
Thus, the two substrates of this enzyme are ATP and nicotinate ribonucleotide, whereas its two products are diphosphate and deamido-NAD+.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:nicotinate-ribonucleotide adenylyltransferase. Other names in common use include deamido-NAD+ pyrophosphorylase, nicotinate mononucleotide adenylyltransferase, deamidonicotinamide adenine dinucleotide pyrophosphorylase, NaMN-ATase, and nicotinic acid mononucleotide adenylyltransferase. 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 2.7.7
Enzymes of known structure |
https://en.wikipedia.org/wiki/N-methylphosphoethanolamine%20cytidylyltransferase | In enzymology, a N-methylphosphoethanolamine cytidylyltransferase () is an enzyme that catalyzes the chemical reaction
CTP + N-methylethanolamine phosphate diphosphate + CDP-N-methylethanolamine
Thus, the two substrates of this enzyme are CTP and N-methylethanolamine phosphate, whereas its two products are diphosphate and CDP-N-methylethanolamine.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is CTP:N-methylethanolamine-phosphate cytidylyltransferase. Other names in common use include monomethylethanolamine phosphate cytidylyltransferase, and CTP:P-MEA cytidylyltransferase.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Fas-activated%20serine/threonine%20kinase | In enzymology, a Fas-activated serine/threonine kinase () is an enzyme that catalyzes the chemical reaction
ATP + [Fas-activated serine/threonine protein] ADP + [Fas-activated serine/threonine phosphoprotein]
Thus, the two substrates of this enzyme are ATP and Fas-activated serine/threonine protein, whereas its two products are ADP and Fas-activated serine/threonine phosphoprotein.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups protein-serine/threonine kinases. The systematic name of this enzyme class is ATP:[Fas-activated serine/threonine protein] phosphotransferase. Other names in common use include FAST, FASTK, and STK10.
References
EC 2.7.11
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Nucleoside-phosphate%20kinase | In enzymology, a nucleoside-phosphate kinase () is an enzyme that catalyzes the chemical reaction
ATP + nucleoside phosphate ADP + nucleoside diphosphate
Thus, the two substrates of this enzyme are ATP and nucleoside monophosphate, whereas its two products are ADP and nucleoside diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:nucleoside-phosphate phosphotransferase. This enzyme is also called NMP-kinase, or nucleoside-monophosphate kinase.
Structure
A number of crystal structures have been solved for this class of enzymes, revealing that they share a common ATP binding domain. This section of the enzyme is commonly referred to as the P-loop, in reference to its interaction with the phosphoryl groups on ATP. This binding domain also consists of a β sheet flanked by α helices.
The [P-loop] typically has the amino acid sequence of Gly-X-X-X-X-Gly-Lys. Similar sequences are found in many other nucleotide-binding proteins.
Mechanism
Metal ion interaction
To allow for interaction with this class of enzymes, ATP must first bind to a metal ion such as magnesium or manganese. The metal ion forms a complex with the phosphoryl-group, as well as several water molecules. These water molecules then form hydrogen bonds to a conserved aspartate residue on the enzyme.
The metal ion interaction fa |
https://en.wikipedia.org/wiki/Nucleoside%20phosphotransferase | In enzymology, a nucleoside phosphotransferase () is an enzyme that catalyzes the chemical reaction
a nucleotide + a 2'-deoxynucleoside a nucleoside + a 2'-deoxynucleoside 5'-phosphate
Thus, the two substrates of this enzyme are nucleotide and 2'-deoxynucleoside, whereas its two products are nucleoside and 2'-deoxynucleoside 5'-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is nucleotide:nucleoside 5'-phosphotransferase. Other names in common use include nonspecific nucleoside phosphotransferase, and nucleotide:3'-deoxynucleoside 5'-phosphotransferase.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Nucleoside-triphosphate%E2%80%94adenylate%20kinase | In enzymology, a nucleoside-triphosphate-adenylate kinase () is an enzyme that catalyzes the chemical reaction
nucleoside triphosphate + AMP nucleoside diphosphate + ADP
Thus, the two substrates of this enzyme are nucleoside triphosphate and AMP, whereas its two products are nucleoside diphosphate and ADP.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is nucleoside-triphosphate:AMP phosphotransferase. Other names in common use include guanosine triphosphate-adenylate kinase, nucleoside triphosphate-adenosine monophosphate transphosphorylase, GTP:AMP phosphotransferase, and isozyme 3 of adenylate kinase. This enzyme participates in pyrimidine metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.7.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/Nucleoside-triphosphate-aldose-1-phosphate%20nucleotidyltransferase | In enzymology, a nucleoside-triphosphate-aldose-1-phosphate nucleotidyltransferase () is an enzyme that catalyzes the chemical reaction
nucleoside triphosphate + alpha-D-aldose 1-phosphate diphosphate + NDP-hexose
Thus, the two substrates of this enzyme are nucleoside triphosphate and alpha-D-aldose 1-phosphate, whereas its two products are diphosphate and NDP-hexose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is NTP:alpha-D-aldose-1-phosphate nucleotidyltransferase. Other names in common use include NDP hexose pyrophosphorylase, hexose 1-phosphate nucleotidyltransferase, hexose nucleotidylating enzyme, nucleoside diphosphohexose pyrophosphorylase, hexose-1-phosphate guanylyltransferase, GTP:alpha-D-hexose-1-phosphate guanylyltransferase, GDP hexose pyrophosphorylase, guanosine diphosphohexose pyrophosphorylase, nucleoside-triphosphate-hexose-1-phosphate nucleotidyltransferase, and NTP:hexose-1-phosphate nucleotidyltransferase.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Receptor%20protein%20serine/threonine%20kinase | Receptor protein serine/threonine kinases () are enzyme-linked receptors that belong to protein-serine/threonine kinases. The systematic name of this enzyme class is ATP:[receptor-protein] phosphotransferase. Proteins from this group participate in 7 metabolic pathways: MAPK signaling pathway, cytokine-cytokine receptor interaction, TGF beta signaling pathway, adherens junction, colorectal cancer, pancreatic cancer, and chronic myeloid leukemia.
Links
Receptor protein serine/threonine kinases in IUPHAR Guide to Pharmacology
References
EC 2.7.11
Enzymes of known structure
Single-pass transmembrane proteins |
https://en.wikipedia.org/wiki/Nucleotide%20diphosphokinase | In enzymology, a nucleotide diphosphokinase () is an enzyme that catalyzes the chemical reaction
ATP + nucleoside 5'-phosphate AMP + 5'-phosphonucleoside 3'-diphosphate
Thus, the two substrates of this enzyme are ATP and nucleoside 5'-phosphate, whereas its two products are AMP and 5'-phosphonucleoside 3'-diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring two phosphorus-containing groups (diphosphotransferases). The systematic name of this enzyme class is ATP:nucleoside-5'-phosphate diphosphotransferase. Other names in common use include nucleotide pyrophosphokinase, ATP:nucleotide pyrophosphotransferase, ATP nucleotide 3'-pyrophosphokinase, and nucleotide 3'-pyrophosphokinase.
References
EC 2.7.6
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Opheline%20kinase | In enzymology, an opheline kinase () is an enzyme that catalyzes the chemical reaction
ATP + guanidinoethyl methyl phosphate ADP + N'-phosphoguanidinoethyl methylphosphate
Thus, the two substrates of this enzyme are ATP and guanidinoethyl methyl phosphate, whereas its two products are ADP and N'-phosphoguanidinoethyl methylphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:guanidinoethyl-methyl-phosphate phosphotransferase.
References
EC 2.7.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphatidylglycerol%E2%80%94membrane-oligosaccharide%20glycerophosphotransferase | In enzymology, a phosphatidylglycerol-membrane-oligosaccharide glycerophosphotransferase () is an enzyme that catalyzes the chemical reaction
phosphatidylglycerol + membrane-derived-oligosaccharide D-glucose 1,2-diacyl-sn-glycerol + membrane-derived-oligosaccharide 6-(glycerophospho)-D-glucose
Thus, the two substrates of this enzyme are phosphatidylglycerol and membrane-derived-oligosaccharide D-glucose, whereas its two products are 1,2-diacyl-sn-glycerol and membrane-derived-oligosaccharide 6-(glycerophospho)-D-glucose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups transferases for other substituted phosphate groups. The systematic name of this enzyme class is phosphatidylglycerol:membrane-derived-oligosaccharide-D-glucose glycerophosphotransferase. Other names in common use include phosphoglycerol transferase, oligosaccharide glycerophosphotransferase, and phosphoglycerol transferase I. This enzyme participates in glycerolipid metabolism.
References
EC 2.7.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pantetheine%20kinase | In enzymology, a pantetheine kinase () is an enzyme that catalyzes the chemical reaction
ATP + pantetheine ADP + pantetheine 4'-phosphate
Thus, the two substrates of this enzyme are ATP and pantetheine, whereas its two products are ADP and pantetheine 4'-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:pantetheine 4'-phosphotransferase. This enzyme is also called pantetheine kinase (phosphorylating). This enzyme participates in pantothenate and coa biosynthesis.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pantetheine-phosphate%20adenylyltransferase | In enzymology, a pantetheine-phosphate adenylyltransferase () is an enzyme that catalyzes the chemical reaction
ATP + 4'-Phosphopantetheine diphosphate + 3'-dephospho-CoA
Thus, the two substrates of this enzyme are ATP and 4'-Phosphopantetheine, whereas its two products are diphosphate and 3'-dephospho-CoA.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:pantetheine-4'-phosphate adenylyltransferase. Other names in common use include dephospho-CoA pyrophosphorylase, pantetheine phosphate adenylyltransferase, dephospho-coenzyme A pyrophosphorylase, and 3'-dephospho-CoA pyrophosphorylase. This enzyme participates in pantothenate and coa biosynthesis.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and .
References
EC 2.7.7
Enzymes of known structure |
https://en.wikipedia.org/wiki/Phenylalanine%20adenylyltransferase | In enzymology, a phenylalanine adenylyltransferase () is an enzyme that catalyzes the chemical reaction
ATP + L-phenylalanine diphosphate + N-adenylyl-L-phenylalanine
Thus, the two substrates of this enzyme are ATP and L-phenylalanine, whereas its two products are diphosphate and N-adenylyl-L-phenylalanine.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:L-phenylalanine adenylyltransferase. This enzyme is also called L-phenylalanine adenylyltransferase.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphatidate%20cytidylyltransferase | Phosphatidate cytidylyltransferase () (also known as CDP- diacylglycerol synthase) (CDS) is the enzyme that catalyzes the synthesis of CDP-diacylglycerol from cytidine triphosphate and phosphatidate.
CTP + phosphatidate diphosphate + CDP-diacylglycerol
Thus, the two substrates of this enzyme are cytidine triphosphate, or CTP, and phosphatidate, whereas its two products are diphosphate and CDP-diacylglycerol.
CDP-diacylglycerol is an important branch point intermediate in both prokaryotic and eukaryotic organisms. CDS is a membrane-bound enzyme.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is . Other names in common use include , , , , , , , , , and CDP-DG. This enzyme participates in glycerophospholipid metabolism and phosphatidylinositol signaling system.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphatidylcholine%20synthase | In enzymology, a phosphatidylcholine synthase () is an enzyme that catalyzes the chemical reaction
CDP-diacylglycerol + choline CMP + phosphatidylcholine
Thus, the two substrates of this enzyme are CDP-diacylglycerol and choline, whereas its two products are CMP and phosphatidylcholine.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is CDP-diacylglycerol:choline O-phosphatidyltransferase. This enzyme is also called CDP-diglyceride-choline O-phosphatidyltransferase. This enzyme participates in glycerophospholipid metabolism.
References
EC 2.7.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphatidylinositol-4%2C5-bisphosphate%203-kinase | In enzymology, a phosphatidylinositol-4,5-bisphosphate 3-kinase () is an enzyme that catalyzes the chemical reaction:
ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
Thus, the two substrates of this enzyme are ATP and 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate, whereas its two products are ADP and 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate 3-phosphotransferase. This enzyme is also called type I phosphoinositide 3-kinase. This enzyme participates in 29 metabolic pathways: inositol phosphate metabolism, erbb signaling pathway, phosphatidylinositol signaling system, mtor signaling pathway, apoptosis, VEGF signaling pathway, focal adhesion, toll-like receptor signaling pathway, jak-stat signaling pathway, natural killer cell mediated cytotoxicity, t cell receptor signaling pathway, b cell receptor signaling pathway, fc epsilon ri signaling pathway, leukocyte transendothelial migration, regulation of actin cytoskeleton, insulin signaling pathway, progesterone-mediated oocyte maturation, Type II diabetes mellitus, colorectal cancer, renal cell carcinoma, pancreatic cancer, endometrial cancer, glioma, prostate cancer, melanoma, chronic myelo |
https://en.wikipedia.org/wiki/Phosphatidylinositol-4-phosphate%203-kinase | In enzymology, a phosphatidylinositol-4-phosphate 3-kinase () is an enzyme that catalyzes the chemical reaction
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
Thus, the two substrates of this enzyme are ATP and 1-phosphatidyl-1D-myo-inositol 4-phosphate, whereas its two products are ADP and 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:1-phosphatidyl-1D-myo-inositol-4-phosphate 3-phosphotransferase. Other names in common use include type II phosphoinositide 3-kinase, C2-domain-containing phosphoinositide 3-kinase, and phosphoinositide 3-kinase. This enzyme participates in phosphatidylinositol signaling system.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Phosphoenolpyruvate%E2%80%94glycerone%20phosphotransferase | In enzymology, a phosphoenolpyruvate-glycerone phosphotransferase () is an enzyme that catalyzes the chemical reaction
phosphoenolpyruvate + glycerone pyruvate + glycerone phosphate
Thus, the two substrates of this enzyme are phosphoenolpyruvate and glycerone, whereas its two products are pyruvate and glycerone phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is phosphoenolpyruvate:glycerone phosphotransferase.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphoenolpyruvate%E2%80%94protein%20phosphotransferase | In enzymology, a phosphoenolpyruvate-protein phosphotransferase () is an enzyme that catalyzes the chemical reaction
phosphoenolpyruvate + protein histidine pyruvate + protein Npi-phospho-L-histidine
Thus, the two substrates of this enzyme are phosphoenolpyruvate and protein histidine, whereas its two products are pyruvate and protein Npi-phospho-L-histidine.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. This enzyme participates in phosphotransferase system (pts).
Nomenclature
The systematic name of this enzyme class is phosphoenolpyruvate:protein-L-histidine Npi-phosphotransferase. Other names in common use include phosphoenolpyruvate sugar phosphotransferase enzyme I, phosphopyruvate-protein factor phosphotransferase, phosphopyruvate-protein phosphotransferase, sugar-PEP phosphotransferase enzyme I, and phosphoenolpyruvate:protein-L-histidine N-pros-phosphotransferase.
References
EC 2.7.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Phosphoglucan%2C%20water%20dikinase | In enzymology, a phosphoglucan, water dikinase () is an enzyme that catalyzes the chemical reaction
ATP + [phospho-alpha-glucan] + H2O AMP + O-phospho-[phospho-alpha-glucan] + phosphate
The 3 substrates of this enzyme are ATP, phospho-alpha-glucan, and H2O, whereas its 3 products are AMP, [[O-phospho-[phospho-alpha-glucan]]], and phosphate.
This enzyme belongs to the family of transferases, to be specific, those transferring phosphorus-containing groups (phosphotransferases) with paired acceptors (dikinases). The systematic name of this enzyme class is ATP:phospho-alpha-glucan, water phosphotransferase. Other names in common use include PWD, and OK1.
References
EC 2.7.9
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine%E2%80%94dolichyl-phosphate%20N-acetylglucosaminephosphotransferase | In enzymology, an UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase () is an enzyme that catalyzes the chemical reaction
UDP-N-acetyl-D-glucosamine + dolichyl phosphate UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
Thus, the two substrates of this enzyme are UDP-N-acetyl-D-glucosamine and dolichyl phosphate, whereas its two products are UMP and N-acetyl-D-glucosaminyl-diphosphodolichol.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups transferases for other substituted phosphate groups. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:dolichyl-phosphate N-acetyl-D-glucosaminephosphotransferase. Other names in common use include UDP-D-N-acetylglucosamine N-acetylglucosamine 1-phosphate transferase, UDP-GlcNAc:dolichyl-phosphate GlcNAc-1-phosphate transferase, UDP-N-acetyl-D-glucosamine:dolichol phosphate N-acetyl-D-glucosamine-1-phosphate transferase, uridine diphosphoacetylglucosamine-dolichyl phosphate acetylglucosamine-1-phosphotransferase, chitobiosylpyrophosphoryldolichol synthase, dolichol phosphate N-acetylglucosamine-1-phosphotransferase, UDP-acetylglucosamine-dolichol phosphate acetylglucosamine phosphotransferase, and UDP-acetylglucosamine-dolichol phosphate acetylglucosamine-1-phosphotransferase. This enzyme participates in the biosynthesis of N-glycan and glycan structures.
References
EC 2.7.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphoglucokinase | In enzymology, a phosphoglucokinase () is an enzyme that catalyzes the chemical reaction
ATP + alpha-D-glucose 1-phosphate ADP + alpha-D-glucose 1,6-bisphosphate
Thus, the two substrates of this enzyme are ATP and alpha-D-glucose 1-phosphate, whereas its two products are ADP and alpha-D-glucose 1,6-bisphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:alpha-D-glucose-1-phosphate 6-phosphotransferase. Other names in common use include glucose-phosphate kinase, phosphoglucokinase (phosphorylating), and ATP:D-glucose-1-phosphate 6-phosphotransferase. This enzyme participates in starch and sucrose metabolism.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine%E2%80%94lysosomal-enzyme%20N-acetylglucosaminephosphotransferase | In enzymology, an UDP-N-acetylglucosamine—lysosomal-enzyme N-acetylglucosaminephosphotransferase () is an enzyme that catalyzes the chemical reaction
UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose
Thus, the two substrates of this enzyme are UDP-N-acetyl-D-glucosamine and lysosomal-enzyme D-mannose, whereas its two products are UMP and lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups transferases for other substituted phosphate groups. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:lysosomal-enzyme N-acetylglucosaminephosphotransferase. Other names in common use include UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase, UDP-GlcNAc:glycoprotein N-acetylglucosamine-1-phosphotransferase, uridine diphosphoacetylglucosamine-lysosomal enzyme precursor acetylglucosamine-1-phosphotransferase, uridine diphosphoacetylglucosamine-glycoprotein acetylglucosamine-1-phosphotransferase, lysosomal enzyme precursor acetylglucosamine-1-phosphotransferase, UDP-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase, UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase, UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase, and UDP-N-acetylglucosamine:glycoprotein N-acetylglucosaminyl |
https://en.wikipedia.org/wiki/Phosphoglycerate%20kinase%20%28GTP%29 | In enzymology, a phosphoglycerate kinase (GTP) () is an enzyme that catalyzes the chemical reaction
GTP + 3-phospho-D-glycerate GDP + 3-phospho-D-glyceroyl phosphate
Thus, the two substrates of this enzyme are GTP and 3-phospho-D-glycerate, whereas its two products are GDP and 3-phospho-D-glyceroyl phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is GTP:3-phospho-D-glycerate 1-phosphotransferase.
References
EC 2.7.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/UDP-galactose%E2%80%94UDP-N-acetylglucosamine%20galactose%20phosphotransferase | In enzymology, an UDP-galactose—UDP-N-acetylglucosamine galactose phosphotransferase () is an enzyme that catalyzes the chemical reaction
UDP-galactose + UDP-N-acetyl-D-glucosamine UMP + UDP-N-acetyl-6-(D-galactose-1-phospho)-D-glucosamine
Thus, the two substrates of this enzyme are UDP-galactose and UDP-N-acetyl-D-glucosamine, whereas its two products are UMP and UDP-N-acetyl-6-(D-galactose-1-phospho)-D-glucosamine.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups transferases for other substituted phosphate groups. The systematic name of this enzyme class is UDP-galactose:UDP-N-acetyl-D-glucosamine galactose phosphotransferase. Other names in common use include uridine diphosphogalactose-uridine diphosphoacetylglucosamine galactose-1-phosphotransferase, galactose-1-phosphotransferase, and galactosyl phosphotransferase.
References
EC 2.7.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphomannan%20mannosephosphotransferase | In enzymology, a phosphomannan mannosephosphotransferase () is an enzyme that catalyzes the chemical reaction
GDP-mannose + (phosphomannan)n GMP + (phosphomannan)n+1
Thus, the two substrates of this enzyme are GDP-mannose and (phosphomannan)n, whereas its two products are GMP and (phosphomannan)n+1.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is GDP-mannose:phosphomannan mannose phosphotransferase.
References
EC 2.7.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphomethylpyrimidine%20kinase | In enzymology, a phosphomethylpyrimidine kinase () is an enzyme that catalyzes the chemical reaction
ATP + (4-amino-2-methylpyrimidin-5-yl)methyl phosphate ADP + (4-amino-2-methylpyrimidin-5-yl)methyl diphosphate
Thus, the two substrates of this enzyme are ATP and (4-amino-2-methylpyrimidin-5-yl)methyl phosphate, whereas its two products are ADP and (4-amino-2-methylpyrimidin-5-yl)methyl diphosphate.
This enzyme belongs to the family of transferases, to be specific, those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:(4-amino-2-methylpyrimidin-5-yl)methyl-phosphate phosphotransferase. Other names in common use include hydroxymethylpyrimidine phosphokinase, and ATP:4-amino-2-methyl-5-phosphomethylpyrimidine phosphotransferase. This enzyme participates in thiamine metabolism.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 2.7.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/Phospho-N-acetylmuramoyl-pentapeptide-transferase | In enzymology, a phospho-N-acetylmuramoyl-pentapeptide-transferase () is an enzyme that catalyzes the chemical reaction
UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
Thus, the two substrates of this enzyme are UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) and undecaprenyl phosphate, whereas its 2 products are UMP and Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol.
This enzyme participates in peptidoglycan biosynthesis. It can be expressed efficiently by a cell-free protein expression system.
Nomenclature
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is UDP-MurAc(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala): undecaprenyl-phosphate phospho-N-acetylmuramoyl-pentapeptide-transferase. Other names in common use include MraY transferase, UDP-MurNAc-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala:C55-isoprenoid, alcohol transferase, UDP-MurNAc-Ala-gammaDGlu-Lys-DAla-DAla:undecaprenylphosphate, transferase, phospho-N-acetylmuramoyl pentapeptide translocase, phospho-MurNAc-pentapeptide transferase, phospho-NAc-muramoyl-pentapeptide translocase (UMP), phosphoacetylmuramoylpentapeptide translocase, and phosphoacetylmuramoylpentapeptidetransferase.
References
Further reading
EC 2.7.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphoramidate%E2%80%94hexose%20phosphotransferase | In enzymology, a phosphoramidate-hexose phosphotransferase () is an enzyme that catalyzes the chemical reaction
phosphoramidate + hexose NH3 + alpha-D-hexose 1-phosphate
Thus, the two substrates of this enzyme are phosphoramidate and hexose, whereas its two products are NH3 and alpha-D-hexose 1-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is phosphoramidate:hexose 1-phosphotransferase. Other names in common use include phosphoramidate-hexose transphosphorylase, and phosphoramidic-hexose transphosphorylase.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphoribokinase | In enzymology, a phosphoribokinase () is an enzyme that catalyzes the chemical reaction
ATP + D-ribose 5-phosphate ADP + D-ribose 1,5-bisphosphate
Thus, the two substrates of this enzyme are ATP and D-ribose 5-phosphate, whereas its two products are ADP and D-ribose 1,5-bisphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-ribose-5-phosphate 1-phosphotransferase. This enzyme is also called phosphoribokinase (phosphorylating).
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphoribulokinase | Phosphoribulokinase (PRK) () is an essential photosynthetic enzyme that catalyzes the ATP-dependent phosphorylation of ribulose 5-phosphate (RuP) into ribulose 1,5-bisphosphate (RuBP), both intermediates in the Calvin Cycle. Its main function is to regenerate RuBP, which is the initial substrate and CO2-acceptor molecule of the Calvin Cycle. PRK belongs to the family of transferase enzymes, specifically those transferring phosphorus-containing groups (phosphotransferases) to an alcohol group acceptor. Along with ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCo), phosphoribulokinase is unique to the Calvin Cycle. Therefore, PRK activity often determines the metabolic rate in organisms for which carbon fixation is key to survival. Much initial work on PRK was done with spinach leaf extracts in the 1950s; subsequent studies of PRK in other photosynthetic prokaryotic and eukaryotic organisms have followed. The possibility that PRK might exist was first recognized by Weissbach et al. in 1954; for example, the group noted that carbon dioxide fixation in crude spinach extracts was enhanced by the addition of ATP. The first purification of PRK was conducted by Hurwitz and colleagues in 1956.
ATP + Mg2+ - D-ribulose 5-phosphate ADP + D-ribulose 1,5-bisphosphate
The two substrates of PRK are ATP and D-ribulose 5-phosphate, whereas its two products are ADP and D-ribulose 1,5-bisphosphate. PRK activity requires the presence of a divalent metal cation like Mg2+, as indicated i |
https://en.wikipedia.org/wiki/Polo%20kinase | In enzymology, a polo kinase () is a kinase enzyme i.e. one that catalyzes the chemical reaction
ATP + a protein ADP + a phosphoprotein
Thus, the two substrates of these enzymes are ATP and protein, whereas their two products are ADP and phosphoprotein.
These enzymes belong to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases).
The systematic name of this [polo[-like] kinase] enzyme class is ATP:protein phosphotransferase (spindle-pole-dependent).
Examples and other names in common use include Cdc5, Cdc5p, Plk, PLK, Plk1, Plo1, POLO kinase, polo serine-threonine kinase, polo-like kinase, polo-like kinase 1, serine/threonine-specific Drosophila kinase polo, and STK21.
These enzymes participate in 3 metabolic pathways: cell cycle, cell cycle - yeast, and progesterone-mediated oocyte maturation.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
"Identification and cloning of a protein kinase-encoding mouse gene, Plk, related to the polo gene of Drosophila" 1993
EC 2.7.11
Enzymes of known structure |
https://en.wikipedia.org/wiki/Polynucleotide%205%27-hydroxyl-kinase | In enzymology, a polynucleotide 5'-hydroxyl-kinase () is an enzyme that catalyzes the chemical reaction
ATP + 5'-dephospho-DNA ADP + 5'-phospho-DNA
Thus, the two substrates of this enzyme are ATP and 5'-dephospho-DNA, whereas its two products are ADP and 5'-phospho-DNA. Polynucleotide kinase is a T7 bacteriophage (or T4 bacteriophage) enzyme that catalyzes the transfer of a gamma-phosphate from ATP to the free hydroxyl end of the 5' DNA or RNA. The resulting product could be used to end-label DNA or RNA, or in ligation reactions.
Nomenclature
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as an acceptor. The systematic name of this enzyme class is ATP:5'-dephosphopolynucleotide 5'-phosphotransferase. Other names in common use include:
ATP:5'-dephosphopolynucleotide 5'-phosphatase
PNK
polynucleotide 5'-hydroxyl kinase (phosphorylating),
5'-hydroxyl polynucleotide kinase,
5'-hydroxyl polyribonucleotide kinase,
5'-hydroxyl RNA kinase,
DNA 5'-hydroxyl kinase,
DNA kinase,
polynucleotide kinase, and
polynucleotide 5'-hydroxy-kinase.
References
External links
Vivo
New England Biolabs' T4 PNK page
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Polynucleotide%20adenylyltransferase | In enzymology, a polynucleotide adenylyltransferase () is an enzyme that catalyzes the chemical reaction
ATP + RNA-3'OH pyrophosphate + RNApA-3'OH
Thus, the two substrates of this enzyme are ATP and RNA, whereas its two products are pyrophosphate and RNA with an extra adenosine nucleotide at its 3' end.
Human genes with this activity include TUT1, MTPAP, PAPOLA, PAPOLB, PAPOLG, TENT2, TENT4A, TENT4B, TENT5C, TENT5D.
Function
This enzyme is responsible for the addition of the 3' polyadenine tail to a newly synthesized pre-messenger RNA (pre-mRNA) molecule during the process of gene transcription. The protein is the final addition to a large protein complex that also contains smaller assemblies known as the cleavage and polyadenylation specificity factor (CPSF) and cleavage stimulatory factor (CtSF) and its binding is a necessary prerequisite to the cleavage of the 3' end of the pre-mRNA. After cleavage of the 3' signaling region that directs the assembly of the complex, polyadenylate polymerase (PAP) adds the polyadenine tail to the new 3' end.
The rate at which PAP adds adenine nucleotides is dependent on the presence of another regulatory protein, PABPII (poly-adenine binding protein II). The first few nucleotides added by PAP are added very slowly, but the short polyadenine tail is then bound by PABPII, which accelerates the rate of adenine addition by PAP. The final tail is about 200-250 adenine nucleotides long in mammals.
PAP is phosphorylated by mitosis-promoting |
https://en.wikipedia.org/wiki/Polyphosphate%E2%80%94glucose%20phosphotransferase | In enzymology, a polyphosphate-glucose phosphotransferase () is an enzyme that catalyzes the chemical reaction.
(phosphate)n + D-glucose (phosphate)n-1 + D-glucose 6-phosphate
Thus, the two substrates of this enzyme are (phosphate)n and D-glucose, whereas its two products are (phosphate)n-1 and D-glucose 6-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is polyphosphate:D-glucose 6-phosphotransferase. Other names in common use include polyphosphate glucokinase, polyphosphate-D-(+)-glucose-6-phosphotransferase, and polyphosphate-glucose 6-phosphotransferase. This enzyme participates in glycolysis / gluconeogenesis. It employs one cofactor, neutral salt.
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Polyphosphate%20kinase | In enzymology, a polyphosphate kinase (), or polyphosphate polymerase, is an enzyme that catalyzes the formation of polyphosphate from ATP, with chain lengths of up to a thousand or more orthophosphate moieties.
ATP + (phosphate)n ADP + (phosphate)n+1
Thus, the two substrates of this enzyme are ATP and polyphosphate [(phosphate)n], whereas its two products are ADP and polyphosphate extended by one phosphate moiety [(phosphate)n+1].
This enzyme is a membrane protein and goes through an intermediate stage during the reaction where it is autophosphorylated with a phosphate group covalently linked to a basic amino acyl residue through an N-P bond.
Several enzymes catalyze polyphosphate polymerization. Some of these enzymes couple phosphotransfer to transmembrane transport. These enzyme/transporters are categorized in the Transporter Classification Database (TCDB) under the Polyphosphate Polymerase/YidH Superfamily (TC# 4.E.1) and are transferases that transfer phosphoryl groups (phosphotransferases) with polyphosphate as the acceptor. The systematic name of this enzyme class is ATP:polyphosphate phosphotransferase. This enzyme is also called polyphosphoric acid kinase.
Families
The Polyphosphate Polymerase Superfamily (TC# 4.E.1) includes the following families:
4.E.1 - The Vacuolar (Acidocalcisome) Polyphosphate Polymerase (V-PPP) Family
9.B.51 - The Uncharacterized DUF202/YidH (YidH) Family
The Vacuolar (Acidocalcisome) Polyphosphate Polymerase (V-PPP) Family
Eukary |
https://en.wikipedia.org/wiki/Ch%C3%A2teau%20Laville%20Haut-Brion | Château Laville Haut-Brion was a Bordeaux dry white wine from the Pessac-Léognan appellation, which was ranked among the Crus Classés in the Classification of Graves wine of 1953. The estate is located in close vicinity of the city of Bordeaux, in the commune of Talence.
Since 2009, the fruit from Laville Haut-Brion has been used in the production of Château La Mission Haut-Brion Blanc.
History
Originally acquired in 1611 by Marie de Laville, widow of Sir de Queyrac, the estate remained in the family for over a hundred years, until it was sold in 1717 to Bernard Gaussens. The winery changed ownership several times until 1931 when Leopold Bibonne sold the property to the Frédéric-Otto Woltner, owner of neighbouring estates Château La Mission Haut-Brion and Château La Tour Haut-Brion. His sons Fernand and Henri Woltner were innovative vintners and produced a dry white wine considered the best in Graves, among the reasons behind the latter's reputation as a "wine-making genius". Henri Woltner described the wine as able to be drunk after five years, but seldom at its best before ten years. Its slow-maturing characteristics have been compared to the best of white Burgundies, and the richness akin to a fine Montrachet.
In the 1953 classification of Graves, Château Laville Haut-Brion was rated a Premier Cru as the only of the classed chateaux to be exclusive producers of white wine, and by the mid-1960s, the estate amassed and produced 2,400 cases annually.
Following the death |
https://en.wikipedia.org/wiki/Protein-histidine%20pros-kinase | In enzymology, a protein-histidine pros-kinase () is an enzyme that catalyzes the chemical reaction
ATP + protein L-histidine ADP + protein Nπ-phospho-L-histidine
Thus, the two substrates of this enzyme are ATP and protein L-histidine, whereas its two products are ADP and protein Npi-phospho-L-histidine.
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain of histidine residues in proteins (protein-histidine kinases). The systematic name of this enzyme class is ATP:protein-L-histidine Npi-phosphotransferase. Other names in common use include ATP:protein-L-histidine N-pros-phosphotransferase, histidine kinase, histidine protein kinase, protein histidine kinase, protein kinase (histidine), and HK2.
References
EC 2.7.13
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Protein-histidine%20tele-kinase | In enzymology, a protein-histidine tele-kinase () is an enzyme that catalyzes the chemical reaction
ATP + protein L-histidine ADP + protein Nτ-phospho-L-histidine
Thus, the two substrates of this enzyme are ATP and protein L-histidine, whereas its two products are ADP and protein Ntau-phospho-L-histidine.
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain of histidine residues in proteins (protein-histidine kinases). The systematic name of this enzyme class is ATP:protein-L-histidine Ntau-phosphotransferase. Other names in common use include ATP:protein-L-histidine N-tele-phosphotransferase, histidine kinase, histidine protein kinase, protein histidine kinase, protein kinase (histidine), and HK3.
References
EC 2.7.13
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Protein-Npi-phosphohistidine-sugar%20phosphotransferase | In enzymology, a protein-Npi-phosphohistidine-sugar phosphotransferase () is an enzyme that catalyzes the chemical reaction
protein Npi-phospho-L-histidine + sugar protein histidine + sugar phosphate
Thus, the two substrates of this enzyme are protein Npi-phospho-L-histidine and sugar, whereas its two products are protein histidine and sugar phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is protein-Npi-phosphohistidine:sugar Npi-phosphotransferase. Other names in common use include glucose permease, PTS permease, phosphotransferase, phosphohistidinoprotein-hexose, enzyme IIl4ac, gene glC proteins, gene bglC RNA formation factors, PEP-dependent phosphotransferase enzyme II, PEP-sugar phosphotransferase enzyme II, phosphoenolpyruvate-sugar phosphotransferase enzyme II, phosphohistidinoprotein-hexose phosphotransferase, phosphohistidinoprotein-hexose phosphoribosyltransferase, phosphoprotein factor-hexose phosophotransferase, protein, specific or class, gene bglC, ribonucleic acid formation factor, gene glC, sucrose phosphotransferase system II, and protein-Npi-phosphohistidine:sugar N-pros-phosphotransferase. This enzyme participates in 7 metabolic pathways: glycolysis / gluconeogenesis, fructose and mannose metabolism, galactose metabolism, ascorbate and aldarate metabolism, starch and sucrose metabo |
https://en.wikipedia.org/wiki/%28protein-PII%29%20uridylyltransferase | In enzymology, a [protein-PII] uridylyltransferase () is an enzyme that catalyzes the chemical reaction
UTP + [protein-PII] diphosphate + uridylyl-[protein-PII]
Thus, the two substrates of this enzyme are UTP and protein-PII, whereas its two products are diphosphate and [[uridylyl-[protein-PII]]].
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is UTP:[protein-PII] uridylyltransferase. Other names in common use include PII uridylyl-transferase, and uridyl removing enzyme. This enzyme participates in two-component system - general.
References
Protein-PII uridylyltransferase
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pseudouridine%20kinase | In enzymology, a pseudouridine kinase () is an enzyme that catalyzes the chemical reaction
ATP + pseudouridine ADP + pseudouridine 5'-phosphate
Thus, the two substrates of this enzyme are ATP and pseudouridine, whereas its two products are ADP and pseudouridine 5'-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:pseudouridine 5'-phosphotransferase. This enzyme is also called pseudouridine kinase (phosphorylating). This enzyme participates in pyrimidine metabolism.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pyridoxal%20kinase | In enzymology, a pyridoxal kinase () is an enzyme that catalyzes the chemical reaction
ATP + pyridoxal ADP + pyridoxal 5'-phosphate
Thus, the two substrates of this enzyme are ATP and pyridoxal, whereas its two products are ADP and pyridoxal 5'-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:pyridoxal 5'-phosphotransferase. Other names in common use include pyridoxal kinase (phosphorylating), pyridoxal 5-phosphate-kinase, pyridoxal phosphokinase, and pyridoxine kinase. This enzyme participates in vitamin B6 metabolism.
Structural studies
As of late 2007, 15 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , and .
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Pyruvate%2C%20phosphate%20dikinase | Pyruvate, phosphate dikinase, or PPDK () is an enzyme in the family of transferases that catalyzes the chemical reaction
ATP + pyruvate + phosphate AMP + phosphoenolpyruvate + diphosphate
This enzyme has been studied primarily in plants, but it has been studied in some bacteria as well. It is a key enzyme in gluconeogenesis and photosynthesis that is responsible for reversing the reaction performed by pyruvate kinase in Embden-Meyerhof-Parnas glycolysis. It should not be confused with pyruvate, water dikinase.
It belongs to the family of transferases, to be specific, those transferring phosphorus-containing groups (phosphotransferases) with paired acceptors (dikinases). This enzyme participates in pyruvate metabolism and carbon fixation.
Nomenclature
The systematic name of this enzyme class is ATP:pyruvate, phosphate phosphotransferase. Other names in common use include pyruvate, orthophosphate dikinase, pyruvate-phosphate dikinase (phosphorylating), pyruvate phosphate dikinase, pyruvate-inorganic phosphate dikinase, pyruvate-phosphate dikinase, pyruvate-phosphate ligase, pyruvic-phosphate dikinase, pyruvic-phosphate ligase, pyruvate, Pi dikinase, and PPDK.
Reaction mechanism
PPDK catalyses the conversion of pyruvate to phosphoenolpyruvate (PEP), consuming 1 molecule of ATP, and producing one molecule of AMP in the process. The mechanism consists of 3 reversible reactions:
The enzyme PPDK binds to ATP, to produce AMP and a diphosphorylated PPDK.
The diphosphoryla |
https://en.wikipedia.org/wiki/Pyruvate%2C%20water%20dikinase | In enzymology, a pyruvate, water dikinase (EC 2.7.9.2) is an enzyme that catalyzes the chemical reaction
ATP + pyruvate + H2O AMP + phosphoenolpyruvate + phosphate
The 3 substrates of this enzyme are ATP, pyruvate, and H2O, whereas its 3 products are AMP, phosphoenolpyruvate, and phosphate. This reaction catalyzed by pyruvate, water dikinase can run in both directions, but has a strong preference for AMP, phosphate, and phosphoenolpyruvate as substrate and typically runs in the ATP producing direction.
This enzyme belongs to the family of transferases, to be specific, those transferring phosphorus-containing groups (phosphotransferases) with paired acceptors (dikinases). The systematic name of this enzyme class is ATP:pyruvate, water phosphotransferase. Other names in common use include phosphoenolpyruvate synthase, pyruvate-water dikinase (phosphorylating), PEP synthetase, PEP synthase, PEPS, phoephoenolpyruvate synthetase, phosphoenolpyruvic synthase, and phosphopyruvate synthetase. This enzyme participates in pyruvate metabolism and reductive carboxylate cycle (CO2 fixation). It employs one cofactor, manganese.
Studied organisms
According to the BRENDA database, pyruvate, water dikinase has been studied in nine unique bacterial and archaea species under a wide range of names. Many of the studied organisms are thermophilic or hyperthermophilic, meaning they live and function in very high temperatures in their natural environments, and have been found in hot springs, |
https://en.wikipedia.org/wiki/Rhamnulokinase | In enzymology, a rhamnulokinase () is an enzyme that catalyzes the chemical reaction
ATP + L-rhamnulose ADP + L-rhamnulose 1-phosphate
Thus, the two substrates of this enzyme are ATP and L-rhamnulose, whereas its two products are ADP and L-rhamnulose 1-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:L-rhamnulose 1-phosphotransferase. Other names in common use include RhuK, rhamnulokinase (phosphorylating), L-rhamnulokinase, L-rhamnulose kinase, and rhamnulose kinase. This enzyme participates in pentose and glucuronate interconversions and fructose and mannose metabolism. This enzyme can catalyze the xylulose phosphorilation:
ATP + L-Xylulose ADP + L-Xylulose 1-phosphate
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes by Grueninger and Schulz with PDB accession codes , , , and .
References
D.Grueninger and G.E.Schulz (2006). Structure and reaction mechanism of L-rhamnulose kinase from Escherichia coli.. J. Mol. Biol., 359, 787-797.
D.Grueninger and G.E.Schulz (2007). Substrate spectrum of L-rhamnulose kinase related to models derived from two ternary complex structures.. FEBS Lett, 581, 3127-3130.
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Riboflavin%20kinase | In enzymology, a riboflavin kinase () is an enzyme that catalyzes the chemical reaction
ATP + riboflavin ADP + FMN
Thus, the two substrates of this enzyme are ATP and riboflavin, whereas its two products are ADP and FMN.
Riboflavin is converted into catalytically active cofactors (FAD and FMN) by the actions of riboflavin kinase (), which converts it into FMN, and FAD synthetase (), which adenylates FMN to FAD. Eukaryotes usually have two separate enzymes, while most prokaryotes have a single bifunctional protein that can carry out both catalyses, although exceptions occur in both cases. While eukaryotic monofunctional riboflavin kinase is orthologous to the bifunctional prokaryotic enzyme, the monofunctional FAD synthetase differs from its prokaryotic counterpart, and is instead related to the PAPS-reductase family. The bacterial FAD synthetase that is part of the bifunctional enzyme has remote similarity to nucleotidyl transferases and, hence, it may be involved in the adenylylation reaction of FAD synthetases.
This enzyme belongs to the family of transferases, to be specific, those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:riboflavin 5'-phosphotransferase. This enzyme is also called flavokinase. This enzyme participates in riboflavin metabolism.
However, archaeal riboflavin kinases () in general utilize CTP rather than ATP as the donor nucleotide, catalyzing the |
https://en.wikipedia.org/wiki/Riboflavin%20phosphotransferase | In enzymology, a riboflavin phosphotransferase () is an enzyme that catalyzes the chemical reaction
alpha-D-glucose 1-phosphate + riboflavin D-glucose + FMN
Thus, the two substrates of this enzyme are alpha-D-glucose 1-phosphate and riboflavin, whereas its two products are D-glucose and FMN.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is alpha-D-glucose-1-phosphate:riboflavin 5'-phosphotransferase. Other names in common use include riboflavine phosphotransferase, glucose-1-phosphate phosphotransferase, G-1-P phosphotransferase, and D-glucose-1-phosphate:riboflavin 5'-phosphotransferase.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ribokinase | In enzymology, a ribokinase () is an enzyme that catalyzes the chemical reaction
ATP + -ribose ⇌ ADP + -ribose 5-phosphate
Thus, the two substrates of this enzyme are ATP and -ribose, whereas its two products are ADP and -ribose 5-phosphate.
The systematic name of this enzyme class is ATP:-ribose 5-phosphotransferase. Other names in common use include deoxyribokinase, ribokinase (phosphorylating), and -ribokinase. This enzyme participates in pentose phosphate pathway.
Ribokinase (RK) belongs to the phosphofructokinase B (PfkB) family of sugar kinases. Other members of this family (also known as the RK family) include adenosine kinase (AK), inosine-guanosine kinase, fructokinase, and 1-phosphofructokinase. The members of the PfkB/RK family are identified by the presence of three conserved sequence motifs and the enzymatic activity of this family of protein generally shows a dependence on the presence of pentavalent ions. The conserved NXXE motif, which is a distinctive property of the PfkB family of proteins, is involved in pentavalent ion dependency. The structures of RK and several other PfK family of proteins have been determined from a number of organisms. Despite low sequence similarity between AdK and other PfkB family of proteins, these proteins are quite similar at structural levels.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
Further reading
EC 2.7. |
https://en.wikipedia.org/wiki/Ribose%201%2C5-bisphosphate%20phosphokinase | In enzymology, a ribose 1,5-bisphosphate phosphokinase () is an enzyme that catalyzes the chemical reaction
ATP + ribose 1,5-bisphosphate ADP + 5-phospho-alpha-D-ribose 1-diphosphate
Thus, the two substrates of this enzyme are ATP and ribose 1,5-bisphosphate, whereas its two products are ADP and 5-phospho-alpha-D-ribose 1-diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:ribose-1,5-bisphosphate phosphotransferase. Other names in common use include ribose 1,5-bisphosphokinase, and PhnN. This enzyme participates in pentose phosphate pathway.
References
EC 2.7.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ribose-5-phosphate%20adenylyltransferase | In enzymology, a ribose-5-phosphate adenylyltransferase () is an enzyme that catalyzes the chemical reaction
ADP + D-ribose 5-phosphate phosphate + ADP-ribose
Thus, the two substrates of this enzyme are ADP and D-ribose 5-phosphate, whereas its two products are phosphate and ADP-ribose.
This enzyme belongs to the family of transferases, specifically ones transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ADP:D-ribose-5-phosphate adenylyltransferase. Other names in common use include ADP ribose phosphorylase, and adenosine diphosphoribose phosphorylase.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ribosylnicotinamide%20kinase | In enzymology, a ribosylnicotinamide kinase () is an enzyme that catalyzes the chemical reaction
ATP + N-ribosylnicotinamide ADP + nicotinamide ribonucleotide
Thus, the two substrates of this enzyme are ATP and N-ribosylnicotinamide, whereas its two products are ADP and nicotinamide ribonucleotide.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:N-ribosylnicotinamide 5'-phosphotransferase. This enzyme is also called ribosylnicotinamide kinase (phosphorylating). This enzyme participates in nicotinate and nicotinamide metabolism.
Health
Studies show potential for obesity treatment and for longer healthier life. Ribosylnicotinamide kinase seems to activate similar genes that Resveratrol does.
Food
The enzyme can be found in milk and beer. Since the molecules are difficult to detect, it is expected that there are a lot more food products containing ribosylnicotinamide kinase.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ribulokinase | In enzymology, a ribulokinase () is an enzyme that catalyzes the chemical reaction
ATP + L(or D)-ribulose ADP + L(or D)-ribulose 5-phosphate
The 3 substrates of this enzyme are ATP, L-ribulose, and D-ribulose, whereas its 3 products are ADP, L-ribulose 5-phosphate, and D-ribulose 5-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:L(or D)-ribulose 5-phosphotransferase. Other names in common use include ribulokinase (phosphorylating), and L-ribulokinase. This enzyme participates in pentose and glucuronate interconversions.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28RNA-polymerase%29-subunit%20kinase | In enzymology, an [RNA-polymerase]-subunit kinase () is an enzyme that catalyzes the chemical reaction
ATP + [DNA-directed RNA polymerase] ADP + phospho-[DNA-directed RNA polymerase]
Thus, the two substrates of this enzyme are ATP and DNA-directed RNA polymerase, whereas its two products are ADP and phospho-DNA-directed RNA polymerase.
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is ATP:[DNA-directed RNA polymerase] phosphotransferase. Other names in common use include CTD kinase, and STK9.
References
EC 2.7.11
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/RNA%20uridylyltransferase | In enzymology, a RNA uridylyltransferase () is an enzyme that catalyzes the chemical reaction
UTP + RNAn diphosphate + RNAn+1
Thus, the two substrates of this enzyme are UTP and RNAn, whereas its two products are diphosphate and RNAn+1.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is UTP:RNA uridylyltransferase. Other names in common use include terminal uridylyltransferase, and TUT.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and .
References
EC 2.7.7
Enzymes of known structure |
https://en.wikipedia.org/wiki/Metabolon | In biochemistry, a metabolon is a temporary structural-functional complex formed between sequential enzymes of a metabolic pathway, held together both by non-covalent interactions and by structural elements of the cell, such as integral membrane proteins and proteins of the cytoskeleton.
The formation of metabolons allows the intermediate product from one enzyme to be passed (channelling) directly into the active site of the next consecutive enzyme of the metabolic pathway. The citric acid cycle is an example of a metabolon that facilitates substrate channeling. Another example is the dhurrin synthesis pathway in sorghum, in which the enzymes assemble as a metabolon in lipid membranes. During the functioning of metabolons, the amount of water needed to hydrate the enzymes is reduced and enzyme activity is increased.
History
The concept of structural-metabolic cellular complexes was first conceived in 1970 by A. M. Kuzin of the USSR Academy of Sciences, and adopted in 1972 by Paul A. Srere of the University of Texas for the enzymes of the citric acid cycle. This hypothesis was well accepted in the former USSR and further developed for the complex of glycolytic enzymes (Embden-Meyerhof-Parnas pathway) by B.I. Kurganov and A.E. Lyubarev. In the mid-1970s, the group of F.M. Clarke at the University of Queensland, Australia also worked on the concept. The name “metabolon” was first proposed in 1985 by Paul Srere during a lecture in Debrecen, Hungary.
The case of Fatty Acid S |
https://en.wikipedia.org/wiki/Scyllo-inosamine%204-kinase | In enzymology, a scyllo-inosamine 4-kinase () is an enzyme that catalyzes the chemical reaction
ATP + 1-amino-1-deoxy-scyllo-inositol ADP + 1-amino-1-deoxy-scyllo-inositol 4-phosphate
Thus, the two substrates of this enzyme are ATP and 1-amino-1-deoxy-scyllo-inositol, whereas its two products are ADP and 1-amino-1-deoxy-scyllo-inositol 4-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:1-amino-1-deoxy-scyllo-inositol 4-phosphotransferase. Other names in common use include scyllo-inosamine kinase (phosphorylating), scyllo-inosamine kinase, and ATP:inosamine phosphotransferase. This enzyme participates in streptomycin biosynthesis.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sedoheptulokinase | In enzymology, a sedoheptulokinase () is an enzyme that catalyzes the chemical reaction
ATP + sedoheptulose ADP + sedoheptulose 7-phosphate
Thus, the two substrates of this enzyme are ATP and sedoheptulose, whereas its two products are ADP and sedoheptulose 7-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:sedoheptulose 7-phosphotransferase. Other names in common use include heptulokinase, and sedoheptulokinase (phosphorylating). This enzyme participates in carbon fixation.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Selenide%2C%20water%20dikinase | In enzymology, a selenide, water dikinase () is an enzyme that catalyzes the chemical reaction
ATP + selenide + H2O AMP + selenophosphate + phosphate
The 3 substrates of this enzyme are ATP, selenide, and H2O, whereas its 3 products are AMP, selenophosphate, and phosphate.
This enzyme belongs to the family of transferases, to be specific, those transferring phosphorus-containing groups (phosphotransferases) with paired acceptors (dikinases). The systematic name of this enzyme class is ATP:selenide, water phosphotransferase. This enzyme is also called selenophosphate synthetase. This enzyme participates in selenoamino acid metabolism.
References
EC 2.7.9
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Serine-phosphoethanolamine%20synthase | In enzymology, a serine-phosphoethanolamine synthase () is an enzyme that catalyzes the chemical reaction
CDP-ethanolamine + L-serine CMP + L-serine-phosphoethanolamine
Thus, the two substrates of this enzyme are CDP-ethanolamine and L-serine, whereas its two products are CMP and L-serine-phosphoethanolamine.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is CDP-ethanolamine:L-serine ethanolamine phosphotransferase. Other names in common use include serine ethanolamine phosphate synthetase, serine ethanolamine phosphodiester synthase, serine ethanolaminephosphotransferase, serine-phosphinico-ethanolamine synthase, and serinephosphoethanolamine synthase. This enzyme participates in glycerophospholipid metabolism.
References
EC 2.7.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Shikimate%20kinase | Shikimate kinase () is an enzyme that catalyzes the ATP-dependent phosphorylation of shikimate to form shikimate 3-phosphate. This reaction is the fifth step of the shikimate pathway, which is used by plants and bacteria to synthesize the common precursor of aromatic amino acids and secondary metabolites. The systematic name of this enzyme class is ATP:shikimate 3-phosphotransferase. Other names in common use include shikimate kinase (phosphorylating), and shikimate kinase II.
Background
The shikimate pathway consists of seven enzymatic reactions by which phosphoenolpyruvate and erythrose 4-phosphate are converted to chorismate, the common precursor of the aromatic amino acids phenylalanine, tyrosine, and tryptophan. The aromatic amino acids are used in the synthesis of proteins and, in plants, fungi, and bacteria, give rise to a number of other specialized metabolites, such as phenylpropanoids and alkaloids. Chorismate and several other intermediates of the pathway serve as precursors for a number of other metabolites, such as folates, quinates, and quinones. The four enzymes that precede shikimate kinase in the pathway are DAHP synthase, 3-dehydroquinate synthase, 3-dehydroquinate dehydratase, and shikimate dehydrogenase, and the two that follow it are EPSP synthase and chorismate synthase. In fungi and protists, it is part of the AROM complex, in which the five central steps of the shikimate pathway are co-localized. The pathway is not found in humans and other animals, w |
https://en.wikipedia.org/wiki/S-methyl-5-thioribose%20kinase | In enzymology, a S-methyl-5-thioribose kinase () is an enzyme that catalyzes the chemical reaction
ATP + S-methyl-5-thio-D-ribose ADP + S-methyl-5-thio-alpha-D-ribose 1-phosphate
Thus, the two substrates of this enzyme are ATP and S-methyl-5-thio-D-ribose, whereas its two products are ADP and S-methyl-5-thio-alpha-D-ribose 1-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:S-methylmethyl-5-thio-D-ribose 1-phosphotransferase. Other names in common use include 5-methylthioribose kinase (phosphorylating), methylthioribose kinase, 5-methylthioribose kinase, and ATP:S5-methyl-5-thio-D-ribose 1-phosphotransferase. This enzyme participates in methionine metabolism.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Sphingomyelin%20synthase | In enzymology, a sphingomyelin synthase () is an enzyme that catalyzes the chemical reaction
a ceramide + a phosphatidylcholine a sphingomyelin + a 1,2-diacyl-sn-glycerol
Thus, the two substrates of this enzyme are ceramide and phosphatidylcholine, whereas its two products are sphingomyelin and 1,2-diacyl-sn-glycerol.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is ceramide:phosphatidylcholine cholinephosphotransferase. Other names in common use include SM synthase, SMS1, and SMS2.
References
EC 2.7.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sphingosine%20cholinephosphotransferase | In enzymology, a sphingosine cholinephosphotransferase () is an enzyme that catalyzes the chemical reaction
CDP-choline + sphingosine CMP + sphingosyl-phosphocholine
Thus, the two substrates of this enzyme are CDP-choline and sphingosine, whereas its two products are CMP and sphingosyl-phosphocholine.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is CDP-choline:sphingosine cholinephosphotransferase. Other names in common use include CDP-choline-sphingosine cholinephosphotransferase, phosphorylcholine-sphingosine transferase, cytidine diphosphocholine-sphingosine cholinephosphotransferase, and sphingosine choline phosphotransferase. This enzyme participates in sphingolipid metabolism.
References
EC 2.7.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Streptomycin%203%22-adenylyltransferase | In enzymology, a streptomycin 3"-adenylyltransferase () is an enzyme that catalyzes the chemical reaction:
ATP + streptomycin diphosphate + 3"-adenylylstreptomycin
Thus, the two substrates of this enzyme are ATP and streptomycin, whereas its two products are diphosphate and 3''-adenylylstreptomycin.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:streptomycin 3"-adenylyltransferase. Other names in common use include streptomycin adenylate synthetase, streptomycin adenyltransferase, streptomycin adenylylase, streptomycin adenylyltransferase, streptomycin-spectinomycin adenylyltransferase, AAD (3"), and aminoglycoside 3"-adenylyltransferase.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Streptomycin%203%22-kinase | In enzymology, a streptomycin 3"-kinase () is an enzyme that catalyzes the chemical reaction
ATP + streptomycin ADP + streptomycin 3"-phosphate
Thus, the two substrates of this enzyme are ATP and streptomycin, whereas its two products are ADP and streptomycin 3''-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:streptomycin 3"-phosphotransferase. Other names in common use include streptomycin 3"-kinase (phosphorylating), and streptomycin 3"-phosphotransferase.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Streptomycin%206-kinase | In enzymology, a streptomycin 6-kinase () is an enzyme that catalyzes the chemical reaction
ATP + streptomycin ADP + streptomycin 6-phosphate
Thus, the two substrates of this enzyme are ATP and streptomycin, whereas its two products are ADP and streptomycin 6-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:streptomycin 6-phosphotransferase. Other names in common use include streptidine kinase, SM 6-kinase, streptomycin 6-kinase (phosphorylating), streptidine kinase (phosphorylating), streptomycin 6-O-phosphotransferase, and streptomycin 6-phosphotransferase. This enzyme participates in streptomycin biosynthesis.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sulfate%20adenylyltransferase | In enzymology, a sulfate adenylyltransferase () is an enzyme that catalyzes the chemical reaction
ATP + sulfate pyrophosphate + adenylyl sulfate
Thus, the two substrates of this enzyme are ATP and sulfate, whereas its two products are pyrophosphate and adenylyl sulfate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:sulfate adenylyltransferase. Other names in common use include adenosine-5'-triphosphate sulfurylase, adenosinetriphosphate sulfurylase, adenylylsulfate pyrophosphorylase, ATP sulfurylase, ATP-sulfurylase, and sulfurylase. This enzyme participates in 3 metabolic pathways: purine metabolism, selenoamino acid metabolism, and sulfur metabolism.
Some sulfate adenylyltransferases are part of a bifunctional polypeptide chain associated with adenosyl phosphosulfate (APS) kinase. Both enzymes are required for PAPS (phosphoadenosine-phosphosulfate) synthesis from inorganic sulfate.
Within the cell Sulfate adenylyltransferase plays a key role in both assimilatory sulfur reduction and dissimilatory sulfur oxidation and reduction (DSR) and participates in the biogeochemically relevant sulfur cycle. In dissimilatory sulfate reduction the SAT enzyme, acts as the first priming step in the reduction converting sulfate(+6) to Adenosine 5'-phosphosulfate (APS) via adenylation at the cost of an ATP. If the organisms participati |
https://en.wikipedia.org/wiki/Sulfate%20adenylyltransferase%20%28ADP%29 | In enzymology, a sulfate adenylyltransferase (ADP) () is an enzyme that catalyzes the chemical reaction
ADP + sulfate phosphate + adenylyl sulfate
Thus, the two substrates of this enzyme are ADP and sulfate, whereas its two products are phosphate and adenylyl sulfate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ADP:sulfate adenylyltransferase. Other names in common use include ADP-sulfurylase, sulfate (adenosine diphosphate) adenylyltransferase, and adenosine diphosphate sulfurylase. This enzyme participates in sulfur metabolism.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/T2-induced%20deoxynucleotide%20kinase | In enzymology, a T2-induced deoxynucleotide kinase () is an enzyme that catalyzes the chemical reaction
ATP + dGMP (or dTMP) ADP + dGDP (or dTDP)
The 3 substrates of this enzyme are ATP, dGMP, and dTMP, whereas its 3 products are ADP, dGDP, and dTDP.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:(d)NMP phosphotransferase.
References
EC 2.7.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tagatose-6-phosphate%20kinase | In enzymology, a tagatose-6-phosphate kinase () is an enzyme that catalyzes the chemical reaction
ATP + D-tagatose 6-phosphate ADP + D-tagatose 1,6-bisphosphate
Thus, the two substrates of this enzyme are ATP and D-tagatose 6-phosphate, whereas its two products are ADP and D-tagatose 1,6-bisphosphate.
This enzyme belongs to the phosphofructokinase B (PfkB) or Ribokinase family of sugar kinases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-tagatose-6-phosphate 1-phosphotransferase. The members of the PfkB/RK family are identified by the presence of three conserved sequence motifs and their enzymatic activity generally shows a dependence on the presence of pentavalent ions. Pentavalent ions dependency is a conserved property of adenosine kinase from diverse sources: identification of a novel motif implicated in phosphate and magnesium ion binding and substrate inhibition. Biochemistry 2002, 41: 4059-4069.</ref> This enzyme participates in galactose metabolism.
Structural studies
As of late 2007, five structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Tagatose%20kinase | In enzymology, a tagatose kinase () is an enzyme that catalyzes the chemical reaction
ATP + D-tagatose ADP + D-tagatose 6-phosphate
Thus, the two substrates of this enzyme are ATP and D-tagatose, whereas its two products are ADP and D-tagatose 6-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-tagatose 6-phosphotransferase. Other names in common use include tagatose 6-phosphate kinase (phosphorylating), D-tagatose 6-phosphate kinase, and tagatose-6-phosphate kinase. This enzyme participates in galactose metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Tau-protein%20kinase | In enzymology, a tau-protein kinase () is an enzyme that catalyzes the chemical reaction
ATP + tau protein ADP + O-phospho-tau-protein
Thus, the two substrates of this enzyme are ATP and tau protein, whereas its two products are ADP and O-phospho-tau-protein.
This enzyme belongs to the family of transferases, specifically, those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). This enzyme participates in 14 metabolic pathways: erbb signaling pathway, cell cycle, wnt signaling pathway, hedgehog signaling pathway, axon guidance, focal adhesion, b cell receptor signaling pathway, insulin signaling pathway, melanogenesis, alzheimer's disease, colorectal cancer, endometrial cancer, prostate cancer, and basal cell carcinoma.
Nomenclature
The systematic name of this enzyme class is ATP:[tau-protein] O-phosphotransferase. Other names in common use include ATP:tau-protein O-hosphotransferase, brain protein kinase PK40erk, cdk5/p20, CDK5/p23, glycogen synthase kinase-3beta, GSK, protein tau kinase, STK31, tau kinase, [tau-protein] kinase, tau-protein kinase I, tau-protein kinase II, tau-tubulin kinase, TPK, TPK I, TPK II, and TTK.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
Examples
Human genes encoding proteins with Tau-protein kinase activity include:
BRSK1
BRSK2
GSK3A
GSK3B
References
|
https://en.wikipedia.org/wiki/Taurocyamine%20kinase | In enzymology, a taurocyamine kinase () is an enzyme that catalyzes the chemical reaction
ATP + taurocyamine ADP + N-phosphotaurocyamine
Thus, the two substrates of this enzyme are ATP and taurocyamine, whereas its two products are ADP and N-phosphotaurocyamine.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:taurocyamine N-phosphotransferase. Other names in common use include taurocyamine phosphotransferase, and ATP:taurocyamine phosphotransferase. This enzyme participates in taurine and hypotaurine metabolism.
References
EC 2.7.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tetraacyldisaccharide%204%27-kinase | Tetraacyldisaccharide 4'-kinase is an enzyme that phosphorylates the 4'-position of a tetraacyldisaccharide 1-phosphate precursor (DS-1-P) of lipopolysaccharide lipid A. This lipid forms outer membranes of Gram-negative bacteria. This enzyme catalyzes the chemical reaction
ATP + [2-N,3-O-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl]-(1->6)-[2- N,3-O-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl phosphate] ADP + [2-N,3-O-bis(3-hydroxytetradecanoyl)-4-O-phosphono-beta-D- glucosaminyl]-(1->6)-[2-N,3-O-bis(3-hydroxytetradecanoyl)-beta-D- glucosaminyl phosphate]
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor.
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Thiamine-diphosphate%20kinase | In enzymology, a thiamine-diphosphate kinase is an enzyme involved in thiamine metabolism. It catalyzes the chemical reaction
thiamine diphosphate + ATP thiamine triphosphate + ADP
Thus, the two substrates of this enzyme are ATP and thiamine diphosphate, whereas its two products are ADP and thiamine triphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:thiamine-diphosphate phosphotransferase. Other names in common use include ATP:thiamin-diphosphate phosphotransferase, TDP kinase, thiamin diphosphate kinase, thiamin diphosphate phosphotransferase, thiamin pyrophosphate kinase, thiamine diphosphate kinase, and protein bound thiamin diphosphate:ATP phosphoryltransferase.
See also
Thiamine-triphosphatase
References
EC 2.7.4
Enzymes of unknown structure |
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