ExplorEnz: EC 2.7.1*

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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, PDB, 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. [PMID: 13905785]

[EC 2.7.1.51 created 1965]

2.7.1.52

Accepted name:

fucokinase

Reaction:

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

For diagram of GDP-L-fucose and GDP-mannose biosynthesis, 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. [DOI] [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. [DOI] [PMID: 9488699]

[EC 2.7.1.52 created 1972, modified 2004]

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. [PMID: 13861293]

[EC 2.7.1.53 created 1972]

2.7.1.54

Accepted name:

D-arabinokinase

Reaction:

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

For diagram of D-arabinose catabolism, click here

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. [PMID: 13926593]

[EC 2.7.1.54 created 1972]

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, PDB, 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]

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, PDB, 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]

2.7.1.57

Deleted entry:

mannitol kinase

[EC 2.7.1.57 created 1972, deleted 1984]

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 the Entner-Doudoroff pathway, 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]

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. [DOI] [PMID: 4319609]

[EC 2.7.1.59 created 1972]

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 N-Acetylneuraminic acid biosynthesis, 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. [DOI] [PMID: 4889177]
2.	Ghosh, S. and Roseman, S. Enzymatic phosphorylation of N-acetyl-D-mannosamine. Proc. Natl. Acad. Sci. USA 47 (1961) 955–958. [PMID: 13704957]
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]

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. [DOI] [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]

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]

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, PDB, 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. [PMID: 14212975]

[EC 2.7.1.63 created 1972]

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, PDB, 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. [DOI] [PMID: 5907906]
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. [PMID: 16662739]
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]

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. Enzymatic reactions involved in streptomycin biosynthesis and metabolism. Lloydia 34 (1971) 363–371. [PMID: 4376579]
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]

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]

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

Glossary:

1-phosphatidyl-1D-myo-inositol = PtdIns
1-phosphatidyl-1D-myo-inositol 4-phosphate = PtdIns4P

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. [DOI] [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. [DOI] [PMID: 11244087]

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

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

Glossary:

1-phosphatidyl-1D-myo-inositol = PtdIns
1-phosphatidyl-1D-myo-inositol 3-phosphate = PtdIns3P
1-phosphatidyl-1D-myo-inositol 4-phosphate = PtdIns4P
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate = PtdIns(3,4)P₂
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = PtdIns(4,5)P₂

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. [DOI] [PMID: 9367159]

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

2.7.1.69

Transferred entry:

protein-N^π-phosphohistidine—sugar phosphotransferase, now covered by EC 2.7.1.191 protein-N^π-phosphohistidine—D-mannose phosphotransferase, EC 2.7.1.192 protein-N^π-phosphohistidine—N-acetylmuramate phosphotransferase, EC 2.7.1.193 protein-N^π-phosphohistidine—N-acetyl-D-glucosamine phosphotransferase, EC 2.7.1.194 protein-N^π-phosphohistidine—L-ascorbate phosphotransferase, EC 2.7.1.195 protein-N^π-phosphohistidine—2-O-α-mannosyl-D-glycerate phosphotransferase, EC 2.7.1.196 protein-N^π-phosphohistidine—N,N′-diacetylchitobiose phosphotransferase, EC 2.7.1.197 protein-N^π-phosphohistidine—D-mannitol phosphotransferase, EC 2.7.1.198 protein-N^π-phosphohistidine—D-sorbitol phosphotransferase, EC 2.7.1.199 protein-N^π-phosphohistidine—D-glucose phosphotransferase, EC 2.7.1.200 protein-N^π-phosphohistidine—galactitol phosphotransferase, EC 2.7.1.201 protein-N^π-phosphohistidine—trehalose phosphotransferase, EC 2.7.1.202 protein-N^π-phosphohistidine—D-fructose phosphotransferase, EC 2.7.1.203 protein-N^π-phosphohistidine—D-glucosaminate phosphotransferase, EC 2.7.1.204 protein-N^π-phosphohistidine—D-galactose phosphotransferase, EC 2.7.1.205 protein-N^π-phosphohistidine—cellobiose phosphotransferase, EC 2.7.1.206 protein-N^π-phosphohistidine—L-sorbose phosphotransferase, EC 2.7.1.207 protein-N^π-phosphohistidine—lactose phosphotransferase and EC 2.7.1.208 protein-N^π-phosphohistidine—maltose phosphotransferase.

[EC 2.7.1.69 created 1972, modified 2000, deleted 2016]

2.7.1.70

Deleted entry:

protamine kinase. Now included in EC 2.7.11.1, non-specific serine/threonine protein kinase

[EC 2.7.1.70 created 1972, deleted 2004]

2.7.1.71

Accepted name:

shikimate kinase

Reaction:

ATP + shikimate = ADP + 3-phosphoshikimate

For diagram of shikimate and chorismate biosynthesis, 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]

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. [DOI] [PMID: 6075410]

[EC 2.7.1.72 created 1972, modified 1976]

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, PDB, 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]

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. [PMID: 5687717]
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]

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]

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, PDB, 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. [DOI] [PMID: 5667299]

[EC 2.7.1.76 created 1972]

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, PDB, 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]

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]

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. [DOI] [PMID: 4319153]

[EC 2.7.1.79 created 1972]

2.7.1.80

Accepted name:

diphosphate—serine phosphotransferase

Reaction:

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

For diagram of serine biosynthesis, 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]

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]

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. [DOI] [PMID: 5047700]

[EC 2.7.1.82 created 1976]

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, PDB, 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. [DOI] [PMID: 4334133]

[EC 2.7.1.83 created 1976]

2.7.1.84

Accepted name:

alkylglycerone kinase

Reaction:

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

Glossary:

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

2.7.1.85

Accepted name:

β-glucoside kinase

Reaction:

ATP + cellobiose = ADP + 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]

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)]

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, KEGG, MetaCyc, 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]

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]

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. [DOI] [PMID: 4550803]

[EC 2.7.1.89 created 1976]

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 glycolysis, 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. PP_i-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]

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, PDB, 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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 18557834]

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

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 inositol catabolism, 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]

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]

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, PDB, 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. [PMID: 14486486]
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. [PMID: 14342303]

[EC 2.7.1.94 created 1976]

2.7.1.95

Accepted name:

kanamycin kinase

Reaction:

ATP + kanamycin = ADP + kanamycin 3′-phosphate

Glossary:

kanamycin

Other name(s):

neomycin-kanamycin 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. [PMID: 13416259]

[EC 2.7.1.95 created 1976]

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]

2.7.1.97

Deleted entry:

opsin kinase. Identical with EC 2.7.11.14, rhodopsin kinase

[EC 2.7.1.97 created 1978, deleted 1992]

2.7.1.98

Deleted entry:

phosphoenolpyruvate—fructose phosphotransferase

[EC 2.7.1.98 created 1978, deleted 1984]

2.7.1.99

Transferred entry:

[pyruvate dehydrogenase (lipoamide)] kinase. Now EC 2.7.11.2, [pyruvate dehydrogenase (acetyl-transferring)] kinase

[EC 2.7.1.99 created 1978, deleted 2005]

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 of the methionine-salvage pathway, 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-methyl-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. [PMID: 16662931]

[EC 2.7.1.100 created 1980]