Enzyme Nomenclature

EC 2.7.1 Phosphotransferases with an Alcohol Group as Acceptor (Continued)

Continued from EC 2.7.1.1 to EC 2.7.1.50

See separate file for EC 2.7.1.101 to EC 2.7.1.150,
EC 2.7.1.151 to EC 2.7.1.224.

Contents

EC 2.7.1.51 L-fuculokinase
EC 2.7.1.52 fucokinase
EC 2.7.1.53 L-xylulokinase
EC 2.7.1.54 D-arabinokinase
EC 2.7.1.55 allose kinase
EC 2.7.1.56 1-phosphofructokinase
EC 2.7.1.57 deleted
EC 2.7.1.58 2-dehydro-3-deoxygalactonokinase
EC 2.7.1.59 N-acetylglucosamine kinase
EC 2.7.1.60 N-acylmannosamine kinase
EC 2.7.1.61 acyl-phosphate—hexose phosphotransferase
EC 2.7.1.62 phosphoramidate—hexose phosphotransferase
EC 2.7.1.63 polyphosphate—glucose phosphotransferase
EC 2.7.1.64 inositol 3-kinase
EC 2.7.1.65 scyllo-inosamine 4-kinase
EC 2.7.1.66 undecaprenol kinase
EC 2.7.1.67 1-phosphatidylinositol 4-kinase
EC 2.7.1.68 1-phosphatidylinositol-4-phosphate 5-kinase
EC 2.7.1.69 protein-Nπ-phosphohistidine—sugar phosphotransferase
EC 2.7.1.69 now covered by EC 2.7.1.191, EC 2.7.1.192, EC 2.7.1.193, EC 2.7.1.194, EC 2.7.1.195, EC 2.7.1.196, EC 2.7.1.197, EC 2.7.1.198, EC 2.7.1.199, EC 2.7.1.200, EC 2.7.1.201, EC 2.7.1.202,EC 2.7.1.203, EC 2.7.1.204, EC 2.7.1.205, EC 2.7.1.206, EC 2.7.1.207, EC 2.7.1.208.
EC 2.7.1.70 identical to EC 2.7.1.37.
EC 2.7.1.71 shikimate kinase
EC 2.7.1.72 streptomycin 6-kinase
EC 2.7.1.73 inosine kinase
EC 2.7.1.74 deoxycytidine kinase
EC 2.7.1.75 now EC 2.7.1.21
EC 2.7.1.76 2'-deoxyadenosine kinase
EC 2.7.1.77 nucleoside phosphotransferase
EC 2.7.1.78 polynucleotide 5'-hydroxyl-kinase
EC 2.7.1.79 diphosphate—glycerol phosphotransferase
EC 2.7.1.80 diphosphate—serine phosphotransferase
EC 2.7.1.81 hydroxylysine kinase
EC 2.7.1.82 ethanolamine kinase
EC 2.7.1.83 pseudouridine kinase
EC 2.7.1.84 alkylglycerone kinase
EC 2.7.1.85 β-glucoside kinase
EC 2.7.1.86 NADH kinase
EC 2.7.1.87 streptomycin 3"-kinase
EC 2.7.1.88 dihydrostreptomycin-6-phosphate 3'α-kinase
EC 2.7.1.89 thiamine kinase
EC 2.7.1.90 diphosphate—fructose-6-phosphate 1-phosphotransferase
EC 2.7.1.91 sphingosine kinase
EC 2.7.1.92 5-dehydro-2-deoxygluconokinase
EC 2.7.1.93 alkylglycerol kinase
EC 2.7.1.94 acylglycerol kinase
EC 2.7.1.95 kanamycin kinase
EC 2.7.1.96 deleted, included in EC 2.7.1.86
EC 2.7.1.97 deleted, identical to EC 2.7.1.125
EC 2.7.1.98 deleted
EC 2.7.1.99 now EC 2.7.11.2
EC 2.7.1.100 S-methyl-5-thioribose kinase

Continued with:

EC 2.7.1.101 to EC 2.7.1.150
EC 2.7.1.151 to EC 2.7.1.224

Entries

EC 2.7.1.51

Accepted name: L-fuculokinase

Reaction: ATP + L-fuculose = ADP + L-fuculose 1-phosphate

Other name(s): L-fuculokinase (phosphorylating); L-fuculose kinase

Systematic name: ATP:L-fuculose 1-phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9026-64-6

References:

1. Heath, E.C. and Ghalambor, M.A. The metabolism of L-fucose. I. The purification and properties of L-fuculose kinase. J. Biol. Chem. 237 (1962) 2423-2426.

[EC 2.7.1.51 created 1965]

EC 2.7.1.52

Accepted name: fucokinase

Reaction: ATP + L-fucose = ADP + β-L-fucose 1-phosphate

For diagram click here.

Other name(s): fucokinase (phosphorylating); fucose kinase; L-fucose kinase; L-fucokinase; ATP:6-deoxy-L-galactose 1-phosphotransferase; ATP:L-fucose 1-phosphotransferase

Systematic name: ATP:β-L-fucose 1-phosphotransferase

Comments: Requires a divalent cation for activity, with Mg2+ and Fe2+ giving rise to the highest enzyme activity. Forms part of a salvage pathway for reutilization of L-fucose. Can also phosphorylate D-arabinose, but more slowly.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-00-5

References:

1. Ishihara, H., Massaro, D.J. and Heath, E.C. The metabolism of L-fucose. 3. The enzymatic synthesis of β-L-fucose 1-phosphate. J. Biol. Chem. 243 (1968) 1103-1109. [PMID: 5646161]

2. Butler, W. and Serif, G.S. Fucokinase, its anomeric specificity and mechanism of phosphate group transfer. Biochim. Biophys. Acta 829 (1985) 238-243. [PMID: 2986701]

3. Park, S.H., Pastuszak, I., Drake, R. and Elbein, A.D. Purification to apparent homogeneity and properties of pig kidney L-fucose kinase. J. Biol. Chem. 273 (1998) 5685-5691. [PMID: 9488699]

[EC 2.7.1.52 created 1972, modified 2004]

EC 2.7.1.53

Accepted name: L-xylulokinase

Reaction: ATP + L-xylulose = ADP + L-xylulose 5-phosphate

Other name(s): L-xylulokinase (phosphorylating)

Systematic name: ATP:L-xylulose 5-phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-01-6

References:

1. Anderson, R.L. and Wood, W.A. Purification and properties of L-xylulokinase. J. Biol. Chem. 237 (1962) 1029-1033.

[EC 2.7.1.53 created 1972]

EC 2.7.1.54

Accepted name: D-arabinokinase

Reaction: ATP + D-arabinose = ADP + D-arabinose 5-phosphate

Other name(s): D-arabinokinase (phosphorylating)

Systematic name: ATP:D-arabinose 5-phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-02-7

References:

1. Volk, W.A. Purification and properties of D-arabinokinase from Propionibacterium pentosaceum. J. Biol. Chem. 237 (1962) 19-23.

[EC 2.7.1.54 created 1972]

EC 2.7.1.55

Accepted name: allose kinase

Reaction: ATP + D-allose = ADP + D-allose 6-phosphate

Other name(s): allokinase (phosphorylating); allokinase; D-allokinase; D-allose-6-kinase

Systematic name: ATP:D-allose 6-phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9031-78-1

References:

1. Gibbins, L.N. and Simpson, F.J. The purification and properties of D-allose-6-kinase from Aerobacter aerogenes. Can. J. Microbiol. 9 (1963) 769-779.

[EC 2.7.1.55 created 1972]

EC 2.7.1.56

Accepted name: 1-phosphofructokinase

Reaction: ATP + D-fructose 1-phosphate = ADP + D-fructose 1,6-bisphosphate

Other name(s): fructose-1-phosphate kinase; 1-phosphofructokinase (phosphorylating); D-fructose-1-phosphate kinase; fructose 1-phosphate kinase; phosphofructokinase 1

Systematic name: ATP:D-fructose-phosphate 6-phosphotransferase

Comments: ITP, GTP or UTP can replace ATP.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-03-8

References:

1. Reeves, R.E., Warren, L.G. and Hsu, D.S. 1-Phosphofructokinase from an anaerobe. J. Biol. Chem. 241 (1966) 1257-1261. [PMID: 4222878]

2. Sapico, V. and Anderson, R.L. D-Fructose 1-phosphate kinase and D-fructose 6-phosphate kinase from Aerobacter aerogenes. A comparative study of regulatory properties. J. Biol. Chem. 244 (1969) 6280-6288. [PMID: 4242639]

[EC 2.7.1.56 created 1972]

[EC 2.7.1.57 Deleted entry: mannitol kinase (EC 2.7.1.57 created 1972, deleted 1984)]

EC 2.7.1.58

Accepted name: 2-dehydro-3-deoxygalactonokinase

Reaction: ATP + 2-dehydro-3-deoxy-D-galactonate = ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate

For diagram of reaction click here.

Other name(s): 2-keto-3-deoxygalactonokinase; 2-keto-3-deoxygalactonate kinase (phosphorylating); 2-oxo-3-deoxygalactonate kinase;

Systematic name: ATP:2-dehydro-3-deoxy-D-galactonate 6-phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37278-05-0

References:

1. Stouthamer, A.H. Glucose and galactose metabolism in Gluconobacter liquefaciens. Biochim. Biophys. Acta 48 (1961) 484-500.

[EC 2.7.1.58 created 1972]

EC 2.7.1.59

Accepted name: N-acetylglucosamine kinase

Reaction: ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-D-glucosamine 6-phosphate

Other name(s): acetylglucosamine kinase (phosphorylating); ATP:2-acetylamino-2-deoxy-D-glucose 6-phosphotransferase; 2-acetylamino-2-deoxy-D-glucose kinase; acetylaminodeoxyglucokinase

Systematic name: ATP:N-acetyl-D-glucosamine 6-phosphotransferase

Comments: The bacterial enzyme also acts on D-glucose.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9027-48-9

References:

1. Asensio, C. and Ruiz-Amil, M. N-Acetyl-D-glucosamine kinase. II. Escherichia coli. Methods Enzymol. 9 (1966) 421-425.

2. Barkulis, S.S. N-Acetyl-D-glucosamine kinase. I. Streptococcus pyrogenes. Methods Enzymol. 9 (1966) 415-420.

3. Datta, A. Studies on hog spleen N-acetylglucosamine kinase. I. Purification and properties of N-acetylglucosamine kinase. Biochim. Biophys. Acta 220 (1970) 51-60. [PMID: 4319609]

[EC 2.7.1.59 created 1972]

EC 2.7.1.60

Accepted name: N-acylmannosamine kinase

Reaction: ATP + N-acyl-D-mannosamine = ADP + N-acyl-D-mannosamine 6-phosphate

For diagram of reaction click here.

Other name(s): acylmannosamine kinase (phosphorylating); acetylamidodeoxymannokinase; acetylmannosamine kinase; acylaminodeoxymannokinase; acylmannosamine kinase; N-acyl-D-mannosamine kinase; N-acetylmannosamine kinase; ATP:N-acetylmannosamine 6-phosphotransferase

Systematic name: ATP:N-acyl-D-mannosamine 6-phosphotransferase

Comments: Acts on the acetyl and glycolyl derivatives.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9027-53-6

References:

1. Banerjee, S. and Ghosh, S. Purification and properties of N-acetylmannosamine kinase from Salmonella typhimurium. Eur. J. Biochem. 8 (1969) 200-206. [PMID: 4889177]

2. Ghosh, S. and Roseman, S. Enzymatic phosphorylation of N-acetyl-D-mannosamine. Proc. Natl. Acad. Sci. USA 47 (1961) 955-958.

3. Kundig, W., Ghosh, S. and Roseman, S. The sialic acids. VII. N-Acyl-D-mannosamine kinase from rat liver. J. Biol. Chem. 241 (1966) 5619-5626. [PMID: 5928201]

[EC 2.7.1.60 created 1972]

EC 2.7.1.61

Accepted name: acyl-phosphate—hexose phosphotransferase

Reaction: acyl phosphate + D-hexose = a carboxylate + D-hexose phosphate

Other name(s): hexose phosphate:hexose phosphotransferase

Systematic name: acyl-phosphate:D-hexose phosphotransferase

Comments: Phosphorylates D-glucose and D-mannose on O-6, and D-fructose on O-1 or O-6.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-06-1

References:

1. Anderson, R.L. and Kamel, M.Y. Acyl phosphate:hexose phosphotransferase (hexose phosphate:hexose phosphotransferase). Methods Enzymol. 9 (1966) 392-396.

2. Kamel, M.Y. and Anderson, R.L. Acyl phosphate: hexose phosphotransferase. Purification and properties of the enzyme from Aerobacter aerogenes and evidence for its common identity with hexose phosphate: hexose phosphotransferase. Arch. Biochem. Biophys. 120 (1967) 322-331. [PMID: 6033450]

3. Casazza, J.P. and Fromm, H.J. Purification and initial rate kinetics of acyl-phosphate-hexose phosphotransferase from Aerobacter aerogenes. Biochemistry 16 (1977) 3091-3097. [PMID: 196625]

[EC 2.7.1.61 created 1972, modified 2011]

EC 2.7.1.62

Accepted name: phosphoramidate—hexose phosphotransferase

Reaction: phosphoramidate + D-hexose = NH3 + α-D-hexose 1-phosphate

Other name(s): phosphoramidate-hexose transphosphorylase; phosphoramidic-hexose transphosphorylase; phosphoramidate:hexose 1-phosphotransferase

Systematic name: phosphoramidate:D-hexose 1-phosphotransferase

Comments: Activity is observed with several hexoses; of these glucose is the best substrate and the product from it is α-D-glucose 1-phosphate. The phosphoramidate donor can be replaced by N-phosphoglycine and by an N-phosphohistidine. May be identical with EC 3.1.3.9 glucose-6-phosphatase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9031-45-2

References:

1. Smith R.A. and Thiesen, M.C. Phosphoramidate-hexose transphosphorylase. Methods Enzymol. 9 (1966) 403-407.

[EC 2.7.1.62 created 1972]

EC 2.7.1.63

Accepted name: polyphosphate—glucose phosphotransferase

Reaction: (phosphate)n + D-glucose = (phosphate)n-1 + D-glucose 6-phosphate

Other name(s): polyphosphate glucokinase; polyphosphate-D-(+)-glucose-6-phosphotransferase; polyphosphate-glucose 6-phosphotransferase

Systematic name: polyphosphate:D-glucose 6-phosphotransferase

Comments: Requires a neutral salt, e.g. KCl, for maximum activity. Also acts on glucosamine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9033-50-5

References:

1. Szymona, M. Purification and properties of a new hexokinase utilizing inorganic pyrophosphate. Acta Biochim. Pol. 9 (1962) 165-181.

2. Szymona, M. and Ostrowski, W. Inorganic polyphosphate glucokinase of Mycobacterium phlei. Biochim. Biophys. Acta 85 (1964) 283-295.

[EC 2.7.1.63 created 1972]

EC 2.7.1.64

Accepted name: inositol 3-kinase

Reaction: ATP + myo-inositol = ADP + 1D-myo-inositol 3-phosphate

Other name(s): inositol-1-kinase (phosphorylating); myoinositol kinase; myo-inositol 1-kinase

Systematic name: ATP:myo-inositol 1-phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-07-2

References:

1. English, P.D., Dietz, M. and Albersheim, P. Myoinositol kinase: partial purification and identification of product. Science 151 (1966) 198-199.

2. Loewus, M.W., Sasaki, K., Leavitt, A.C., Muscell, L., Sherman, W.R. and Loewus, F.A. Enantiomeric form of myo-inositol-1-phosphate produced by myo-inositol-1-phosphate synthase and myoinositol kinase in higher-plants. Plant Physiol. 70 (1982) 1661-1663.

3.Stephens, L.R., Kay, R.R. and Irvine, R.F. A myo-inositol D-3 hydroxykinase activity in Dictyostelium. Biochem. J. 272 (1990) 201-210. [PMID: 2176081]

[EC 2.7.1.64 created 1972, modified 2001]

EC 2.7.1.65

Accepted name: scyllo-inosamine 4-kinase

Reaction: ATP + 1-amino-1-deoxy-scyllo-inositol = ADP + 1-amino-1-deoxy-scyllo-inositol 4-phosphate

Other name(s): scyllo-inosamine kinase (phosphorylating); scyllo-inosamine kinase; ATP:inosamine phosphotransferase

Systematic name: ATP:1-amino-1-deoxy-scyllo-inositol 4-phosphotransferase

Comments: Also acts on streptamine, 2-deoxystreptamine and 1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-08-3

References:

1. Walker, J.B. Enzymic reactions involved in streptomycin biosynthesis and metabolisms. Lloydia 34 (1971) 363-371.

2. Walker, J.B. and Walker, M.S. Enzymatic synthesis of streptidine from scyllo-inosamine. Biochemistry 6 (1967) 3821-3829. [PMID: 6076630]

[EC 2.7.1.65 created 1972, modified 1976]

EC 2.7.1.66

Accepted name: undecaprenol kinase

Reaction: ATP + undecaprenol = ADP + undecaprenyl phosphate

Other name(s): isoprenoid alcohol kinase; isoprenoid alcohol phosphokinase; C55-isoprenoid alcohol phosphokinase; isoprenoid alcohol kinase (phosphorylating); C55-isoprenoid alcohol kinase; C55-isoprenyl alcohol phosphokinase; polyisoprenol kinase

Systematic name: ATP:undecaprenol phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9068-22-8

References:

1. Higashi, Y., Siewert, G. and Strominger, J.L. Biosynthesis of the peptidoglycan of bacterial cell walls. XIX. Isoprenoid alcohol phosphokinase. J. Biol. Chem. 245 (1970) 3683-3690. [PMID: 4248528]

[EC 2.7.1.66 created 1972]

EC 2.7.1.67

Accepted name: 1-phosphatidylinositol 4-kinase

Reaction: ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate

For diagram click here.

Other name(s): phosphatidylinositol kinase (phosphorylating); phosphatidylinositol 4-kinase; phosphatidylinositol kinase; type II phosphatidylinositol kinase; PI kinase; PI 4-kinase

Systematic name: ATP:1-phosphatidyl-1D-myo-inositol 4-phosphotransferase

Comments: This reaction is catalysed by at least two different isoforms.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 37205-54-2

References:

1. Colodzin, M. and Kennedy, E.P. Biosynthesis of diphosphoinositide in brain. J. Biol. Chem. 240 (1965) 3771-3780. [PMID: 4284712]

2. Kai, M., White, G.L. and Hawthorne, J.N. The phosphatidylinositol kinase of rat brain. Biochem. J. 101 (1966) 328-337. [PMID: 4290722]

3. Walker, D.H., Dougherty, N. and Pike, L.J. Purification and characterization of a phosphatidylinositol kinase from A431 cells. Biochemistry 27 (1988) 6504-6511. [PMID: 2851325]

4. 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]

5. Barylko, B., Gerber, S.H., Binns, D.D., Grichine, N., Khvotchev, M., Sudhof, T.C. and Albanesi, J.P. A novel family of phosphatidylinositol 4-kinases conserved from yeast to humans. J. Biol. Chem. 276 (2001) 7705-7708. [PMID: 11244087]

[EC 2.7.1.67 created 1972, modified 1982, modified 2002]

EC 2.7.1.68

Accepted name: 1-phosphatidylinositol-4-phosphate 5-kinase

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

For diagram click here.

Other name(s): diphosphoinositide kinase; PIP kinase; phosphatidylinositol 4-phosphate kinase; phosphatidylinositol-4-phosphate 5-kinase; type I PIP kinase

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

Comments: This enzyme can also phosphorylate PtdIns3P in the 4-position, and PtdIns, PtdIns3P and PtdIns(3,4)P2 in the 5-position in vitro, but to a lesser extent. The last of these reactions occurs in vivo and is physiologically relevant. Three different isoforms are known.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 104645-76-3

References:

1. Kai, M., Salway, J.G. and Hawthorne, J.N. The diphosphoinositide kinase of rat brain. Biochem. J. 106 (1968) 791-801. [PMID: 4295336]

2. Kai, M., Salway, J.G., Michell, R.H. and Hawthorne, J.N. The biosynthesis of triphosphoinositide by rat brain in vitro. Biochem. Biophys. Res. Commun. 22 (1966) 370-375.

3. 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]

[EC 2.7.1.68 created 1972, modified 1980, modified 1982, modified 2002]

[EC 2.7.1.69 Transferred entry: protein-Nπ-phosphohistidine—sugar phosphotransferase, now covered by EC 2.7.1.191 protein-Nπ-phosphohistidine—D-mannose phosphotransferase, EC 2.7.1.192 protein-Nπ-phosphohistidine—N-acetylmuramate phosphotransferase, EC 2.7.1.193 protein-Nπ-phosphohistidine—N-acetyl-D-glucosamine phosphotransferase, EC 2.7.1.194 protein-Nπ-phosphohistidine—L-ascorbate phosphotransferase, EC 2.7.1.195 protein-Nπ-phosphohistidine—2-O-α-mannosyl-D-glycerate phosphotransferase, EC 2.7.1.196 protein-Nπ-phosphohistidine—N,N'-diacetylchitobiose phosphotransferase, EC 2.7.1.197 protein-Nπ-phosphohistidine—D-mannitol phosphotransferase, EC 2.7.1.198 protein-Nπ-phosphohistidine—D-sorbitol phosphotransferase, EC 2.7.1.199 protein-Nπ-phosphohistidine—D-glucose phosphotransferase, EC 2.7.1.200 protein-Nπ-phosphohistidine—galactitol phosphotransferase, EC 2.7.1.201 protein-Nπ-phosphohistidine—trehalose phosphotransferase, EC 2.7.1.202 protein-Nπ-phosphohistidine—D-fructose phosphotransferase, EC 2.7.1.203 protein-Nπ-phosphohistidine—D-glucosaminate phosphotransferase, EC 2.7.1.204 protein-Nπ-phosphohistidine—D-galactose phosphotransferase, EC 2.7.1.205 protein-Nπ-phosphohistidine—D-cellobiose phosphotransferase, EC 2.7.1.206 protein-Nπ-phosphohistidine—L-sorbose phosphotransferase, EC 2.7.1.207 protein-Nπ-phosphohistidine—lactose phosphotransferase and EC 2.7.1.208 protein-Nπ-phosphohistidine—maltose phosphotransferase. (EC 2.7.1.69 created 1972, modified 2000, deleted 2016)]

[EC 2.7.1.70 Deleted entry: protamine kinase. This enzyme is not dependent on cAMP as was thought and is therefore identical to EC 2.7.1.37, protein kinase. (EC 2.7.1.70 created 1972, deleted 2004)]

EC 2.7.1.71

Accepted name: shikimate kinase

Reaction: ATP + shikimate = ADP + 3-phosphoshikimate

For diagram click here.

Other name(s): shikimate kinase (phosphorylating); shikimate kinase II

Systematic name: ATP:shikimate 3-phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9031-51-0

References:

1. Morell, H. and Sprinson, D.B. Shikimate kinase isoenzymes in Salmonella typhimurium. J. Biol. Chem. 243 (1968) 676-677. [PMID: 4866525]

[EC 2.7.1.71 created 1972]

EC 2.7.1.72

Accepted name: streptomycin 6-kinase

Reaction: ATP + streptomycin = ADP + streptomycin 6-phosphate

Other name(s): streptidine kinase; SM 6-kinase; streptomycin 6-kinase (phosphorylating); streptidine kinase (phosphorylating); streptomycin 6-O-phosphotransferase; streptomycin 6-phosphotransferase

Systematic name: ATP:streptomycin 6-phosphotransferase

Comments: dATP can replace ATP; and dihydrostreptomycin, streptidine and
2-deoxystreptidine can act as acceptors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-11-8

References:

1. Walker, J.B. and Skorvaga, M. Phosphorylation of streptomycin and dihydrostreptomycin by Streptomyces. Enzymatic synthesis of different diphosphorylated derivatives. J. Biol. Chem. 248 (1973) 2435-2440. [PMID: 4121456]

2. Walker, J.B. and Walker, M.S. Streptomycin biosynthesis. Enzymatic synthesis of O-phosphorylstreptidine from streptidine and adenosinetriphosphate. Biochim. Biophys. Acta 148 (1967) 335-341. [PMID: 6075410]

[EC 2.7.1.72 created 1972, modified 1976]

EC 2.7.1.73

Accepted name: inosine kinase

Reaction: ATP + inosine = ADP + IMP

Other name(s): inosine-guanosine kinase; inosine kinase (phosphorylating)

Systematic name: ATP:inosine 5'-phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37237-46-0

References:

1. Pierre, K.J. and LePage, G.A. Formation of inosine-5'-monophosphate by a kinase in cell-free extracts of Ehrlich ascites cells in vitro. Proc. Soc. Exp. Biol. Med. 127 (1968) 432-440. [PMID: 5645030]

[EC 2.7.1.73 created 1972]

EC 2.7.1.74

Accepted name: deoxycytidine kinase

Reaction: NTP + deoxycytidine = NDP + dCMP

Other name(s): deoxycytidine kinase (phosphorylating); 2'-deoxycytidine kinase; Ara-C kinase; arabinofuranosylcytosine kinase; deoxycytidine-cytidine kinase

Systematic name: NTP:deoxycytidine 5'-phosphotransferase

Comments: Cytosine arabinoside can act as acceptor; all natural nucleoside triphosphates (except dCTP) can act as donors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9039-45-6

References:

1. Durham, J.P. and Ives, D.H. Deoxycytidine kinase. II. Purification and general properties of the calf thymus enzyme. J. Biol. Chem. 245 (1970) 2276-2284. [PMID: 5442271]

2. Ives, D.H. and Durham, J.P. Deoxycytidine kinase. 3. Kinetics and allosteric regulation of the calf thymus enzyme. J. Biol. Chem. 245 (1970) 2285-2294. [PMID: 5462538]

3. Kessel, D. Properties of deoxycytidine kinase partially purified from L1210 cells. J. Biol. Chem. 243 (1968) 4739-4744.

4. Momparler, R.L. and Fischer, G.A. Mammalian deoxynucleoside kinase. I. Deoxycytidine kinase: purification, properties, and kinetic studies with cytosine arabinoside. J. Biol. Chem. 243 (1968) 4298-4304. [PMID: 5684726]

[EC 2.7.1.74 created 1972]

[EC 2.7.1.75 Deleted entry: thymidine kinase. Now EC 2.7.1.21 thymidine kinase (EC 2.7.1.75 created 1972, deleted 1976)]

EC 2.7.1.76

Accepted name: 2'-deoxyadenosine kinase

Reaction: ATP + 2'-deoxyadenosine = ADP + dAMP

Other name(s): purine-deoxyribonucleoside kinase

deoxyadenosine kinase (phosphorylating) (ambiguous); purine-deoxyribonucleoside kinase (ambiguous); deoxyadenosine kinase (ambiguous); ATP:deoxyadenosine 5'-phosphotransferase (ambiguous)

Systematic name: ATP:2'-deoxyadenosine 5'-phosphotransferase

Comments: 2'-Deoxyguanosine can also act as acceptor. Possibly identical with EC 2.7.1.74 deoxycytidine kinase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-12-9

References:

1. Chang, C.H., Brockman, R.W. and Bennett, L.L., Jr. Purification and some properties of a deoxyribonucleoside kinase from L1210 cells. Cancer Res. 42 (1982) 3033-3039. [PMID: 6284353]

2. Krygier, V. and Momparler, R.L. The regulatory properties of deoxyadenosine kinase. Biochim. Biophys. Acta 161 (1968) 578-580. [PMID: 5667299]

[EC 2.7.1.76 created 1972]

EC 2.7.1.77

Accepted name: nucleoside phosphotransferase

Reaction: a nucleotide + a 2'-deoxyribonucleoside = a nucleoside + a 2'-deoxyribonucleoside 5'-phosphate

Other name(s): nonspecific nucleoside phosphotransferase; nucleotide:3'-deoxynucleoside 5'-phosphotransferase

Systematic name: nucleotide:nucleoside 5'-phosphotransferase

Comments: Phenyl phosphate and nucleoside 3'-phosphates can act as donors, although not so well as nucleoside 5'-phosphates. Nucleosides as well as 2'-deoxyribonucleosides can act as acceptors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9055-37-2

References:

1. Brunngraber, E.F. and Chargaff, E. Purification and properties of a nucleoside phosphotransferase from carrot. J. Biol. Chem. 242 (1967) 4834-4840. [PMID: 6061424]

2. Prasher, D.C., Carr, M.C., Ives, D.H., Tsai, T.-C. and Frey, P.A. Nucleoside phosphotransferase from barley. Characterization and evidence for ping pong kinetics involving phosphoryl enzyme. J. Biol. Chem. 257 (1982) 4931-4939. [PMID: 6279651]

[EC 2.7.1.77 created 1972]

EC 2.7.1.78

Accepted name: polynucleotide 5'-hydroxyl-kinase

Reaction: ATP + 5'-dephospho-DNA = ADP + 5'-phospho-DNA

Other name(s): 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; polynucleotide 5'-hydroxy-kinase

Systematic name: ATP:5'-dephosphopolynucleotide 5'-phosphotransferase

Comments: Also acts on 5'-dephospho-RNA 3'-mononucleotides.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37211-65-7

References:

1. Novogrodsky, A. and Hurwitz, J. The enzymatic phosphorylation of ribonucleic acid and deoxyribonucleic acid. I. Phosphorylation at 5'-hydroxyl termini. J. Biol. Chem. 241 (1966) 2923-2932. [PMID: 4287929]

2. Novogrodsky, A., Tal, M., Traub, A. and Hurwitz, J. The enzymatic phosphorylation of ribonucleic acid and deoxyribonucleic acid. II. Further properties of the 5'-hydroxyl polynucleotide kinase. J. Biol. Chem. 241 (1966) 2933-2943. [PMID: 4287930]

[EC 2.7.1.78 created 1972]

EC 2.7.1.79

Accepted name: diphosphate—glycerol phosphotransferase

Reaction: diphosphate + glycerol = phosphate + glycerol 1-phosphate

Other name(s): PPi-glycerol phosphotransferase; pyrophosphate-glycerol phosphotransferase

Systematic name: diphosphate:glycerol 1-phosphotransferase

Comments: May be identical with EC 3.1.3.9 glucose-6-phosphatase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-13-0

References:

1. Stetten, M.R. Enzymatic synthesis of glycerol I-phosphate. Elevation in diabetic and fasted animals, compared with glucose-6-phosphatase and related enzyme activities. Biochim. Biophys. Acta 208 (1970) 394-403. [PMID: 4319153]

[EC 2.7.1.79 created 1972]

EC 2.7.1.80

Accepted name: diphosphate—serine phosphotransferase

Reaction: diphosphate + L-serine = phosphate + O-phospho-L-serine

For diagram of reaction click here.

Other name(s): pyrophosphate-serine phosphotransferase; pyrophosphate-L-serine phosphotransferase

Systematic name: diphosphate:L-serine O-phosphotransferase

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 37205-58-6

References:

1. Cagen, L.M. and Friedmann, H.C. Enzymatic phosphorylation of serine. J. Biol. Chem. 247 (1972) 3382-3392. [PMID: 4337852]

[EC 2.7.1.80 created 1972]

EC 2.7.1.81

Accepted name: hydroxylysine kinase

Reaction: GTP + 5-hydroxy-L-lysine = GDP + 5-phosphooxy-L-lysine

Other name(s): hydroxylysine kinase (phosphorylating); guanosine triphosphate:5-hydroxy-L-lysine O-phosphotransferase

Systematic name: GTP:5-hydroxy-L-lysine O-phosphotransferase

Comments: Both the natural 5-hydroxy-L-lysine and its 5-epimer act as acceptors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9073-58-9

References:

1. Hiles, R.A. and Henderson, L.M. The partial purification and properties of hydroxylysine kinase from rat liver. J. Biol. Chem. 247 (1972) 646-651. [PMID: 4621658]

[EC 2.7.1.81 created 1972]

EC 2.7.1.82

Accepted name: ethanolamine kinase

Reaction: ATP + ethanolamine = ADP + O-phosphoethanolamine

Other name(s): ethanolamine kinase (phosphorylating); ethanolamine phosphokinase

Systematic name: ATP:ethanolamine O-phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9075-78-9

References:

1. Faulkner, A. and Turner, J.M. Phosphorylation of ethanolamine in catabolism: biodegradative adenosine triphosphate-ethanolamine phosphotransferase and related enzymes in bacteria. Biochem. Soc. Trans. 2 (1974) 133-136.

2. Sung, C.-P. and Johnstone, R.M. Phosphorylation of choline and ethanolamine in Ehrlich ascites-carcinoma cells. Biochem. J. 105 (1967) 497-503. [PMID: 5626092]

3. Weinhold, P.A. and Rethy, V.B. Ethanolamine phosphokinase: activity and properties during liver development. Biochim. Biophys. Acta 276 (1972) 143-154. [PMID: 5047700]

[EC 2.7.1.82 created 1976]

EC 2.7.1.83

Accepted name: pseudouridine kinase

Reaction: ATP + pseudouridine = ADP + pseudouridine 5'-phosphate

Other name(s): pseudouridine kinase (phosphorylating)

Systematic name: ATP:pseudouridine 5'-phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 62213-40-5

References:

1. Solomon, L.R. and Breitman, T.R. Pseudouridine kinase of Escherichia coli: a new enzyme. Biochem. Biophys. Res. Commun. 44 (1971) 299-304. [PMID: 4334133]

[EC 2.7.1.83 created 1976]

EC 2.7.1.84

Accepted name: alkylglycerone kinase

Reaction: ATP + O-alkylglycerone = ADP + O-alkylglycerone phosphate

Other name(s): alkyldihydroxyacetone kinase (phosphorylating); alkyldihydroxyacetone kinase

Systematic name: ATP:O-alkylglycerone phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 52227-80-2

References:

1. Chae, K., Piantadosi, C. and Snyder, F. Reductase, phosphatase, and kinase activities in the metabolism of alkyldihydroxyacetone phosphate and alkyldihydroxyacetone. J. Biol. Chem. 248 (1973) 6718-6723. [PMID: 4147653]

[EC 2.7.1.84 created 1976]

EC 2.7.1.85

Accepted name: β-glucoside kinase

Reaction: ATP + cellobiose = 6-phospho-β-D-glucosyl-(1→4)-D-glucose

Other name(s): β-D-glucoside kinase (phosphorylating)

Systematic name: ATP:cellobiose 6-phosphotransferase

Comments: Phosphorylates a number of β-D-glucosides; GTP, CTP, ITP and UTP can also act as donors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37205-53-1

References:

1. Palmer, R.E. and Anderson, R.L. Cellobiose metabolism in Aerobacter aerogenes. II. Phosphorylation of cellobiose with adenosine 5'-triphosphate by a β-glucoside kinase. J. Biol. Chem. 247 (1972) 3415-3419. [PMID: 5030625]

[EC 2.7.1.85 created 1976]

EC 2.7.1.86

Accepted name: NADH kinase

Reaction: ATP + NADH = ADP + NADPH

Other name(s): reduced nicotinamide adenine dinucleotide kinase (phosphorylating); DPNH kinase; reduced diphosphopyridine nucleotide kinase; NADH2 kinase

Systematic name: ATP:NADH 2'-phosphotransferase

Comments: CTP, ITP, UTP and GTP can also act as phosphate donors (in decreasing order of activity). The enzyme is specific for NADH. Activated by acetate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 62213-39-2

References:

1. Griffiths, M.M. and Bernofsky, C. Purification and properties of reduced diphosphopyridine nucleotide kinase from yeast mitochondria. J. Biol. Chem. 247 (1972) 1473-1478. [PMID: 4335000]

[EC 2.7.1.86 created 1976 (EC 2.7.1.96 created 1978, incorporated 1978)]

EC 2.7.1.87

Accepted name: streptomycin 3"-kinase

Reaction: ATP + streptomycin = ADP + streptomycin 3"-phosphate

Other name(s): streptomycin 3"-kinase (phosphorylating); streptomycin 3"-phosphotransferase

Systematic name: ATP:streptomycin 3"-phosphotransferase

Comments: Also phosphorylates dihydrostreptomycin, 3'-deoxydihydrostreptomycin and their 6-phosphates.

Links to other databases: BRENDA, EXPASY, KEMetacyc, CAS registry number: 39391-15-6

References:

1. Walker, J.B. and Skorvaga, M. Phosphorylation of streptomycin and dihydrostreptomycin by Streptomyces. Enzymatic synthesis of different diphosphorylated derivatives. J. Biol. Chem. 248 (1973) 2435-2440. [PMID: 4121456]

[EC 2.7.1.87 created 1976]

EC 2.7.1.88

Accepted name: dihydrostreptomycin-6-phosphate 3'α-kinase

Reaction: ATP + dihydrostreptomycin 6-phosphate = ADP + dihydrostreptomycin 3'α,6-bisphosphate

Other name(s): dihydrostreptomycin 6-phosphate kinase (phosphorylating); ATP:dihydrostreptomycin-6-P 3'α-phosphotransferase

Systematic name: ATP:dihydrostreptomycin-6-phosphate 3'α-phosphotransferase

Comments: 3'-Deoxydihydrostreptomycin 6-phosphate can also act as acceptor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 39391-14-5

References:

1. Walker, J.B. and Skorvaga, M. Phosphorylation of streptomycin and dihydrostreptomycin by Streptomyces. Enzymatic synthesis of different diphosphorylated derivatives. J. Biol. Chem. 248 (1973) 2435-2440. [PMID: 4121456]

[EC 2.7.1.88 created 1976]

EC 2.7.1.89

Accepted name: thiamine kinase

Reaction: ATP + thiamine = ADP + thiamine phosphate

Other name(s): thiamin kinase (phosphorylating); thiamin phosphokinase; ATP:thiamin phosphotransferase; thiamin kinase

Systematic name: ATP:thiamine phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 62213-38-1

References:

1. Iwashima, A., Nishino, H. and Nose, Y. Conversion of thiamine to thiamine monophosphate by cell-free extracts of Escherichia coli. Biochim. Biophys. Acta 258 (1972) 333-337. [PMID: 4550803]

[EC 2.7.1.89 created 1976]

EC 2.7.1.90

Accepted name: diphosphate—fructose-6-phosphate 1-phosphotransferase

Reaction: diphosphate + D-fructose 6-phosphate = phosphate + D-fructose 1,6-bisphosphate

For diagram of reaction click here.

Other name(s): 6-phosphofructokinase (pyrophosphate); pyrophosphate-fructose 6-phosphate 1-phosphotransferase; inorganic pyrophosphate-dependent phosphofructokinase; inorganic pyrophosphate-phosphofructokinase; pyrophosphate-dependent phosphofructo-1-kinase; pyrophosphate-fructose 6-phosphate phosphotransferase

Systematic name: diphosphate:D-fructose-6-phosphate 1-phosphotransferase

Comments: The enzyme catalyses a similar reaction to EC 2.7.1.11, 6-phosphofructokinase, but utilizes diphosphate instead of ATP as the the phosphate donor. It has been described in higher plants, primitive eukaryotes, bacteria, and archaea.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 55326-40-4

References:

1. Reeves, R.E., Serrano, R. and South, D.J. 6-Phosphofructokinase (pyrophosphate). Properties of the enzyme from Entamoeba histolytica and its reaction mechanism. J. Biol. Chem. 251 (1976) 2958-2962. [PMID: 178659]

2. Reeves, R.E., South, D.J., Blytt, H.J. and Warren, L.G. Pyrophosphate:D-fructose 6-phosphate 1-phosphotransferase. A new enzyme with the glycolytic function of 6-phosphofructokinase. J. Biol. Chem. 249 (1974) 7737-7741. [PMID: 4372217]

3. Carlisle, S.M., Blakeley, S.D., Hemmingsen, S.M., Trevanion, S.J., Hiyoshi, T., Kruger, N.J. and Dennis, D.T. Pyrophosphate-dependent phosphofructokinase. Conservation of protein sequence between the α- and β-subunits and with the ATP-dependent phosphofructokinase. J. Biol. Chem. 265 (1990) 18366-18371. [PMID: 2170409]

4. Ladror, U.S., Gollapudi, L., Tripathi, R.L., Latshaw, S.P. and Kemp, R.G. Cloning, sequencing, and expression of pyrophosphate-dependent phosphofructokinase from Propionibacterium freudenreichii. J. Biol. Chem. 266 (1991) 16550-16555. [PMID: 1653240]

5. Siebers, B., Klenk, H.P. and Hensel, R. PPi-dependent phosphofructokinase from Thermoproteus tenax, an archaeal descendant of an ancient line in phosphofructokinase evolution. J. Bacteriol. 180 (1998) 2137-2143. [PMID: 9555897]

[EC 2.7.1.90 created 1976]

EC 2.7.1.91

Accepted name: sphingosine kinase

Reaction: ATP + a sphingoid base = ADP + a sphingoid base 1-phosphate

Other name(s): SPHK1 (gene name); SPHK2 (gene name); dihydrosphingosine kinase; dihydrosphingosine kinase (phosphorylating); sphingosine kinase (phosphorylating); sphingoid base kinase; sphinganine kinase; ATP:sphinganine 1-phosphotransferase

Systematic name: ATP:sphingoid base 1-phosphotransferase

Comments: The enzyme is involved in the production of sphingolipid metabolites. It phosphorylates various sphingoid long-chain bases, such as sphingosine, D-erythro-dihydrosphingosine (sphinganine), phytosphingosine (4-hydroxysphinganine), 4-hydroxy-8-sphingenine, 4,8-sphingadienine and D-threo-dihydrosphingosine and L-threo-dihydrosphingosine. The exact substrate range depends on the species.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 50864-48-7

References:

1. Stoffel, W., Heimann, G. and Hellenbroich, B. Sphingosine kinase in blood platelets. Hoppe-Seyler's Z. Physiol. Chem. 354 (1973) 562-566. [PMID: 4372149]

2. Stoffel, W., Bauer, E. and Stahl, J. The metabolism of sphingosine bases in Tetrahymena pyriformis. Sphingosine kinase and sphingosine-1-phosphate lyase. Hoppe-Seyler's Z. Physiol. Chem. 355 (1974) 61-74. [PMID: 4373374]

3. Nagiec, M.M., Skrzypek, M., Nagiec, E.E., Lester, R.L. and Dickson, R.C. The LCB4 (YOR171c) and LCB5 (YLR260w) genes of Saccharomyces encode sphingoid long chain base kinases. J. Biol. Chem. 273 (1998) 19437-19442. [PMID: 9677363]

4. Kohama, T., Olivera, A., Edsall, L., Nagiec, M.M., Dickson, R. and Spiegel, S. Molecular cloning and functional characterization of murine sphingosine kinase. J. Biol. Chem. 273 (1998) 23722-23728. [PMID: 9726979]

5. Liu, H., Sugiura, M., Nava, V.E., Edsall, L.C., Kono, K., Poulton, S., Milstien, S., Kohama, T. and Spiegel, S. Molecular cloning and functional characterization of a novel mammalian sphingosine kinase type 2 isoform. J. Biol. Chem. 275 (2000) 19513-19520. [PMID: 10751414]

6. Worrall, D., Liang, Y.K., Alvarez, S., Holroyd, G.H., Spiegel, S., Panagopulos, M., Gray, J.E. and Hetherington, A.M. Involvement of sphingosine kinase in plant cell signalling. Plant J. 56 (2008) 64-72. [PMID: 18557834]

[EC 2.7.1.91 created 1976, modified 1980, modified 2016]

EC 2.7.1.92

Accepted name: 5-dehydro-2-deoxygluconokinase

Reaction: ATP + 5-dehydro-2-deoxy-D-gluconate = ADP + 6-phospho-5-dehydro-2-deoxy-D-gluconate

For diagram of reaction click here.

Other name(s): 5-keto-2-deoxygluconokinase; 5-keto-2-deoxyglucono kinase (phosphorylating); DKH kinase

Systematic name: ATP:5-dehydro-2-deoxy-D-gluconate 6-phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 62213-35-8

References:

1. Anderson, W.A. and Magasanik, B. The pathway of myo-inositol degradation in Aerobacter aerogenes. Conversion of 2-deoxy-5-keto-D-gluconic acid to glycolytic intermediates. J. Biol. Chem. 246 (1971) 5662-5675. [PMID: 4328832]

[EC 2.7.1.92 created 1976]

EC 2.7.1.93

Accepted name: alkylglycerol kinase

Reaction: ATP + 1-O-alkyl-sn-glycerol = ADP + 1-O-alkyl-sn-glycerol 3-phosphate

Other name(s): 1-alkylglycerol kinase (phosphorylating); ATP-alkylglycerol phosphotransferase; alkylglycerol phosphotransferase; ATP: 1-alkyl-sn-glycerol phosphotransferase

Systematic name: ATP:1-O-alkyl-sn-glycerol 3-phosphotransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 55354-37-5

References:

1. Rock, C.O. and Snyder, F. Biosynthesis of 1-alkyl-sn-glycero-3-phosphate via adenosine triphosphate:1-alkyl-sn-glycerol phosphotransferase. J. Biol. Chem. 249 (1974) 5382-5387. [PMID: 4369816]

[EC 2.7.1.93 created 1976]

EC 2.7.1.94

Accepted name: acylglycerol kinase

Reaction: ATP + acylglycerol = ADP + acyl-sn-glycerol 3-phosphate

Other name(s): monoacylglycerol kinase; monoacylglycerol kinase (phosphorylating); sn-2-monoacylglycerol kinase; MGK; monoglyceride kinase; monoglyceride phosphokinase

Systematic name: ATP:acylglycerol 3-phosphotransferase

Comments: Acts on both 1- and 2-acylglycerols.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 62213-37-0

References:

1. Pieringer, R.A. and Hokin, L.E. Biosynthesis of lysophosphatidic acid from monoglyceride and adenosine triphosphate. J. Biol. Chem. 237 (1962) 653-658.

2. Pieringer, R.A. and Kunnes, R.S. The biosynthesis of phosphatidic acid and lysophosphatidic acid by glyceride phosphokinase pathways in Escherichia coli. J. Biol. Chem. 240 (1965) 2833-2838.

[EC 2.7.1.94 created 1976]

EC 2.7.1.95

Accepted name: kanamycin kinase

Reaction: ATP + kanamycin = ADP + kanamycin 3'-phosphate

Glossary: kanamycin

Other name(s): neomycin-kanamycin phosphotransferase;

kanamycin kinase (phosphorylating); neomycin phosphotransferase

Systematic name: ATP:kanamycin 3'-O-phosphotransferase

Comments: Also acts on the antibiotics neomycin, paromomycin, neamine, paromamine, vistamycin and gentamicin A. An enzyme from Pseudomonas aeruginosa also acts on butirosin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 62213-36-9

References:

1. Doi, O., Ogura, M., Tanaka, N. and Umezawa, H. Inactivation of kanamycin, neomycin, and streptomycin by enzymes obtained in cells of Pseudomonas aeruginosa. Appl. Microbiol. 16 (1968) 1276-1281. [PMID: 4970990]

2. Dolin, M.I. The Streptococcus faecalis oxidases for reduced diphosphopyridine nucleotide. III. Isolation and properties of a flavin peroxidase for reduced diphosphopyridine nucleotide. J. Biol. Chem. 225 (1957) 557-573.

[EC 2.7.1.95 created 1976]

[EC 2.7.1.96 Deleted entry: NADH kinase. Now included with EC 2.7.1.86 NADH kinase (EC 2.7.1.96 created 1978, deleted 1978)]

[EC 2.7.1.97 Deleted entry: identical with EC 2.7.1.125 rhodopsin kinase (EC 2.7.1.97 created 1978, deleted 1992)]

[EC 2.7.1.98 Deleted entry: phosphoenolpyruvate—fructose phosphotransferase (EC 2.7.1.98 created 1978, deleted 1984)]

[EC 2.7.1.99 Transferred entry: now EC 2.7.11.2, [pyruvate dehydrogenase (acetyl-transferring)] kinase (EC 2.7.1.99 created 1978, deleted 2005)]

EC 2.7.1.100

Accepted name: S-methyl-5-thioribose kinase

Reaction: ATP + S-methyl-5-thio-D-ribose = ADP + S-methyl-5-thio-α-D-ribose 1-phosphate

For diagram click here.

Other name(s): 5-methylthioribose kinase (phosphorylating); methylthioribose kinase; 5-methylthioribose kinase; ATP:S5-methyl-5-thio-D-ribose 1-phosphotransferase

Systematic name: ATP:S-methylmethyl-5-thio-D-ribose 1-phosphotransferase

Comments: CTP also acts, but more slowly.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 68247-56-3

References:

1. Ferro, A.J., Barrett, A. and Shapiro, S.K. 5-Methylthioribose kinase. A new enzyme involved in the formation of methionine from 5-methylthioribose. J. Biol. Chem. 253 (1978) 6021-6025. [PMID: 210167]

2. Guranowski, A. Plant 5-methylthioribose kinase. Plant Physiol. 71 (1983) 932-935.

[EC 2.7.1.100 created 1980]


Continued with EC 2.7.1.101 to EC 2.7.1.172
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