EC 2.7.1.1 to EC 2.7.1.50See separate file for EC 2.7.1.151 to EC 2.7.1.239
EC 2.7.1.51 to EC 2.7.1.100
EC 2.7.1.151 to EC 2.7.1.239
Accepted name: tagatose kinase
Reaction: ATP + D-tagatose = ADP + D-tagatose 6-phosphate
For diagram of reaction click here.
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. [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) 28963Ð28976. [PMID: 26472925]
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. [PMID: 6249593]
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. [PMID: 6163840]
[EC 2.7.1.104 Transferred entry: now EC 2.7.99.1, triphosphate—protein phosphotransferase (EC 2.7.1.104 created 1987, deleted 2005)]
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. [PMID: 6458291]
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]
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. [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. [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. [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]
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 2.7.1.109 Transferred entry: now EC 2.7.11.31, [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase (EC 2.7.1.109 created 1984, deleted 2005)]
[EC 2.7.1.110 Transferred entry: now EC 2.7.11.3, dephospho-[reductase kinase] kinase (EC 2.7.1.110 created 1984, deleted 2005)]
[EC 2.7.1.111 Deleted entry. Now listed as EC 2.7.1.128 [acetyl-CoA carboxylase] kinase (EC 2.7.1.111 created 1984, deleted 1992)]
[EC 2.7.1.112 Transferred entry: protein-tyrosine kinase. Now EC 2.7.10.1, receptor protein-tyrosine kinase and EC 2.7.10.2, non-specific protein-tyrosine kinase (EC 2.7.1.112 created 1984, deleted 2005)]
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. [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]
Accepted name: AMP—thymidine kinase
Reaction: AMP + thymidine = adenosine + dTMP
Glossary: dTMP = thymidine 5'-phosphate
Other name(s): adenylate-nucleoside phosphotransferase;
AMP:dThd kinase; adenylic acid:deoxythymidine 5'-phosphotransferase; AMP:deoxythymidine kinase; AMP:deoxythymidine 5'-phosphotransferase; thymidine 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 Mueller, 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. [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. [PMID: 6267178]
[EC 2.7.1.115 Transferred entry: now EC 2.7.11.4, [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase (EC 2.7.1.115 created 1986, deleted 2005)]
[EC 2.7.1.116 Transferred entry: now EC 2.7.11.5, [isocitrate dehydrogenase (NADP+)] kinase. (EC 2.7.1.116 created 1986, deleted 2005)]
[EC 2.7.1.117 Transferred entry: now EC 2.7.11.18, myosin-light-chain kinase (EC 2.7.1.117 created 1986, deleted 2005)]
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 Mueller, 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. [PMID: 6293576]
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. [PMID: 3026811]
[EC 2.7.1.120 Transferred entry: caldesmon kinase. Now part of EC 2.7.11.17, Ca2+/calmodulin-dependent protein kinase (EC 2.7.1.120 created 1989, modified 1990, deleted 2005)]
Accepted name: phosphoenolpyruvate—glycerone phosphotransferase
Reaction: phosphoenolpyruvate + glycerone = pyruvate + glycerone 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. [PMID: 6368745]
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 2.7.1.123 Transferred entry: calmodulin-dependent protein kinase. Now part of EC 2.7.11.17, Ca2+/calmodulin-dependent protein kinase (EC 2.7.1.123 created 1989, deleted 2005)]
[EC 2.7.1.124 Transferred entry: now EC 2.7.11.6, [tyrosine 3-monooxygenase] kinase (EC 2.7.1.124 created 1989, deleted 2005)]
[EC 2.7.1.125 Transferred entry: 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)]
[EC 2.7.1.126 Transferred entry: now EC 2.7.11.15, β-adrenergic-receptor kinase (EC 2.7.1.126 created 1989, deleted 2005)]
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 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. [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. [PMID: 11331907]
[EC 2.7.1.128 Transferred entry: 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)]
[EC 2.7.1.129 Transferred entry: now EC 2.7.11.7, myosin-heavy-chain [EC 2.7.1.129 created 1990, deleted 2005]
Accepted name: tetraacyldisaccharide 4'-kinase
Reaction: ATP + a lipid A disaccharide = ADP + a lipid IVA
For diagram of reaction click here
Glossary: a lipid A disaccharide = a dephospho-lipid IVA = 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 IVA = 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. [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. [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. [PMID: 25023290]
[EC 2.7.1.131 Transferred entry: now EC 2.7.11.29, low-density-lipoprotein receptor kinase (EC 2.7.1.131 created 1990, deleted 2005)]
[EC 2.7.1.132 Transferred entry: now EC 2.7.11.28, tropomyosin kinase (EC 2.7.1.132 created 1990, deleted 2005)]
[EC 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)]
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 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 signalling by a reversible kinase/phosphatase. Curr. Biol. 12 (2002) 477-482. [PMID: 11909533]
[EC 2.7.1.135 Transferred entry: now EC 2.7.11.26, tau-protein kinase (EC 2.7.1.135 created 1990, deleted 2005)]
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]
Accepted name: phosphatidylinositol 3-kinase
Reaction: ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
For diagram click here.
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. [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. [PMID: 11395417]
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 2.7.1.139 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)]
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. [PMID: 12226109]
[EC 2.7.1.141 Transferred entry: now EC 2.7.11.23, [RNA-polymerase]-subunit kinase (EC 2.7.1.141 created 1992, deleted 2005)]
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]
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.
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., 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. [PMID: 7772602]
Accepted name: deoxynucleoside kinase
Reaction: ATP + 2'-deoxyribonucleoside = ADP + 2'-deoxyribonucleoside 5'-phosphate
Other names: multispecific deoxynucleoside kinase; ms-dNK; multisubstrate deoxyribonucleoside kinase; multifunctional deoxynucleoside kinase; D. melanogaster deoxynucleoside kinase; Dm-dNK
Systematic name: ATP:deoxynucleoside 5'-phosphotransferase
Comments: The enzyme from embryonic cells of Drosophila melanogaster differs from other 2'-deoxyribonucleoside kinases [EC 2.7.1.76 (2'-deoxyadenosine kinase) and EC 2.7.1.113 (deoxyguanosine kinase)] in its broad specificity for all four common deoxynucleosides.
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. [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. [PMID: 10692477]
Accepted name: ADP-specific phosphofructokinase
Reaction: ADP + D-fructose 6-phosphate = AMP + D-fructose 1,6-bisphosphate
For diagram of reaction 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:
1. 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. [PMID: 10409652]
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. [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 (2018) S1389-1723(. [PMID: 29146530]
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 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. [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.
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 click here.
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. [PMID: 9367159]
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 click here.
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, CAS registry number:
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. [PMID: 9811604]