ExplorEnz: EC 2.7.1*

Displaying entries 101-150 of 285.

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2.7.1.101

Accepted name:

tagatose kinase

Reaction:

ATP + D-tagatose = ADP + D-tagatose 6-phosphate

Other name(s):

AtuFK

Systematic name:

ATP:D-tagatose 6-phosphotransferase

Comments:

The enzyme from Agrobacterium fabrum C58 is part of D-altritol and galactitol degradation pathways.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39434-00-9

References:

1.	Szumilo, T. A novel enzyme, tagatose kinase, from Mycobacterium butyricum. Biochim. Biophys. Acta 660 (1981) 366–370. [DOI] [PMID: 6269638]
2.	Wichelecki, D.J., Vetting, M.W., Chou, L., Al-Obaidi, N., Bouvier, J.T., Almo, S.C. and Gerlt, J.A. ATP-binding cassette (ABC) transport system solute-binding protein-guided identification of novel D-altritol and galactitol catabolic pathways in Agrobacterium tumefaciens C58. J. Biol. Chem. 290 (2015) 28963–28976. [DOI] [PMID: 26472925]

[EC 2.7.1.101 created 1983]

2.7.1.102

Accepted name:

hamamelose kinase

Reaction:

ATP + D-hamamelose = ADP + D-hamamelose 2′-phosphate

Other name(s):

hamamelose kinase (phosphorylating); hamamelosekinase (ATP: hamamelose 2′-phosphotransferase); ATP/hamamelose 2′-phosphotransferase

Systematic name:

ATP:D-hamamelose 2′-phosphotransferase

Comments:

Also acts, more slowly, on D-hamamelitol.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 74506-53-9

References:

1.	Beck, E., Wieczorek, J. and Reinecke, W. Purification and properties of hamamelosekinase. Eur. J. Biochem. 107 (1980) 485–489. [DOI] [PMID: 6249593]

[EC 2.7.1.102 created 1983]

2.7.1.103

Accepted name:

viomycin kinase

Reaction:

ATP + viomycin = ADP + O-phosphoviomycin

Other name(s):

viomycin phosphotransferase; capreomycin phosphotransferase

Systematic name:

ATP:viomycin O-phosphotransferase

Comments:

Acts also on capreomycins. A serine residue in the peptide antibiotics acts as phosphate-acceptor.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 77000-11-4

References:

1.	Skinner, R.H. and Cundliffe, E. Resistance to the antibiotics viomycin and capreomycin in the Streptomyces species which produce them. J. Gen. Microbiol. 120 (1980) 95–104. [DOI] [PMID: 6163840]

[EC 2.7.1.103 created 1983]

2.7.1.104

Transferred entry:

diphosphate—protein phosphotransferase. Now EC 2.7.99.1, triphosphate—protein phosphotransferase

[EC 2.7.1.104 created 1987, deleted 2005]

2.7.1.105

Accepted name:

6-phosphofructo-2-kinase

Reaction:

ATP + β-D-fructose 6-phosphate = ADP + β-D-fructose 2,6-bisphosphate

Other name(s):

phosphofructokinase 2; 6-phosphofructose 2-kinase; 6-phosphofructo-2-kinase (phosphorylating); fructose 6-phosphate 2-kinase; ATP:D-fructose-6-phosphate 2-phosphotransferase

Systematic name:

ATP:β-D-fructose-6-phosphate 2-phosphotransferase

Comments:

Not identical with EC 2.7.1.11 6-phosphofructokinase. The enzyme co-purifies with EC 3.1.3.46 fructose-2,6-bisphosphate 2-phosphatase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 78689-77-7

References:

1.	Van Schaftingen, E. and Hers, H.-G. Phosphofructokinase 2: the enzyme that forms fructose 2,6-bisphosphate from fructose 6-phosphate and ATP. Biochem. Biophys. Res. Commun. 107 (1981) 1078–1084. [DOI] [PMID: 6458291]

[EC 2.7.1.105 created 1984]

2.7.1.106

Accepted name:

glucose-1,6-bisphosphate synthase

Reaction:

3-phospho-D-glyceroyl phosphate + α-D-glucose 1-phosphate = 3-phospho-D-glycerate + α-D-glucose 1,6-bisphosphate

Other name(s):

glucose 1,6-diphosphate synthase; glucose-1,6-bisphosphate synthetase; 3-phospho-D-glyceroyl-phosphate:D-glucose-1-phosphate 6-phosphotransferase

Systematic name:

3-phospho-D-glyceroyl-phosphate:α-D-glucose-1-phosphate 6-phosphotransferase

Comments:

D-Glucose 6-phosphate can act as acceptor, forming α-D-glucose 1,6-bisphosphate.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 56214-39-2

References:

1.	Rose, I.A., Warms, J.V.B. and Kaklij, G. A specific enzyme for glucose 1,6-bisphosphate synthesis. J. Biol. Chem. 250 (1975) 3466–3470. [PMID: 235548]

[EC 2.7.1.106 created 1984]

2.7.1.107

Accepted name:

diacylglycerol kinase (ATP)

Reaction:

ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate

Glossary:

1,2-diacyl-sn-glycerol 3-phosphate = phosphatidate

Other name(s):

diglyceride kinase (ambiguous); 1,2-diacylglycerol kinase (phosphorylating) (ambiguous); 1,2-diacylglycerol kinase (ambiguous); sn-1,2-diacylglycerol kinase (ambiguous); DG kinase (ambiguous); DGK (ambiguous); ATP:diacylglycerol phosphotransferase; arachidonoyl-specific diacylglycerol kinase; diacylglycerol:ATP kinase; ATP:1,2-diacylglycerol 3-phosphotransferase; diacylglycerol kinase (ATP dependent)

Systematic name:

ATP:1,2-diacyl-sn-glycerol 3-phosphotransferase

Comments:

Involved in synthesis of membrane phospholipids and the neutral lipid triacylglycerol. Activity is stimulated by certain phospholipids [4,7]. In plants and animals the product 1,2-diacyl-sn-glycerol 3-phosphate is an important second messenger. cf. EC 2.7.1.174, diacylglycerol kinase (CTP).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 60382-71-0

References:

1.	Hokin, L.E. and Hokin, M.R. Diglyceride kinase and other pathways for phosphatidic acid synthesis in the erythrocyte membrane. Biochim. Biophys. Acta 67 (1963) 470–484. [PMID: 13961253]
2.	Weissbach, H., Thomas, E. and Kaback, H.R. Studies on the metabolism of ATP by isolated bacterial membranes: formation and metabolism of membrane-bound phosphatidic acid. Arch. Biochem. Biophys. 147 (1971) 249–254. [DOI] [PMID: 4940043]
3.	Daleo, G.R., Piras, M.M. and Piras, R. Diglyceride kinase activity of microtubules. Characterization and comparison with the protein kinase and ATPase activities associated with vinblastine-isolated tubulin of chick embryonic muscles. Eur. J. Biochem. 68 (1976) 339–346. [DOI] [PMID: 185051]
4.	Walsh, J.P. and Bell, R.M. sn-1,2-Diacylglycerol kinase of Escherichia coli. Structural and kinetic analysis of the lipid cofactor dependence. J. Biol. Chem. 261 (1986) 15062–15069. [PMID: 3021764]
5.	Russ, E., Kaiser, U. and Sandermann, H., Jr. Lipid-dependent membrane enzymes. Purification to homogeneity and further characterization of diacylglycerol kinase from Escherichia coli. Eur. J. Biochem. 171 (1988) 335–342. [PMID: 2828054]
6.	Walsh, J.P. and Bell, R.M. Diacylglycerol kinase from Escherichia coli. Methods Enzymol. 209 (1992) 153–162. [DOI] [PMID: 1323028]
7.	Wissing, J.B. and Wagner, K.G. Diacylglycerol kinase from suspension cultured plant cells : characterization and subcellular localization. Plant Physiol. 98 (1992) 1148–1153. [PMID: 16668739]

[EC 2.7.1.107 created 1984, modified 2013]

2.7.1.108

Accepted name:

dolichol kinase

Reaction:

CTP + dolichol = CDP + dolichyl phosphate

Other name(s):

dolichol phosphokinase

Systematic name:

CTP:dolichol O-phosphotransferase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 71768-07-5

References:

1.	Burton, W.A., Scher, M.G. and Waechter, C.J. Enzymatic phosphorylation of dolichol in central nervous tissue. J. Biol. Chem. 254 (1979) 7129–7136. [PMID: 457672]
2.	Rip, J.W. and Carroll, K.K. Properties of a dolichol phosphokinase activity associated with rat liver microsomes. Can. J. Biochem. 58 (1980) 1051–1056. [PMID: 6257336]

[EC 2.7.1.108 created 1984]

2.7.1.109

Transferred entry:

[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase. Now EC 2.7.11.31, [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase

[EC 2.7.1.109 created 1984, deleted 2005]

2.7.1.110

Transferred entry:

dephospho-[reductase kinase] kinase. Now EC 2.7.11.3, dephospho-[reductase kinase] kinase

[EC 2.7.1.110 created 1984, deleted 2005]

2.7.1.111

Deleted entry:

[acetyl-CoA carboxylase] kinase. Now listed as EC 2.7.11.27, [acetyl-CoA carboxylase] kinase

[EC 2.7.1.111 created 1984, deleted 1992]

2.7.1.112

Transferred entry:

protein-tyrosine kinase. Now EC 2.7.10.2, non-specific protein-tyrosine kinase

[EC 2.7.1.112 created 1984, deleted 2005]

2.7.1.113

Accepted name:

deoxyguanosine kinase

Reaction:

ATP + deoxyguanosine = ADP + dGMP

Other name(s):

deoxyguanosine kinase (phosphorylating); (dihydroxypropoxymethyl)guanine kinase; 2′-deoxyguanosine kinase; NTP-deoxyguanosine 5′-phosphotransferase

Systematic name:

ATP:deoxyguanosine 5′-phosphotransferase

Comments:

Deoxyinosine can also act as acceptor.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39471-28-8

References:

1.	Barker, J. and Lewis, R.A. Deoxyguanosine kinase of neonatal mouse skin tissue. Biochim. Biophys. Acta 658 (1981) 111–123. [DOI] [PMID: 6260206]
2.	Gower, W.R., Jr., Carr, M.C. and Ives, D.H. Deoxyguanosine kinase. Distinct molecular forms in mitochondria and cytosol. J. Biol. Chem. 254 (1979) 2180–2183. [PMID: 218928]

[EC 2.7.1.113 created 1984]

2.7.1.114

Accepted name:

AMP—thymidine kinase

Reaction:

AMP + thymidine = adenosine + dTMP

Glossary:

dTMP = thymidine 5′-phosphate

Other name(s):

adenylate-nucleoside phosphotransferase

Systematic name:

AMP:thymidine 5′-phosphotransferase

Comments:

The deoxypyrimidine kinase complex induced by Herpes simplex virus catalyses this reaction as well as those of EC 2.7.1.21 (thymidine kinase), EC 2.7.1.118 (ADP—thymidine kinase) and EC 2.7.4.9 (dTMP kinase).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 60440-28-0

References:

1.	Falke, D., Labenz, J., Brauer, D. and Muller, W.E.G. Adenosine diphosphate: thymidine 5′-phosphotransferase, a new enzyme activity, associated with the Herpes simplex virus-induced deoxypyrimidine kinase. Biochim. Biophys. Acta 708 (1982) 99–103. [DOI] [PMID: 6293576]
2.	Falke, D., Nehrbass, W., Brauer, D. and Mueller, W.E.G. Adenylic acid: deoxythymidine 5′-phosphotransferase: evidence for the existence of a novel Herpes simplex virus-induced enzyme. J. Gen. Virol. 53 (1981) 247–255. [DOI] [PMID: 6267178]

[EC 2.7.1.114 created 1984]

2.7.1.115

Transferred entry:

[3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] kinase. Now EC 2.7.11.4, [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase

[EC 2.7.1.115 created 1986, deleted 2005]

2.7.1.116

Transferred entry:

[isocitrate dehydrogenase (NADP⁺)] kinase. Now EC 2.7.11.5, [isocitrate dehydrogenase (NADP⁺)] kinase

[EC 2.7.1.116 created 1986, deleted 2005]

2.7.1.117

Transferred entry:

myosin-light-chain kinase. Now EC 2.7.11.18, myosin-light-chain kinase

[EC 2.7.1.117 created 1986, deleted 2005]

2.7.1.118

Accepted name:

ADP—thymidine kinase

Reaction:

ADP + thymidine = AMP + dTMP

Glossary:

dTMP = thymidine 5′-phosphate

Other name(s):

ADP:dThd phosphotransferase; adenosine diphosphate-thymidine phosphotransferase

Systematic name:

ADP:thymidine 5′-phosphotransferase

Comments:

The deoxypyrimidine kinase complex induced by Herpes simplex virus catalyses this reaction as well as those of EC 2.7.1.21 (thymidine kinase), EC 2.7.1.114 (AMP—thymidine kinase) and EC 2.7.4.9 (dTMP kinase).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 82114-39-4

References:

1.	Falke, D., Labenz, J., Brauer, D. and Muller, W.E.G. Adenosine diphosphate: thymidine 5′-phosphotransferase, a new enzyme activity, associated with the Herpes simplex virus-induced deoxypyrimidine kinase. Biochim. Biophys. Acta 708 (1982) 99–103. [DOI] [PMID: 6293576]

[EC 2.7.1.118 created 1986]

2.7.1.119

Accepted name:

hygromycin-B 7′′-O-kinase

Reaction:

ATP + hygromycin B = ADP + 7′′-O-phosphohygromycin B

For diagram click here

Other name(s):

hygromycin B phosphotransferase; hygromycin-B kinase (ambiguous)

Systematic name:

ATP:hygromycin-B 7′′-O-phosphotransferase

Comments:

Phosphorylates the antibiotics hygromycin B, 1-N-hygromycin B and destomycin, but not hygromycin B2, at the 7′′-hydroxy group in the destomic acid ring.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 88361-67-5

References:

1.	Zalacain, M., Pardo, J.M. and Jiménez, A. Purification and characterization of a hygromycin B phosphotransferase from Streptomyces hygroscopicus. Eur. J. Biochem. 162 (1987) 419–422. [DOI] [PMID: 3026811]

[EC 2.7.1.119 created 1989, modified 2009, modified 2011]

2.7.1.120

Transferred entry:

caldesmon kinase. Now EC 2.7.11.17, Ca²⁺/calmodulin-dependent protein kinase

[EC 2.7.1.120 created 1989, modified 1990, deleted 2005]

2.7.1.121

Accepted name:

phosphoenolpyruvate—glycerone phosphotransferase

Reaction:

phosphoenolpyruvate + glycerone = pyruvate + glycerone phosphate

Glossary:

glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate

Systematic name:

phosphoenolpyruvate:glycerone phosphotransferase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 91755-81-6

References:

1.	Jin, R.Z. and Lin, E.C.C. An inducible phosphoenolpyruvate: dihydroxyacetone phosphotransferase system in Escherichia coli. J. Gen. Microbiol. 130 (1984) 83–88. [DOI] [PMID: 6368745]

[EC 2.7.1.121 created 1989]

2.7.1.122

Accepted name:

xylitol kinase

Reaction:

ATP + xylitol = ADP + xylitol 5-phosphate

Systematic name:

ATP:xylitol 5-phosphotransferase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 91273-86-8

References:

1.	Assev, S. and Roella, G. Evidence for presence of a xylitol phosphotransferase system in Streptococcus mutans OMZ 176. Acta Pathol. Microbiol. Immunol. Scand. 92B (1984) 89–92. [PMID: 6730972]

[EC 2.7.1.122 created 1989]

2.7.1.123

Transferred entry:

Ca²⁺/calmodulin-dependent protein kinase. Now EC 2.7.11.17, Ca²⁺/calmodulin-dependent protein kinase

[EC 2.7.1.123 created 1989, deleted 2005]

2.7.1.124

Transferred entry:

[tyrosine 3-monooxygenase] kinase. Now EC 2.7.11.6, [tyrosine 3-monooxygenase] kinase

[EC 2.7.1.124 created 1989, deleted 2005]

2.7.1.125

Transferred entry:

rhodopsin kinase. Now EC 2.7.11.14, rhodopsin kinase

[EC 2.7.1.125 created 1989 (EC 2.7.1.97 created 1978, incorporated 1992), deleted 2005]

2.7.1.126

Transferred entry:

[β-adrenergic-receptor] kinase. Now EC 2.7.11.15, β-adrenergic-receptor kinase

[EC 2.7.1.126 created 1989, deleted 2005]

2.7.1.127

Accepted name:

inositol-trisphosphate 3-kinase

Reaction:

ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate

For diagram of myo-inositol-phosphate biosynthesis, click here

Other name(s):

1D-myo-inositol-trisphosphate 3-kinase; Ins(1,4,5)P₃ 3-kinase

Systematic name:

ATP:1D-myo-inositol-1,4,5-trisphosphate 3-phosphotransferase

Comments:

Activated by Ca²⁺. Three isoforms have been shown to exist [3].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 106283-10-7

References:

1.	Hansen, C.A., Mah, S. and Williamson, J.R. Formation and metabolism of inositol 1,3,4,5-tetrakisphosphate in liver. J. Biol. Chem. 261 (1986) 8100–8103. [PMID: 3487541]
2.	Irvine, R.F., Letcher, A.J., Heslop, J.P. and Berridge, M.J. The inositol tris/tetrakisphosphate pathway - demonstration of Ins(1,4,5)P₃ 3-kinase activity in animal tissues. Nature 320 (1986) 631–634. [DOI] [PMID: 3010126]
3.	Irvine, R.F. and Schell, M.J. Back in the water - the return of the inositol phosphates. Nat. Rev. Mol. Cell. Biol. 2 (2001) 327–338. [DOI] [PMID: 11331907]

[EC 2.7.1.127 created 1989, modified 2002]

2.7.1.128

Transferred entry:

[acetyl-CoA carboxylase] kinase. Now EC 2.7.11.27, [acetyl-CoA carboxylase] kinase

[EC 2.7.1.128 created 1990 (EC 2.7.1.111 created 1984, incorporated 1992), deleted 2005]

2.7.1.129

Transferred entry:

[myosin-heavy-chain] kinase. Now EC 2.7.11.7, myosin-heavy-chain kinase

[EC 2.7.1.129 created 1990, deleted 2005]

2.7.1.130

Accepted name:

tetraacyldisaccharide 4′-kinase

Reaction:

ATP + a lipid A disaccharide = ADP + a lipid IV_A

For diagram of lipid IV_A biosynthesis, click here

Glossary:

a lipid A disaccharide = a dephospho-lipid IV_A = 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose
a lipid IV_A = 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose

Other name(s):

lpxK (gene name); lipid-A 4′-kinase; ATP:2,2′,3,3′-tetrakis[(3R)-3-hydroxytetradecanoyl]-β-D-glucosaminyl-(1→6)-α-D-glucosaminyl-phosphate 4′-O-phosphotransferase

Systematic name:

ATP:2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose 4′-O-phosphotransferase

Comments:

Involved with EC 2.3.1.129 (acyl-[acyl-carrier-protein]—UDP-N-acetylglucosamine O-acyltransferase) and EC 2.4.1.182 (lipid-A-disaccharide synthase) in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane of Gram-negative bacteria.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 107309-06-8

References:

1.	Ray, B.L. and Raetz, C.R.H. The biosynthesis of gram-negative endotoxin. A novel kinase in Escherichia coli membranes that incorporates the 4′-phosphate of lipid A. J. Biol. Chem. 262 (1987) 1122–1128. [PMID: 3027079]
2.	Emptage, R.P., Daughtry, K.D., Pemble, C.W., 4th and Raetz, C.R. Crystal structure of LpxK, the 4′-kinase of lipid A biosynthesis and atypical P-loop kinase functioning at the membrane interface. Proc. Natl. Acad. Sci. USA 109 (2012) 12956–12961. [DOI] [PMID: 22826246]
3.	Emptage, R.P., Pemble, C.W., 4th, York, J.D., Raetz, C.R. and Zhou, P. Mechanistic characterization of the tetraacyldisaccharide-1-phosphate 4′-kinase LpxK involved in lipid A biosynthesis. Biochemistry 52 (2013) 2280–2290. [DOI] [PMID: 23464738]
4.	Emptage, R.P., Tonthat, N.K., York, J.D., Schumacher, M.A. and Zhou, P. Structural basis of lipid binding for the membrane-embedded tetraacyldisaccharide-1-phosphate 4′-kinase LpxK. J. Biol. Chem. 289 (2014) 24059–24068. [DOI] [PMID: 25023290]

[EC 2.7.1.130 created 1990, modified 2021]

2.7.1.131

Transferred entry:

[low-density-lipoprotein] kinase. Now EC 2.7.11.29, low-density-lipoprotein receptor kinase

[EC 2.7.1.131 created 1990, deleted 2005]

2.7.1.132

Transferred entry:

tropomyosin kinase. Now EC 2.7.11.28, tropomyosin kinase

[EC 2.7.1.132 created 1990, deleted 2005]

2.7.1.133

Deleted entry:

inositol-trisphosphate 6-kinase. Now included with EC 2.7.1.134, inositol-tetrakisphosphate 1-kinase

[EC 2.7.1.133 created 1990, deleted 2002]

2.7.1.134

Accepted name:

inositol-tetrakisphosphate 1-kinase

Reaction:

ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate

For diagram of myo-inositol-phosphate biosynthesis, click here

Other name(s):

1D-myo-inositol-tetrakisphosphate 1-kinase; inositol-trisphosphate 6-kinase; 1D-myo-inositol-trisphosphate 6-kinase; ATP:1D-myo-inositol-1,3,4-trisphosphate 6-phosphotransferase; inositol-trisphosphate 5-kinase; 1D-myo-inositol-trisphosphate 5-kinase; ATP:1D-myo-inositol-1,3,4-trisphosphate 5-phosphotransferase

Systematic name:

ATP:1D-myo-inositol-3,4,5,6-tetrakisphosphate 1-phosphotransferase

Comments:

This enzyme also phosphorylates Ins(1,3,4)P₃ on O-5 and O-6. The phosphotransfer from ATP to either inositol 1,3,4-trisphosphate or inositol 3,4,5,6-tetrakisphosphate appears to be freely reversible to the extent that the enzyme can act like an inositol polyphosphate phosphatase in the presence of ADP. It can also catalyse an isomerization between Ins(1,3,4,5)P₄ and Ins(1,3,4,6)P₄ in the presence of ADP. The enzymes from animals and plants also have the activity of EC 2.7.1.159, inositol-1,3,4-trisphosphate 5/6-kinase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 187175-98-0

References:

1.	Stephens, L.R., Hawkins, P.T., Morris, A.J. and Downes, P.C. L-myo-Inositol 1,4,5,6-tetrakisphosphate (3-hydroxy)kinase. Biochem. J. 249 (1988) 283–292. [PMID: 2829850]
2.	Balla, T., Guillemette, G., Baukal, A.J. and Catt, K. Metabolism of inositol 1,3,4-trisphosphate to a new tetrakisphosphate isomer in angiotensin-stimulated adrenal glomerulosa cells. J. Biol. Chem. 262 (1987) 9952–9955. [PMID: 3497156]
3.	Shears, S.B., Parry, J.B., Tang, E.K.Y., Irvine, R.F., Michell, R.H. and Kirk, C.J. Metabolism of D-myo-inositol 1,3,4,5-tetrakisphosphate by rat liver, including the synthesis of a novel isomer of myo-inositol tetrakisphosphate. Biochem. J. 246 (1987) 139–147. [PMID: 2823793]
4.	Shears, S.B. The pathway of myo-inositol 1,3,4-trisphosphate phosphorylation in liver. Identification of myo-inositol 1,3,4-trisphosphate 6-kinase, myo-inositol 1,3,4-trisphosphate 5-kinase, and myo-inositol 1,3,4,6-tetrakisphosphate 5-kinase. J. Biol. Chem. 264 (1989) 19879–19886. [PMID: 2584198]
5.	Yang, X. and Shears, S.B. Multitasking in signal transduction by a promiscuous human Ins(3,4,5,6)P₄ 1-kinase/Ins(1,3,4)P₃ 5/6-kinase. Biochem. J. 351 (2000) 551–555. [PMID: 11042108]
6.	Ho, M.W., Yang, X., Carew, M.A., Zhang, T., Hua, L., Kwon, Y.U., Chung, S.K., Adelt, S., Vogel, G., Riley, A.M., Potter, B.V. and Shears, S.B. Regulation of Ins(3,4,5,6)P₄ signaling by a reversible kinase/phosphatase. Curr. Biol. 12 (2002) 477–482. [DOI] [PMID: 11909533]

[EC 2.7.1.134 created 1990, (EC 2.7.1.133 created 1989, incorporated 2002, EC 2.7.1.139 created 1992, incorporated 2002), modified 2002]

2.7.1.135

Transferred entry:

[tau-protein] kinase. Now EC 2.7.11.26, tau-protein kinase

[EC 2.7.1.135 created 1990, deleted 2005]

2.7.1.136

Accepted name:

macrolide 2′-kinase

Reaction:

ATP + oleandomycin = ADP + oleandomycin 2′-O-phosphate

Systematic name:

ATP:macrolide 2′-O-phosphotransferase

Comments:

Erythromycin, spiramycin and some other macrolide antibiotics can also act as acceptors.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 116036-69-2

References:

1.	O'Hara, K., Kanda, T. and Kono, M. Structure of a phosphorylated derivative of oleandomycin, obtained by reaction of oleandomycin with an extract of an erythromycin-resistant strain of Escherichia coli. J. Antibiot. 41 (1988) 823–827. [PMID: 3042731]

[EC 2.7.1.136 created 1992]

2.7.1.137

Accepted name:

phosphatidylinositol 3-kinase

Reaction:

ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate

For diagram of 1-phosphatidyl-myo-inositol metabolism, click here

Glossary:

1-phosphatidyl-1D-myo-inositol = PtdIns
1-phosphatidyl-1D-myo-inositol 3-phosphate = PtdIns3P

Other name(s):

1-phosphatidylinositol 3-kinase; type III phosphoinositide 3-kinase; Vps34p; type I phosphatidylinositol kinase

Systematic name:

ATP:1-phosphatidyl-1D-myo-inositol 3-phosphotransferase

Comments:

One mammalian isoform is known.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 115926-52-8

References:

1.	Whitman, M., Downes, C.P., Keeler, M., Keller, T. and Cantley, L. Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate. Nature 332 (1988) 644–646. [DOI] [PMID: 2833705]
2.	Vanhaesebroeck, B., Leevers, S.J., Ahmadi, K., Timms, J., Katso, R., Driscoll, P.C., Woscholski, R., Parker, P.J. and Waterfield, M.D. Synthesis and function of 3-phosphorylated inositol lipids. Annu. Rev. Biochem. 70 (2001) 535–602. [DOI] [PMID: 11395417]

[EC 2.7.1.137 created 1992, modified 2002]

2.7.1.138

Accepted name:

ceramide kinase

Reaction:

ATP + ceramide = ADP + ceramide 1-phosphate

Other name(s):

acylsphingosine kinase

Systematic name:

ATP:ceramide 1-phosphotransferase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 123175-68-8

References:

1.	Bajjalieh, S.M., Martin, T.F.J. and Floor, E. Synaptic vesicle ceramide kinase. A calcium-stimulated lipid kinase that co-purifies with brain synaptic vesicles. J. Biol. Chem. 264 (1989) 14354–14360. [PMID: 2547795]

[EC 2.7.1.138 created 1992]

2.7.1.139

Deleted entry:

inositol-trisphosphate 5-kinase. Now included with EC 2.7.1.134, inositol-tetrakisphosphate 1-kinase

[EC 2.7.1.139 created 1992, deleted 2002]

2.7.1.140

Accepted name:

inositol-tetrakisphosphate 5-kinase

Reaction:

ATP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate

Other name(s):

1D-myo-inositol-tetrakisphosphate 5-kinase

Systematic name:

ATP:1D-myo-inositol-1,3,4,6-tetrakisphosphate 5-phosphotransferase

Comments:

The enzyme from plants and yeast can also use Ins(1,2,3,4,6)P₅ as a substrate [2].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 123940-40-9

References:

1.	Shears, S.B. The pathway of myo-inositol 1,3,4-trisphosphate phosphorylation in liver. Identification of myo-inositol 1,3,4-trisphosphate 6-kinase, myo-inositol 1,3,4-trisphosphate 5-kinase, and myo-inositol 1,3,4,6-tetrakisphosphate 5-kinase. J. Biol. Chem. 264 (1989) 19879–19886. [PMID: 2584198]
2.	Stevenson-Paulik, J., Odom, A.R. and York, J.D. Molecular and biochemical characterization of two plant inositol polyphosphate 6-/3-/5-kinases. J. Biol. Chem. 277 (2002) 42711–42718. [DOI] [PMID: 12226109]

[EC 2.7.1.140 created 1992]

2.7.1.141

Transferred entry:

[RNA-polymerase]-subunit kinase. Now EC 2.7.11.23, [RNA-polymerase]-subunit kinase

[EC 2.7.1.141 created 1992, deleted 2005]

2.7.1.142

Accepted name:

glycerol-3-phosphate—glucose phosphotransferase

Reaction:

sn-glycerol 3-phosphate + D-glucose = glycerol + D-glucose 6-phosphate

Systematic name:

sn-glycerol-3-phosphate:D-glucose 6-phosphotransferase

Comments:

Involved in the anaerobic metabolism of sugars in the bloodstream of trypanosomes.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 125008-33-5

References:

1.	Kiaira, J.K. and Njogu, R.M. Evidence for glycerol 3-phosphate:glucose transphosphorylase activity in bloodstream Trypanosoma brucei brucei. Int. J. Biochem. 21 (1989) 839–845. [PMID: 2555230]

[EC 2.7.1.142 created 1992]

2.7.1.143

Accepted name:

diphosphate-purine nucleoside kinase

Reaction:

diphosphate + a purine nucleoside = phosphate + a purine mononucleotide

Other name(s):

pyrophosphate-purine nucleoside kinase

Systematic name:

diphosphate:purine nucleoside phosphotransferase

Comments:

The enzyme from the Acholeplasma class of Mollicutes catalyses the conversion of adenosine, guanosine and inosine to AMP, GMP and IMP. ATP cannot substitute for diphosphate as a substrate.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 70356-41-1

References:

1.	Tryon, V.V., Pollack, D. Purine metabolism in Acholeplasma laidlawii B: novel PPi-dependent nucleoside kinase activity. J. Bacteriol. 159 (1984) 265–270. [PMID: 6330034]
2.	Tryon, V.V., Pollack, J.D. Distinctions in Mollicutes purine metabolism: pyrophosphate-dependent nucleoside kinase and dependence on guanylate salvage. Int. J. Systematic Bacteriol. 35 (1985) 497–501.

[EC 2.7.1.143 created 1999]

2.7.1.144

Accepted name:

tagatose-6-phosphate kinase

Reaction:

ATP + D-tagatose 6-phosphate = ADP + D-tagatose 1,6-bisphosphate

Systematic name:

ATP:D-tagatose-6-phosphate 1-phosphotransferase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39434-00-9

References:

1.	Nobelmann, B. and Lengeler, J.W. Sequence of the gat operon for galactitol utilization from a wild-type strain EC3132 of Escherichia coli. Biochim. Biophys. Acta 1262 (1995) 69–72. [DOI] [PMID: 7772602]

[EC 2.7.1.144 created 1999]

2.7.1.145

Accepted name:

deoxynucleoside kinase

Reaction:

ATP + a 2′-deoxyribonucleoside = ADP + a 2′-deoxyribonucleoside 5′-phosphate

Other name(s):

multispecific deoxynucleoside kinase; ms-dNK; multisubstrate deoxyribonucleoside kinase; multifunctional deoxynucleoside kinase; D. melanogaster deoxynucleoside kinase; Dm-dNK; ATP:deoxynucleoside 5′-phosphotransferase

Systematic name:

ATP:deoxyribonucleoside 5′-phosphotransferase

Comments:

The enzyme from embryonic cells of the fruit fly Drosophila melanogaster differs from other 2′-deoxyribonucleoside kinases [EC 2.7.1.76 (deoxyadenosine kinase) and EC 2.7.1.113 (deoxyguanosine kinase)] in its broad specificity for all four common 2′-deoxyribonucleosides.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 52227-81-3

References:

1.	Munch-Petersen, B., Piskur, J. and Søndergaard, L. Four deoxynucleoside kinase activities from Drosophila melanogaster are contained within a single monomeric enzyme, a new multifunctional deoxynucleoside kinase. J. Biol. Chem. 273 (1998) 3926–3931. [DOI] [PMID: 9461577]
2.	Munch-Petersen, B., Knecht, W., Lenz, C., Søndergaard, L. and Piskur, J. Functional expression of a multisubstrate deoxyribonculeoside kinase from Drosophila melanogaster and its C-terminal deletion. J. Biol. Chem. 275 (2000) 6673–6679. [DOI] [PMID: 10692477]

[EC 2.7.1.145 created 2001]

2.7.1.146

Accepted name:

ADP-specific phosphofructokinase

Reaction:

ADP + D-fructose 6-phosphate = AMP + D-fructose 1,6-bisphosphate

For diagram of glycolysis, click here

Other name(s):

ADP-6-phosphofructokinase; ADP-dependent phosphofructokinase

Systematic name:

ADP:D-fructose-6-phosphate 1-phosphotransferase

Comments:

ADP can be replaced by GDP, ATP and GTP, to a limited extent. Divalent cations are necessary for activity, with Mg²⁺ followed by Co²⁺ being the most effective.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 237739-62-7

References:

Tuininga, J.E., Verhees, C.H., van der Oost, J., Kengen, S.W., Stams, A.J. and de Vos, W.M. Molecular and biochemical characterization of the ADP-dependent phosphofructokinase from the hyperthermophilic archaeon Pyrococcus furiosus. J. Biol. Chem. 274 (1999) 21023–21028. [DOI] [PMID: 10409652]

[EC 2.7.1.146 created 2001]

2.7.1.147

Accepted name:

ADP-specific glucose/glucosamine kinase

Reaction:

(1) ADP + D-glucose = AMP + D-glucose 6-phosphate
(2) ADP + D-glucosamine = AMP + D-glucosamine 6-phosphate

Other name(s):

ADP-specific glucokinase; ADP-dependent glucokinase

Systematic name:

ADP:D-glucose/D-glucosamine 6-phosphotransferase

Comments:

Requires Mg²⁺. The enzyme, characterized from a number of hyperthermophilic archaeal species, is highly specific for ADP. No activity is detected when ADP is replaced by ATP, GDP, phosphoenolpyruvate, diphosphate or polyphosphate.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 173585-07-4

References:

1.	Kengen, S.W., Tuininga, J.E., de Bok, F.A., Stams, A.J. and de Vos, W.M. Purification and characterization of a novel ADP-dependent glucokinase from the hyperthermophilic archaeon Pyrococcus furiosus. J. Biol. Chem. 270 (1995) 30453–30457. [DOI] [PMID: 8530474]
2.	Koga, S., Yoshioka, I., Sakuraba, H., Takahashi, M., Sakasegawa, S., Shimizu, S. and Ohshima, T. Biochemical characterization, cloning, and sequencing of ADP-dependent (AMP-forming) glucokinase from two hyperthermophilic archaea, Pyrococcus furiosus and Thermococcus litoralis. J. Biochem. 128 (2000) 1079–1085. [PMID: 11098152]
3.	Aslam, M., Takahashi, N., Matsubara, K., Imanaka, T., Kanai, T. and Atomi, H. Identification of the glucosamine kinase in the chitinolytic pathway of Thermococcus kodakarensis. J. Biosci. Bioeng. 125:S1389-1723( (2018). [PMID: 29146530]

[EC 2.7.1.147 created 2001, modified 2020]

2.7.1.148

Accepted name:

4-(cytidine 5′-diphospho)-2-C-methyl-D-erythritol kinase

Reaction:

ATP + 4-(cytidine 5′-diphospho)-2-C-methyl-D-erythritol = ADP + 2-phospho-4-(cytidine 5′-diphospho)-2-C-methyl-D-erythritol

For diagram of non-mevalonate terpenoid biosynthesis, click here

Other name(s):

CDP-ME kinase

Systematic name:

ATP:4-(cytidine 5′-diphospho)-2-C-methyl-D-erythritol 2-phosphotransferase

Comments:

The enzyme from Escherichia coli requires Mg²⁺ or Mn²⁺. Forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis (for diagram, click here).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 263016-77-9

References:

1.	Lüttgen, H., Rohdich, F., Herz, S., Wungsintaweekul, J., Hecht, S., Schuhr, C.A., Fellermeier, M., Sagner, S., Zenk, M.H., Bacher, A. and Eisenreich, W. Biosynthesis of terpenoids: YchB protein of Escherichia coli phosphorylates the 2-hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erithritol. Proc. Natl. Acad. Sci. USA 97 (2000) 1062–1067. [DOI] [PMID: 10655484]
2.	Kuzuyama, T., Takagi, M., Kaneda, K., Watanabe, H., Dairi, T. and Seto, H. Studies on the nonmevalonate pathway: conversion of 4-(cytidine 5′-diphospho)-2-C-methyl-D-erythritol to its 2-phospho derivative by 4-(cytidine 5′-diphospho)-2-C-methyl-D-erythritol kinase. Tetrahedron Lett. 41 (2000) 2925–2928.

[EC 2.7.1.148 created 2001]

2.7.1.149

Accepted name:

1-phosphatidylinositol-5-phosphate 4-kinase

Reaction:

ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate

For diagram of 1-phosphatidyl-myo-inositol metabolism (part 2), click here

Glossary:

1-phosphatidyl-1D-myo-inositol 5-phosphate = PtdIns5P
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = PtdIns(4,5)P₂

Other name(s):

type II PIP kinase

Systematic name:

ATP:1-phosphatidyl-1D-myo-inositol-5-phosphate 4-phosphotransferase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 247907-17-1

References:

1.	Rameh, L.E., Tolias, K.F., Duckworth, B.C. and Cantley, L.C. A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate. Nature 390 (1997) 192–196. [DOI] [PMID: 9367159]

[EC 2.7.1.149 created 2002]

2.7.1.150

Accepted name:

1-phosphatidylinositol-3-phosphate 5-kinase

Reaction:

ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate

For diagram of 1-phosphatidyl-myo-inositol metabolism, click here

Glossary:

1-phosphatidyl-1D-myo-inositol 3-phosphate = PtdIns3P
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate = PtdIns(3,5)P₂

Other name(s):

type III PIP kinase; phosphatidylinositol 3-phosphate 5-kinase

Systematic name:

ATP:1-phosphatidyl-1D-myo-inositol-3-phosphate 5-phosphotransferase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Cooke, F.T., Dove, S.K., McEwen, R.K., Painter, G., Holmes, A.B., Hall, M.N., Michell, R.H. and Parker, P.J. The stress-activated phosphatidylinositol 3-phosphate 5-kinase Fab1p is essential for vacuole function in S. cerevisiae. Curr. Biol. 9 (1998) 1219–1222. [DOI] [PMID: 9811604]

[EC 2.7.1.150 created 2002]