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2.5.1.7

Accepted name:

UDP-N-acetylglucosamine 1-carboxyvinyltransferase

Reaction:

phosphoenolpyruvate + UDP-N-acetyl-α-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-α-D-glucosamine

For diagram of peptidoglycan biosynthesis (part 1), click here

Other name(s):

MurA transferase; UDP-N-acetylglucosamine 1-carboxyvinyl-transferase; UDP-N-acetylglucosamine enoylpyruvyltransferase; enoylpyruvate transferase; phosphoenolpyruvate-UDP-acetylglucosamine-3-enolpyruvyltransferase; phosphoenolpyruvate:UDP-2-acetamido-2-deoxy-D-glucose 2-enoyl-1-carboxyethyltransferase; phosphoenolpyruvate:uridine diphosphate N-acetylglucosamine enolpyruvyltransferase; phosphoenolpyruvate:uridine-5′-diphospho-N-acetyl-2-amino-2-deoxyglucose 3-enolpyruvyltransferase; phosphopyruvate-uridine diphosphoacetylglucosamine pyruvatetransferase; pyruvate-UDP-acetylglucosamine transferase; pyruvate-uridine diphospho-N-acetylglucosamine transferase; pyruvate-uridine diphospho-N-acetyl-glucosamine transferase; pyruvic-uridine diphospho-N-acetylglucosaminyltransferase; phosphoenolpyruvate:UDP-N-acetyl-D-glucosamine 1-carboxyvinyltransferase

Systematic name:

phosphoenolpyruvate:UDP-N-acetyl-α-D-glucosamine 1-carboxyvinyltransferase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9023-27-2

References:

1.	Gunetileke, K.G. and Anwar, R.A. Biosynthesis of uridine diphospho-N-acetylmuramic acid. II. Purification and properties of pyruvate-uridine diphospho-N-acetylglucosamine transferase and characterization of uridine diphospho-N-acetylenopyruvylglucosamine. J. Biol. Chem. 243 (1968) 5770–5778. [PMID: 5699062]
2.	Zemell, R.I. and Anwar, R.A. Pyruvate-uridine diphospho-N-acetylglucosamine transferase. Purification to homogeneity and feedback inhibition. J. Biol. Chem. 250 (1975) 3185–3192. [PMID: 1123336]
3.	van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503–519. [PMID: 11699883]

[EC 2.5.1.7 created 1972, modified 1983, modified 2002]

2.5.1.19

Accepted name:

3-phosphoshikimate 1-carboxyvinyltransferase

Reaction:

phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate

For diagram of shikimate and chorismate biosynthesis, click here and for mechanism of reaction, click here

Other name(s):

5-enolpyruvylshikimate-3-phosphate synthase; 3-enolpyruvylshikimate 5-phosphate synthase; 3-enolpyruvylshikimic acid-5-phosphate synthetase; 5′-enolpyruvylshikimate-3-phosphate synthase; 5-enolpyruvyl-3-phosphoshikimate synthase; 5-enolpyruvylshikimate-3-phosphate synthetase; 5-enolpyruvylshikimate-3-phosphoric acid synthase; enolpyruvylshikimate phosphate synthase; EPSP synthase

Systematic name:

phosphoenolpyruvate:3-phosphoshikimate 5-O-(1-carboxyvinyl)-transferase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9068-73-9

References:

1.	Morell, H., Clark, M.J., Knowles, P.F. and Sprinson, D.B. The enzymic synthesis of chorismic and prephenic acids from 3-enolpyruvylshikimic acid 5-phosphate. J. Biol. Chem. 242 (1967) 82–90. [PMID: 4289188]

[EC 2.5.1.19 created 1976, modified 1983, modified 1989]

2.5.1.54

Accepted name:

3-deoxy-7-phosphoheptulonate synthase

Reaction:

phosphoenolpyruvate + D-erythrose 4-phosphate + H₂O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate

For diagram of shikimate and chorismate biosynthesis, click here and for mechanism of reaction, click here

Other name(s):

2-dehydro-3-deoxy-phosphoheptonate aldolase; 2-keto-3-deoxy-D-arabino-heptonic acid 7-phosphate synthetase; 3-deoxy-D-arabino-2-heptulosonic acid 7-phosphate synthetase; 3-deoxy-D-arabino-heptolosonate-7-phosphate synthetase; 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase; 7-phospho-2-keto-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating); 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating); D-erythrose-4-phosphate-lyase; D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating); DAH7-P synthase; DAHP synthase; DS-Co; DS-Mn; KDPH synthase; KDPH synthetase; deoxy-D-arabino-heptulosonate-7-phosphate synthetase; phospho-2-dehydro-3-deoxyheptonate aldolase; phospho-2-keto-3-deoxyheptanoate aldolase; phospho-2-keto-3-deoxyheptonate aldolase; phospho-2-keto-3-deoxyheptonic aldolase; phospho-2-oxo-3-deoxyheptonate aldolase

Systematic name:

phosphoenolpyruvate:D-erythrose-4-phosphate C-(1-carboxyvinyl)transferase (phosphate-hydrolysing, 2-carboxy-2-oxoethyl-forming)

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9026-94-2

References:

1.	Srinivasan, P.R. and Sprinson, D.B. 2-Keto-3-deoxy-D-arabo-heptonic acid 7-phosphate synthetase. J. Biol. Chem. 234 (1959) 716–722. [PMID: 13654249]
2.	Jossek, R., Bongaerts, J. and Sprenger, G.A. Characterization of a new feedback-resistant 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase AroF of Escherichia coli. FEMS Microbiol. Lett. 202 (2001) 145–148. [DOI] [PMID: 11506923]
3.	Schneider, T.R., Hartmann, M. and Braus, G.H. Crystallization and preliminary X-ray analysis of D-arabino-heptulosonate-7-phosphate synthase (tyrosine inhibitable) from Saccharomyces cerevisiae. Acta Crystallogr. D Biol. Crystallogr. 55 (1999) 1586–1588. [PMID: 10489454]

[EC 2.5.1.54 created 1965 as EC 4.1.2.15, modified 1976, transferred 2002 to EC 2.5.1.54]

2.5.1.55

Accepted name:

3-deoxy-8-phosphooctulonate synthase

Reaction:

phosphoenolpyruvate + D-arabinose 5-phosphate + H₂O = 3-deoxy-D-manno-octulosonate 8-phosphate + phosphate

Other name(s):

2-dehydro-3-deoxy-D-octonate-8-phosphate D-arabinose-5-phosphate-lyase (pyruvate-phosphorylating); 2-dehydro-3-deoxy-phosphooctonate aldolase; 2-keto-3-deoxy-8-phosphooctonic synthetase; 3-deoxy-D-manno-octulosonate-8-phosphate synthase; 3-deoxy-D-mannooctulosonate-8-phosphate synthetase; 3-deoxyoctulosonic 8-phosphate synthetase; KDOP synthase; phospho-2-keto-3-deoxyoctonate aldolase

Systematic name:

phosphoenolpyruvate:D-arabinose-5-phosphate C-(1-carboxyvinyl)transferase (phosphate-hydrolysing, 2-carboxy-2-oxoethyl-forming)

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9026-96-4

References:

1.	Levin, D.H. and Racker, E. Condensation of arabinose 5-phosphate and phosphorylenol pyruvate by 2-keto-3-deoxy-8-phosphooctonic acid synthetase. J. Biol. Chem. 234 (1959) 2532–25339. [PMID: 14416200]
2.	Krosky, D.J., Alm, R., Berg, M., Carmel, G., Tummino, P.J., Xu, B. and Yang, W. Helicobacter pylori 3-deoxy-D-manno-octulosonate-8-phosphate (KDO-8-P) synthase is a zinc-metalloenzyme. Biochim. Biophys. Acta 1594 (2002) 297–306. [DOI] [PMID: 11904225]
3.	Asojo, O., Friedman, J., Adir, N., Belakhov, V., Shoham, Y. and Baasov, T. Crystal structures of KDOP synthase in its binary complexes with the substrate phosphoenolpyruvate and with a mechanism-based inhibitor. Biochemistry 40 (2001) 6326–6334. [DOI] [PMID: 11371194]

[EC 2.5.1.55 created 1965 as EC 4.1.2.16, transferred 2002 to EC 2.5.1.55]

2.5.1.56

Accepted name:

N-acetylneuraminate synthase

Reaction:

phosphoenolpyruvate + N-acetyl-D-mannosamine + H₂O = phosphate + N-acetylneuraminate

For diagram of reaction, click here

Other name(s):

(NANA)condensing enzyme; N-acetylneuraminate pyruvate-lyase (pyruvate-phosphorylating); NeuAc synthase

Systematic name:

phosphoenolpyruvate:N-acetyl-D-mannosamine C-(1-carboxyvinyl)transferase (phosphate-hydrolysing, 2-carboxy-2-oxoethyl-forming)

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37290-66-7

References:

1.	Blacklow, R.S. and Warren, L. Biosynthesis of sialic acids by Neisseria meningitidis. J. Biol. Chem. 237 (1962) 3520–3526. [PMID: 13971393]
2.	Komaki, E., Ohta, Y. and Tsukada, Y. Purification and characterization of N-acetylneuraminate synthase from Escherichia coli K1-M12. Biosci. Biotechnol. Biochem. 61 (1997) 2046–2050. [DOI] [PMID: 9438985]

[EC 2.5.1.56 created 1972 as EC 4.1.3.19, transferred 2002 to EC 2.5.1.56]

2.5.1.57

Accepted name:

N-acylneuraminate-9-phosphate synthase

Reaction:

phosphoenolpyruvate + N-acyl-D-mannosamine 6-phosphate + H₂O = N-acylneuraminate 9-phosphate + phosphate

For diagram of reaction, click here

Other name(s):

N-acetylneuraminate 9-phosphate lyase; N-acetylneuraminate 9-phosphate sialic acid 9-phosphate synthase; N-acetylneuraminate 9-phosphate synthetase; N-acylneuraminate-9-phosphate pyruvate-lyase (pyruvate-phosphorylating); sialic acid 9-phosphate synthetase

Systematic name:

phosphoenolpyruvate:N-acyl-D-mannosamine-6-phosphate 1-(2-carboxy-2-oxoethyl)transferase

Comments:

Acts on N-glycoloyl and N-acetyl-derivatives.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-58-7

References:

1.	Roseman, S., Jourdian, G.W., Watson, D. and Rood, R. Enzymatic synthesis of sialic acid 9-phosphates. Proc. Natl. Acad. Sci. USA 47 (1961) 958–961. [PMID: 13743311]
2.	Watson, D.R., Jourdian, G.W. and Roseman, S. The sialic acids. 8. Sialic acid 9-phosphate synthetase. J. Biol. Chem. 241 (1966) 5627–5636. [PMID: 5928202]
3.	Nakata, D., Close, B.E., Colley, K.J., Matsuda, T. and Kitajima, K. Molecular cloning and expression of the mouse N-acetylneuraminic acid 9-phosphate synthase which does not have deaminoneuraminic acid (KDN) 9-phosphate synthase activity. Biochem. Biophys. Res. Commun. 273 (2000) 642–648. [DOI] [PMID: 10873658]

[EC 2.5.1.57 created 1972 as EC 4.1.3.20, transferred 2002 to EC 2.5.1.57]

2.5.1.95

Accepted name:

xanthan ketal pyruvate transferase

Reaction:

phosphoenolpyruvate + D-Man-β-(1→4)-D-GlcA-β-(1→2)-D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphospho-ditrans,octacis-undecaprenol = 4,6-CH₃(COO^-)C-D-Man-β-(1→4)-D-GlcA-β-(1→2)-D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphospho-ditrans,octacis-undecaprenol + phosphate

For diagram of xanthan biosynthesis, click here

Other name(s):

KPT

Systematic name:

phosphoenolpyruvate:D-Man-β-(1→4)-GlcA-β-(1→2)-D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphospho-ditrans,octacis-undecaprenol 4,6-O-(1-carboxyethan-1,1-diyl)transferase

Comments:

Involved in the biosynthesis of the polysaccharide xanthan. 30-40% of the terminal mannose residues of xanthan have a 4,6-O-(1-carboxyethan-1,1-diyl) ketal group. It also acts on the 6-O-acetyl derivative of the inner mannose unit.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Marzocca, M.P., Harding, N.E., Petroni, E.A., Cleary, J.M. and Ielpi, L. Location and cloning of the ketal pyruvate transferase gene of Xanthomonas campestris. J. Bacteriol. 173 (1991) 7519–7524. [DOI] [PMID: 1657892]

[EC 2.5.1.95 created 2011, modified 2012]

2.5.1.97

Accepted name:

pseudaminic acid synthase

Reaction:

phosphoenolpyruvate + 2,4-bis(acetylamino)-2,4,6-trideoxy-β-L-altropyranose + H₂O = 5,7-bis(acetylamino)-3,5,7,9-tetradeoxy-L-glycero-α-L-manno-2-nonulopyranosonic acid + phosphate

Glossary:

pseudaminic acid = 5,7-bis(acetylamino)-3,5,7,9-tetradeoxy-L-glycero-α-L-manno-2-nonulopyranosonic acid

Other name(s):

PseI; NeuB3

Systematic name:

phosphoenolpyruvate:2,4-bis(acetylamino)-2,4,6-trideoxy-β-L-altropyranose transferase (phosphate-hydrolysing, 2,7-acetylamino-transfering, 2-carboxy-2-oxoethyl-forming)

Comments:

The enzyme requires a divalent metal ion, the highest activity values are observed in the presence of Mn²⁺ and Co²⁺ (10 mM).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Chou, W.K., Dick, S., Wakarchuk, W.W. and Tanner, M.E. Identification and characterization of NeuB3 from Campylobacter jejuni as a pseudaminic acid synthase. J. Biol. Chem. 280 (2005) 35922–35928. [DOI] [PMID: 16120604]

[EC 2.5.1.97 created 2011]

2.5.1.98

Accepted name:

Rhizobium leguminosarum exopolysaccharide glucosyl ketal-pyruvate-transferase

Reaction:

phosphoenolpyruvate + [β-D-GlcA-(1→4)-2-O-Ac-β-D-GlcA-(1→4)-β-D-Glc-(1→4)-[3-O-(CH₃CH(OH)CH₂C(O))-4,6-CH₃(COO^-)C-β-D-Gal-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→6)]-2(or 3)-O-Ac-α-D-Glc-(1→6)]_n = [β-D-GlcA-(1→4)-2-O-Ac-β-D-GlcA-(1→4)-β-D-Glc-(1→4)-[3-O-(CH₃CH(OH)CH₂C(O))-4,6-CH₃(COO^-)C-β-D-Gal-(1→3)-4,6-CH₃(COO^-)C-β-D-Glc-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→6)]-2(or 3)-O-Ac-α-D-Glc-(1→6)]_n + phosphate

Other name(s):

PssM; phosphoenolpyruvate:[D-GlcA-β-(1→4)-2-O-Ac-D-GlcA-β-(1→4)-D-Glc-β-(1→4)-[3-O-CH₃-CH₂CH(OH)C(O)-D-Gal-β-(1→4)-D-Glc-β-(1→4)-D-Glc-β-(1→4)-D-Glc-β-(1→6)]-2(or 3)-O-Ac-D-Glc-α-(1→6)]_n 4,6-O-(1-carboxyethan-1,1-diyl)transferase

Systematic name:

phosphoenolpyruvate:[β-D-GlcA-(1→4)-2-O-Ac-β-D-GlcA-(1→4)-β-D-Glc-(1→4)-[3-O-CH₃-CH₂CH(OH)C(O)-4,6-CH₃(COO^-)C-β-D-Gal-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→6)]-2(or 3)-O-Ac-α-D-Glc-(1→6)]_n 4,6-O-(1-carboxyethan-1,1-diyl)transferase

Comments:

The enzyme is responsible for pyruvylation of the subterminal glucose in the acidic octasaccharide repeating unit of the exopolysaccharide of Rhizobium leguminosarum (bv. viciae strain VF39) which is necessary to establish nitrogen-fixing symbiosis with Pisum sativum, Vicia faba, and Vicia sativa.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

Ivashina, T.V., Fedorova, E.E., Ashina, N.P., Kalinchuk, N.A., Druzhinina, T.N., Shashkov, A.S., Shibaev, V.N. and Ksenzenko, V.N. Mutation in the pssM gene encoding ketal pyruvate transferase leads to disruption of Rhizobium leguminosarum bv. viciae—Pisum sativum symbiosis. J. Appl. Microbiol. 109 (2010) 731–742. [DOI] [PMID: 20233262]

[EC 2.5.1.98 created 2012, modified 2018]

2.5.1.101

Accepted name:

N,N′-diacetyllegionaminate synthase

Reaction:

2,4-diacetamido-2,4,6-trideoxy-α-D-mannopyranose + phosphoenolpyruvate + H₂O = N,N′-diacetyllegionaminate + phosphate

For diagram of legionaminic acid biosynthesis, click here

Glossary:

legionaminate = 5,7-diamino-3,5,7,9-tetradeoxy-D-glycero-D-galacto-non-2-ulosonate

Other name(s):

neuB (gene name); legI (gene name)

Systematic name:

phosphoenolpyruvate:2,4-diacetamido-2,4,6-trideoxy-α-D-mannopyranose 1-(2-carboxy-2-oxoethyl)transferase

Comments:

Requires a divalent metal such as Mn²⁺. Isolated from the bacteria Legionella pneumophila and Campylobacter jejuni, where it is involved in the biosynthesis of legionaminic acid, a virulence-associated, cell surface sialic acid-like derivative.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Glaze, P.A., Watson, D.C., Young, N.M. and Tanner, M.E. Biosynthesis of CMP-N,N′-diacetyllegionaminic acid from UDP-N,N′-diacetylbacillosamine in Legionella pneumophila. Biochemistry 47 (2008) 3272–3282. [DOI] [PMID: 18275154]
2.	Schoenhofen, I.C., Vinogradov, E., Whitfield, D.M., Brisson, J.R. and Logan, S.M. The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors. Glycobiology 19 (2009) 715–725. [DOI] [PMID: 19282391]

[EC 2.5.1.101 created 2012]

2.5.1.132

Accepted name:

3-deoxy-D-glycero-D-galacto-nonulopyranosonate 9-phosphate synthase

Reaction:

phosphoenolpyruvate + D-mannose 6-phosphate + H₂O = 3-deoxy-D-glycero-D-galacto-non-2-ulopyranosonate 9-phosphate + phosphate

Glossary:

phosphoenolpyruvate = 2-(phosphooxy)-2-propenoate
3-deoxy-D-glycero-D-galacto-non-2-ulopyranosonate = Kdn

Other name(s):

3-deoxy-D-glycero-D-galacto-nononate 9-phosphate synthase; 2-keto-3-deoxy-D-glycero-D-galacto-9-phosphonononic acid synthase; Kdn 9-P synthase

Systematic name:

phosphoenolpyruvate:D-mannose-6-phosphate 1-(2-carboxy-2-oxoethyl)transferase

Comments:

The enzyme participates in the biosynthesis of the sialic acid 3-deoxy-D-glycero-D-galacto-non-2-ulopyranosonate (Kdn). The human sialic acid synthase (EC 2.5.1.57) is also able to catalyse the reaction. Kdn is abundant in extracellular glycoconjugates of lower vertebrates such as fish and amphibians, but is also found in the capsular polysaccharides of bacteria that belong to the Bacteroides genus.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Angata, T., Nakata, D., Matsuda, T., Kitajima, K. and Troy, F.A., 2nd. Biosynthesis of KDN (2-keto-3-deoxy-D-glycero-D-galacto-nononic acid). Identification and characterization of a KDN-9-phosphate synthetase activity from trout testis. J. Biol. Chem. 274 (1999) 22949–22956. [DOI] [PMID: 10438460]
2.	Lawrence, S.M., Huddleston, K.A., Pitts, L.R., Nguyen, N., Lee, Y.C., Vann, W.F., Coleman, T.A. and Betenbaugh, M.J. Cloning and expression of the human N-acetylneuraminic acid phosphate synthase gene with 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid biosynthetic ability. J. Biol. Chem. 275 (2000) 17869–17877. [DOI] [PMID: 10749855]
3.	Wang, L., Lu, Z., Allen, K.N., Mariano, P.S. and Dunaway-Mariano, D. Human symbiont Bacteroides thetaiotaomicron synthesizes 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). Chem. Biol. 15 (2008) 893–897. [DOI] [PMID: 18804026]

[EC 2.5.1.132 created 2016]

2.7.1.40

Accepted name:

pyruvate kinase

Reaction:

ATP + pyruvate = ADP + phosphoenolpyruvate

For diagram of the Entner-Doudoroff pathway, click here

Other name(s):

phosphoenolpyruvate kinase; phosphoenol transphosphorylase

Systematic name:

ATP:pyruvate 2-O-phosphotransferase

Comments:

UTP, GTP, CTP, ITP and dATP can also act as donors. Also phosphorylates hydroxylamine and fluoride in the presence of CO₂.

Links to other databases:

BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-59-6

References:

1.	Boyer, P.D. Pyruvate kinase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 6, Academic Press, New York, 1962, pp. 95–113.
2.	Kornberg, A. and Pricer, W.E. Enzymatic phosphorylation of adenosine and 2,6-diaminopurine riboside. J. Biol. Chem. 193 (1951) 481–495. [PMID: 14907737]
3.	Kubowitz, F. and Ott, P. Isolierung von Gärungsfermenten aus menschlichen Muskeln. Biochem. Z. 317 (1944) 193–203.
4.	Strominger, J.L. Enzymatic synthesis of guanosine and cytidine triphosphates: a note on the nucleotide specificity of the pyruvate phosphokinase reaction. Biochim. Biophys. Acta 16 (1955) 616–618. [DOI] [PMID: 14389299]
5.	Tietz, A. and Ochoa, S. "Fluorokinase" and pyruvic kinase. Arch. Biochem. Biophys. 78 (1958) 477–493. [DOI] [PMID: 13618030]

[EC 2.7.1.40 created 1961]

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]

2.7.1.121

Accepted name:

phosphoenolpyruvate—glycerone phosphotransferase

Reaction:

phosphoenolpyruvate + glycerone = pyruvate + glycerone phosphate

Glossary:

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

Systematic name:

phosphoenolpyruvate:glycerone phosphotransferase

Links to other databases:

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

References:

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

[EC 2.7.1.121 created 1989]

2.7.1.147

Accepted name:

ADP-specific glucose/glucosamine kinase

Reaction:

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

Other name(s):

ADP-specific glucokinase; ADP-dependent glucokinase

Systematic name:

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

Comments:

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

Links to other databases:

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

References:

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

[EC 2.7.1.147 created 2001, modified 2020]

2.7.1.191

Accepted name:

protein-N^π-phosphohistidine—D-mannose phosphotransferase

Reaction:

[protein]-N^π-phospho-L-histidine + D-mannose_{[side 1]} = [protein]-L-histidine + D-mannose 6-phosphate_{[side 2]}

Other name(s):

manXYZ (gene names); mannose PTS permease; EII^Man; Enzyme II^Man

Systematic name:

protein-N^π-phospho-L-histidine:D-mannose N^π-phosphotransferase

Comments:

This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Erni, B. and Zanolari, B. The mannose-permease of the bacterial phosphotransferase system. Gene cloning and purification of the enzyme IIMan/IIIMan complex of Escherichia coli. J. Biol. Chem. 260 (1985) 15495–15503. [PMID: 2999119]
2.	Williams, N., Fox, D.K., Shea, C. and Roseman, S. Pel, the protein that permits lambda DNA penetration of Escherichia coli, is encoded by a gene in ptsM and is required for mannose utilization by the phosphotransferase system. Proc. Natl. Acad. Sci. USA 83 (1986) 8934–8938. [DOI] [PMID: 2947241]
3.	Erni, B., Zanolari, B. and Kocher, H.P. The mannose permease of Escherichia coli consists of three different proteins. Amino acid sequence and function in sugar transport, sugar phosphorylation, and penetration of phage lambda DNA. J. Biol. Chem. 262 (1987) 5238–5247. [PMID: 2951378]
4.	Stolz, B., Huber, M., Markovic-Housley, Z. and Erni, B. The mannose transporter of Escherichia coli. Structure and function of the IIABMan subunit. J. Biol. Chem. 268 (1993) 27094–27099. [PMID: 8262947]
5.	Rhiel, E., Flukiger, K., Wehrli, C. and Erni, B. The mannose transporter of Escherichia coli K12: oligomeric structure, and function of two conserved cysteines. Biol. Chem. Hoppe Seyler 375 (1994) 551–559. [PMID: 7811395]
6.	Huber, F. and Erni, B. Membrane topology of the mannose transporter of Escherichia coli K12. Eur. J. Biochem. 239 (1996) 810–817. [DOI] [PMID: 8774730]

[EC 2.7.1.191 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.191]

2.7.1.192

Accepted name:

protein-N^π-phosphohistidine—N-acetylmuramate phosphotransferase

Reaction:

[protein]-N^π-phospho-L-histidine + N-acetyl-D-muramate_{[side 1]} = [protein]-L-histidine + N-acetyl-D-muramate 6-phosphate_{[side 2]}

Other name(s):

murP (gene name); N-acetylmuramic acid PTS permease; EII^NAcMur; Enzyme II^NAcMur

Systematic name:

protein-N^π-phospho-L-histidine:N-acetyl-D-muramate N^π-phosphotransferase

Comments:

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Dahl, U., Jaeger, T., Nguyen, B.T., Sattler, J.M. and Mayer, C. Identification of a phosphotransferase system of Escherichia coli required for growth on N-acetylmuramic acid. J. Bacteriol. 186 (2004) 2385–2392. [DOI] [PMID: 15060041]

[EC 2.7.1.192 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.192]

2.7.1.193

Accepted name:

protein-N^π-phosphohistidine—N-acetyl-D-glucosamine phosphotransferase

Reaction:

[protein]-N^π-phospho-L-histidine + N-acetyl-D-glucosamine_{[side 1]} = [protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate_{[side 2]}

Other name(s):

nagE (gene name); N-acetyl-D-glucosamine PTS permease; EII^Nag; Enzyme II^Nag; EIICBA^Nag

Systematic name:

protein-N^π-phospho-L-histidine:N-acetyl-D-glucosamine N^π-phosphotransferase

Comments:

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	White, R.J. The role of the phosphoenolpyruvate phosphotransferase system in the transport of N-acetyl-D-glucosamine by Escherichia coli. Biochem. J. 118 (1970) 89–92. [PMID: 4919472]
2.	Rogers, M.J., Ohgi, T., Plumbridge, J. and Soll, D. Nucleotide sequences of the Escherichia coli nagE and nagB genes: the structural genes for the N-acetylglucosamine transport protein of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and for glucosamine-6-phosphate deaminase. Gene 62 (1988) 197–207. [DOI] [PMID: 3284790]
3.	Peri, K.G. and Waygood, E.B. Sequence of cloned enzyme IIN-acetylglucosamine of the phosphoenolpyruvate:N-acetylglucosamine phosphotransferase system of Escherichia coli. Biochemistry 27 (1988) 6054–6061. [PMID: 3056518]
4.	Plumbridge, J. An alternative route for recycling of N-acetylglucosamine from peptidoglycan involves the N-acetylglucosamine phosphotransferase system in Escherichia coli. J. Bacteriol. 191 (2009) 5641–5647. [DOI] [PMID: 19617367]

[EC 2.7.1.193 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.193]

2.7.1.194

Accepted name:

protein-N^π-phosphohistidine—L-ascorbate phosphotransferase

Reaction:

[protein]-N^π-phospho-L-histidine + L-ascorbate_{[side 1]} = [protein]-L-histidine + L-ascorbate 6-phosphate_{[side 2]}

Other name(s):

ulaABC (gene names); L-ascorbate PTS permease; EII^Sga; Enzyme II^Sga; Enzyme II^Ula

Systematic name:

protein-N^π-phospho-L-histidine:L-ascorbate N^π-phosphotransferase

Comments:

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Zhang, Z., Aboulwafa, M., Smith, M.H. and Saier, M.H., Jr. The ascorbate transporter of Escherichia coli. J. Bacteriol. 185 (2003) 2243–2250. [DOI] [PMID: 12644495]
2.	Hvorup, R., Chang, A.B. and Saier, M.H., Jr. Bioinformatic analyses of the bacterial L-ascorbate phosphotransferase system permease family. J. Mol. Microbiol. Biotechnol. 6 (2003) 191–205. [DOI] [PMID: 15153772]
3.	Luo, P., Yu, X., Wang, W., Fan, S., Li, X. and Wang, J. Crystal structure of a phosphorylation-coupled vitamin C transporter. Nat. Struct. Mol. Biol. 22 (2015) 238–241. [DOI] [PMID: 25686089]

[EC 2.7.1.194 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.194]

2.7.1.195

Accepted name:

protein-N^π-phosphohistidine—2-O-α-mannosyl-D-glycerate phosphotransferase

Reaction:

[protein]-N^π-phospho-L-histidine + 2-O-(α-D-mannopyranosyl)-D-glycerate _{[side 1]} = [protein]-L-histidine + 2-O-(6-phospho-α-D-mannopyranosyl)-D-glycerate _{[side 2]}

Other name(s):

mngA (gene names); 2-O-α-mannosyl-D-glycerate PTS permease; EII^MngA; Enzyme II^MngA; Enzyme II^HrsA; EII^{mannosylglycerate}; Frx

Systematic name:

protein-N^π-phospho-L-histidine:2-O-α-mannopyranosyl-D-glycerate N^π-phosphotransferase

Comments:

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

Sampaio, M.M., Chevance, F., Dippel, R., Eppler, T., Schlegel, A., Boos, W., Lu, Y.J. and Rock, C.O. Phosphotransferase-mediated transport of the osmolyte 2-O-α-mannosyl-D-glycerate in Escherichia coli occurs by the product of the mngA (hrsA) gene and is regulated by the mngR (farR) gene product acting as repressor. J. Biol. Chem. 279 (2004) 5537–5548. [DOI] [PMID: 14645248]

[EC 2.7.1.195 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.195]

2.7.1.196

Accepted name:

protein-N^π-phosphohistidine—N,N′-diacetylchitobiose phosphotransferase

Reaction:

[protein]-N^π-phospho-L-histidine + N,N′-diacetylchitobiose_{[side 1]} = [protein]-L-histidine + N,N′-diacetylchitobiose 6′-phosphate_{[side 2]}

Other name(s):

chbABC (gene names); N,N′-diacetylchitobiose PTS permease; chitobiose PTS permease; EII^cel; EII^chb; Enzyme II^cel; Enzyme II^chb

Systematic name:

protein-N^π-phospho-L-histidine:N,N′-diacetylchitobiose N^π-phosphotransferase

Comments:

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Keyhani, N.O., Wang, L.X., Lee, Y.C. and Roseman, S. The chitin disaccharide, N,N′-diacetylchitobiose, is catabolized by Escherichia coli and is transported/phosphorylated by the phosphoenolpyruvate:glycose phosphotransferase system. J. Biol. Chem. 275 (2000) 33084–33090. [DOI] [PMID: 10913117]
2.	Reizer, J., Reizer, A. and Saier, M.H., Jr. The cellobiose permease of Escherichia coli consists of three proteins and is homologous to the lactose permease of Staphylococcus aureus. Res. Microbiol. 141 (1990) 1061–1067. [DOI] [PMID: 2092358]
3.	Keyhani, N.O., Boudker, O. and Roseman, S. Isolation and characterization of IIAChb, a soluble protein of the enzyme II complex required for the transport/phosphorylation of N, N′-diacetylchitobiose in Escherichia coli. J. Biol. Chem. 275 (2000) 33091–33101. [DOI] [PMID: 10913118]
4.	Keyhani, N.O., Bacia, K. and Roseman, S. The transport/phosphorylation of N,N′-diacetylchitobiose in Escherichia coli. Characterization of phospho-IIB(Chb) and of a potential transition state analogue in the phosphotransfer reaction between the proteins IIA(Chb) AND IIB(Chb). J. Biol. Chem. 275 (2000) 33102–33109. [DOI] [PMID: 10913119]

[EC 2.7.1.196 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.196]

2.7.1.197

Accepted name:

protein-N^π-phosphohistidine—D-mannitol phosphotransferase

Reaction:

[protein]-N^π-phospho-L-histidine + D-mannitol_{[side 1]} = [protein]-L-histidine + D-mannitol 1-phosphate_{[side 2]}

Other name(s):

mtlA (gene name); D-mannitol PTS permease; EII^Mtl

Systematic name:

protein-N^π-phospho-L-histidine:D-mannitol N^π-phosphotransferase

Comments:

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Jacobson, G.R., Lee, C.A. and Saier, M.H., Jr. Purification of the mannitol-specific enzyme II of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system. J. Biol. Chem. 254 (1979) 249–252. [PMID: 368051]
2.	Jacobson, G.R., Tanney, L.E., Kelly, D.M., Palman, K.B. and Corn, S.B. Substrate and phospholipid specificity of the purified mannitol permease of Escherichia coli. J. Cell. Biochem. 23 (1983) 231–240. [DOI] [PMID: 6427236]
3.	Lee, C.A. and Saier, M.H., Jr. Mannitol-specific enzyme II of the bacterial phosphotransferase system. III. The nucleotide sequence of the permease gene. J. Biol. Chem. 258 (1983) 10761–10767. [PMID: 6309813]
4.	Elferink, M.G., Driessen, A.J. and Robillard, G.T. Functional reconstitution of the purified phosphoenolpyruvate-dependent mannitol-specific transport system of Escherichia coli in phospholipid vesicles: coupling between transport and phosphorylation. J. Bacteriol. 172 (1990) 7119–7125. [DOI] [PMID: 2123863]
5.	van Weeghel, R.P., Meyer, G., Pas, H.H., Keck, W. and Robillard, G.T. Cytoplasmic phosphorylating domain of the mannitol-specific transport protein of the phosphoenolpyruvate-dependent phosphotransferase system in Escherichia coli: overexpression, purification, and functional complementation with the mannitol binding domain. Biochemistry 30 (1991) 9478–9485. [PMID: 1909895]
6.	Boer, H., ten Hoeve-Duurkens, R.H. and Robillard, G.T. Relation between the oligomerization state and the transport and phosphorylation function of the Escherichia coli mannitol transport protein: interaction between mannitol-specific enzyme II monomers studied by complementation of inactive site-directed mutants. Biochemistry 35 (1996) 12901–12908. [DOI] [PMID: 8841134]

[EC 2.7.1.197 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.197]

2.7.1.198

Accepted name:

protein-N^π-phosphohistidine—D-sorbitol phosphotransferase

Reaction:

[protein]-N^π-phospho-L-histidine + D-sorbitol_{[side 1]} = [protein]-L-histidine + D-sorbitol 6-phosphate_{[side 2]}

Other name(s):

srlABE (gene names); D-sorbitol PTS permease; sorbitol PTS permease; glucitol PTS permease; EII^Gut; Enzyme II^Gut

Systematic name:

protein-N^π-phospho-L-histidine:D-sorbitol N^π-phosphotransferase

Comments:

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Lengeler, J. Nature and properties of hexitol transport systems in Escherichia coli. J. Bacteriol. 124 (1975) 39–47. [PMID: 1100608]
2.	Reizer, J., Mitchell, W.J., Minton, N., Brehm, J., Reizer, A. and Saier, M.H., Jr. Proposed topology of the glucitol permeases of Escherichia coli and Clostridium acetobutylicum. Curr. Microbiol. 33 (1996) 331–333. [PMID: 8875915]

[EC 2.7.1.198 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.198]

2.7.1.199

Accepted name:

protein-N^π-phosphohistidine—D-glucose phosphotransferase

Reaction:

[protein]-N^π-phospho-L-histidine + D-glucose_{[side 1]} = [protein]-L-histidine + D-glucose 6-phosphate_{[side 2]}

Other name(s):

ptsG (gene name); D-glucose PTS permease; EII^Glc; Enzyme II^Glc

Systematic name:

protein-N^π-phospho-L-histidine:D-glucose N^π-phosphotransferase

Comments:

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Stock, J.B., Waygood, E.B., Meadow, N.D., Postma, P.W. and Roseman, S. Sugar transport by the bacterial phosphotransferase system. The glucose receptors of the Salmonella typhimurium phosphotransferase system. J. Biol. Chem. 257 (1982) 14543–14552. [PMID: 6292227]
2.	Erni, B. and Zanolari, B. Glucose-permease of the bacterial phosphotransferase system. Gene cloning, overproduction, and amino acid sequence of enzyme IIGlc. J. Biol. Chem. 261 (1986) 16398–16403. [PMID: 3023349]

[EC 2.7.1.199 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.199]

2.7.1.200

Accepted name:

protein-N^π-phosphohistidine—galactitol phosphotransferase

Reaction:

[protein]-N^π-phospho-L-histidine + galactitol_{[side 1]} = [protein]-L-histidine + galactitol 1-phosphate_{[side 2]}

Other name(s):

gatABC (gene names); galactitol PTS permease; EII^Gat; Enzyme II^Gat

Systematic name:

protein-N^π-phospho-L-histidine:galactitol N^π-phosphotransferase

Comments:

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Lengeler, J. Nature and properties of hexitol transport systems in Escherichia coli. J. Bacteriol. 124 (1975) 39–47. [PMID: 1100608]
2.	Nobelmann, B. and Lengeler, J.W. Sequence of the gat operon for galactitol utilization from a wild-type strain EC3132 of Escherichia coli. Biochim. Biophys. Acta 1262 (1995) 69–72. [DOI] [PMID: 7772602]
3.	Nobelmann, B. and Lengeler, J.W. Molecular analysis of the gat genes from Escherichia coli and of their roles in galactitol transport and metabolism. J. Bacteriol. 178 (1996) 6790–6795. [DOI] [PMID: 8955298]

[EC 2.7.1.200 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.200]

2.7.1.201

Accepted name:

protein-N^π-phosphohistidine—trehalose phosphotransferase

Reaction:

[protein]-N^π-phospho-L-histidine + α,α-trehalose_{[side 1]} = [protein]-L-histidine + α,α-trehalose 6-phosphate_{[side 2]}

Other name(s):

treB (gene name); trehalose PTS permease; EII^Tre; Enzyme II^Tre

Systematic name:

protein-N^π-phospho-L-histidine:α,α-trehalose N^π-phosphotransferase

Comments:

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Boos, W., Ehmann, U., Forkl, H., Klein, W., Rimmele, M. and Postma, P. Trehalose transport and metabolism in Escherichia coli. J. Bacteriol. 172 (1990) 3450–3461. [DOI] [PMID: 2160944]
2.	Klein, W., Horlacher, R. and Boos, W. Molecular analysis of treB encoding the Escherichia coli enzyme II specific for trehalose. J. Bacteriol. 177 (1995) 4043–4052. [DOI] [PMID: 7608078]

[EC 2.7.1.201 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.201]

2.7.1.202

Accepted name:

protein-N^π-phosphohistidine—D-fructose phosphotransferase

Reaction:

[protein]-N^π-phospho-L-histidine + D-fructose_{[side 1]} = [protein]-L-histidine + D-fructose 1-phosphate_{[side 2]}

Other name(s):

fruAB (gene names); fructose PTS permease; EII^Fru; Enzyme II^Fru

Systematic name:

protein-N^π-phospho-L-histidine:D-fructose N^π-phosphotransferase

Comments:

This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is usually a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). The enzyme from the bacterium Escherichia coli is an exception, since it is phosphorylated directly by EC 2.7.3.9. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Waygood, E.B. Resolution of the phosphoenolpyruvate: fructose phosphotransferase system of Escherichia coli into two components: enzyme IIfructose and fructose-induced HPr-like protein (FPr). Can. J. Biochem. 58 (1980) 1144–1146. [PMID: 7006754]
2.	Kornberg, H. The roles of HPr and FPr in the utilization of fructose by Escherichia coli. FEBS Lett. 194 (1986) 12–15. [DOI] [PMID: 3510127]
3.	Geerse, R.H., Izzo, F. and Postma, P.W. The PEP: fructose phosphotransferase system in Salmonella typhimurium: FPr combines enzyme IIIFru and pseudo-HPr activities. Mol. Gen. Genet. 216 (1989) 517–525. [PMID: 2546043]
4.	Kornberg, H.L. and Lambourne, L.T. Role of the phosphoenolpyruvate-dependent fructose phosphotransferase system in the utilization of mannose by Escherichia coli. Proc Biol Sci 250 (1992) 51–55. [DOI] [PMID: 1361062]

[EC 2.7.1.202 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.202]

2.7.1.203

Accepted name:

protein-N^π-phosphohistidine—D-glucosaminate phosphotransferase

Reaction:

[protein]-N^π-phospho-L-histidine + 2-amino-2-deoxy-D-gluconate_{[side 1]} = [protein]-L-histidine + 2-amino-2-deoxy-D-gluconate 6-phosphate_{[side 2]}

Other name(s):

dgaABCD (gene names); 2-amino-2-deoxy-D-gluconate PTS permease

Systematic name:

protein-N^π-phospho-L-histidine:2-amino-2-deoxy-D-gluconate N^π-phosphotransferase

Comments:

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Miller, K.A., Phillips, R.S., Mrazek, J. and Hoover, T.R. Salmonella utilizes D-glucosaminate via a mannose family phosphotransferase system permease and associated enzymes. J. Bacteriol. 195 (2013) 4057–4066. [DOI] [PMID: 23836865]

[EC 2.7.1.203 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.203]

2.7.1.204

Accepted name:

protein-N^π-phosphohistidine—D-galactose phosphotransferase

Reaction:

[protein]-N^π-phospho-L-histidine + D-galactose_{[side 1]} = [protein]-L-histidine + D-galactose 6-phosphate_{[side 2]}

Other name(s):

D-galactose PTS permease; EII^Gal; Enzyme II^Gal

Systematic name:

protein-N^π-phospho-L-histidine:D-galactose N^π-phosphotransferase

Comments:

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Zeng, L., Martino, N.C. and Burne, R.A. Two gene clusters coordinate galactose and lactose metabolism in Streptococcus gordonii. Appl. Environ. Microbiol. 78 (2012) 5597–5605. [DOI] [PMID: 22660715]
2.	Zeng, L., Xue, P., Stanhope, M.J. and Burne, R.A. A galactose-specific sugar: phosphotransferase permease is prevalent in the non-core genome of Streptococcus mutans. Mol Oral Microbiol 28 (2013) 292–301. [DOI] [PMID: 23421335]

[EC 2.7.1.204 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.204]

2.7.1.205

Accepted name:

protein-N^π-phosphohistidine—cellobiose phosphotransferase

Reaction:

[protein]-N^π-phospho-L-histidine + cellobiose_{[side 1]} = [protein]-L-histidine + 6-phospho-β-D-glucosyl-(1→4)-D-glucose_{[side 2]}

Other name(s):

celB (gene name); cellobiose PTS permease; EII^Cel; Enzyme II^Cel

Systematic name:

protein-N^π-phospho-L-histidine:cellobiose N^π-phosphotransferase

Comments:

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Lai, X. and Ingram, L.O. Cloning and sequencing of a cellobiose phosphotransferase system operon from Bacillus stearothermophilus XL-65-6 and functional expression in Escherichia coli. J. Bacteriol. 175 (1993) 6441–6450. [DOI] [PMID: 8407820]
2.	Lai, X., Davis, F.C., Hespell, R.B. and Ingram, L.O. Cloning of cellobiose phosphoenolpyruvate-dependent phosphotransferase genes: functional expression in recombinant Escherichia coli and identification of a putative binding region for disaccharides. Appl. Environ. Microbiol. 63 (1997) 355–363. [PMID: 9023916]
3.	Stoll, R. and Goebel, W. The major PEP-phosphotransferase systems (PTSs) for glucose, mannose and cellobiose of Listeria monocytogenes, and their significance for extra- and intracellular growth. Microbiology 156 (2010) 1069–1083. [DOI] [PMID: 20056707]
4.	Wu, M.C., Chen, Y.C., Lin, T.L., Hsieh, P.F. and Wang, J.T. Cellobiose-specific phosphotransferase system of Klebsiella pneumoniae and its importance in biofilm formation and virulence. Infect. Immun. 80 (2012) 2464–2472. [DOI] [PMID: 22566508]

[EC 2.7.1.205 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.205]

2.7.1.206

Accepted name:

protein-N^π-phosphohistidine—L-sorbose phosphotransferase

Reaction:

[protein]-N^π-phospho-L-histidine + L-sorbose_{[side 1]} = [protein]-L-histidine + L-sorbose 1-phosphate_{[side 2]}

Other name(s):

sorABFM (gene names); L-sorbose PTS permease; EII^Sor; Enzyme II^Sor

Systematic name:

protein-N^π-phospho-L-histidine:L-sorbose N^π-phosphotransferase

Comments:

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Wehmeier, U.F., Wohrl, B.M. and Lengeler, J.W. Molecular analysis of the phosphoenolpyruvate-dependent L-sorbose: phosphotransferase system from Klebsiella pneumoniae and of its multidomain structure. Mol. Gen. Genet. 246 (1995) 610–618. [PMID: 7700234]
2.	Yebra, M.J., Veyrat, A., Santos, M.A. and Perez-Martinez, G. Genetics of L-sorbose transport and metabolism in Lactobacillus casei. J. Bacteriol. 182 (2000) 155–163. [DOI] [PMID: 10613875]

[EC 2.7.1.206 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.206]

2.7.1.207

Accepted name:

protein-N^π-phosphohistidine—lactose phosphotransferase

Reaction:

[protein]-N^π-phospho-L-histidine + lactose_{[side 1]} = [protein]-L-histidine + lactose 6′-phosphate_{[side 2]}

Other name(s):

lacEF (gene names); lactose PTS permease; EII^Lac; Enzyme II^Lac

Systematic name:

protein-N^π-phospho-L-histidine:lactose N^π-phosphotransferase

Comments:

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Hengstenberg, W. Solubilization of the membrane bound lactose specific component of the staphylococcal PEP dependant phosphotransferase system. FEBS Lett. 8 (1970) 277–280. [DOI] [PMID: 11947593]
2.	Vadeboncoeur, C. and Proulx, M. Lactose transport in Streptococcus mutans: isolation and characterization of factor IIIlac, a specific protein component of the phosphoenolpyruvate-lactose phosphotransferase system. Infect. Immun. 46 (1984) 213–219. [PMID: 6480107]
3.	Breidt, F., Jr., Hengstenberg, W., Finkeldei, U. and Stewart, G.C. Identification of the genes for the lactose-specific components of the phosphotransferase system in the lac operon of Staphylococcus aureus. J. Biol. Chem. 262 (1987) 16444–16449. [PMID: 2824493]
4.	De Vos, W.M., Boerrigter, I., Van Rooijen, R.J., Reiche, B., Hengstenberg, W. Characterization of the lactose-specific enzymes of the phosphotransferase system in Lactococcus lactis. J. Biol. Chem. 265 (1990) 22554–22560. [PMID: 2125052]
5.	Peters, D., Frank, R. and Hengstenberg, W. Lactose-specific enzyme II of the phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus aureus. Purification of the histidine-tagged transmembrane component IICBLac and its hydrophilic IIB domain by metal-affinity chromatography, and functional characterization. Eur. J. Biochem. 228 (1995) 798–804. [DOI] [PMID: 7737179]

[EC 2.7.1.207 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.207]

2.7.1.208

Accepted name:

protein-N^π-phosphohistidine—maltose phosphotransferase

Reaction:

[protein]-N^π-phospho-L-histidine + maltose_{[side 1]} = [protein]-L-histidine + maltose 6′-phosphate_{[side 2]}

Other name(s):

malT (gene name); maltose PTS permease; EII^Mal; Enzyme II^Mal

Systematic name:

protein-N^π-phospho-L-histidine:maltose N^π-phosphotransferase

Comments:

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Robrish, S.A., Fales, H.M., Gentry-Weeks, C. and Thompson, J. Phosphoenolpyruvate-dependent maltose:phosphotransferase activity in Fusobacterium mortiferum ATCC 25557: specificity, inducibility, and product analysis. J. Bacteriol. 176 (1994) 3250–3256. [DOI] [PMID: 8195080]
2.	Webb, A.J., Homer, K.A. and Hosie, A.H. A phosphoenolpyruvate-dependent phosphotransferase system is the principal maltose transporter in Streptococcus mutans. J. Bacteriol. 189 (2007) 3322–3327. [DOI] [PMID: 17277067]

[EC 2.7.1.208 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.208]

2.7.1.211

Accepted name:

protein-N^π-phosphohistidine—sucrose phosphotransferase

Reaction:

[protein]-N^π-phospho-L-histidine + sucrose_{[side 1]} = [protein]-L-histidine + sucrose 6^G-phosphate_{[side 2]}

Other name(s):

scrAB (gene names); sucrose PTS permease; EII^Scr; Enzyme II^Scr

Systematic name:

protein-N^π-phospho-L-histidine:sucrose N^π-phosphotransferase

Comments:

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	St Martin, E.J. and Wittenberger, C.L. Characterization of a phosphoenolpyruvate-dependent sucrose phosphotransferase system in Streptococcus mutans. Infect. Immun. 24 (1979) 865–868. [PMID: 468378]
2.	Lunsford, R.D. and Macrina, F.L. Molecular cloning and characterization of scrB, the structural gene for the Streptococcus mutans phosphoenolpyruvate-dependent sucrose phosphotransferase system sucrose-6-phosphate hydrolase. J. Bacteriol. 166 (1986) 426–434. [DOI] [PMID: 3009399]
3.	Fouet, A., Arnaud, M., Klier, A. and Rapoport, G. Bacillus subtilis sucrose-specific enzyme II of the phosphotransferase system: expression in Escherichia coli and homology to enzymes II from enteric bacteria. Proc. Natl. Acad. Sci. USA 84 (1987) 8773–8777. [DOI] [PMID: 3122206]
4.	Sato, Y., Poy, F., Jacobson, G.R. and Kuramitsu, H.K. Characterization and sequence analysis of the scrA gene encoding enzyme IIScr of the Streptococcus mutans phosphoenolpyruvate-dependent sucrose phosphotransferase system. J. Bacteriol. 171 (1989) 263–271. [DOI] [PMID: 2536656]
5.	Titgemeyer, F., Jahreis, K., Ebner, R. and Lengeler, J.W. Molecular analysis of the scrA and scrB genes from Klebsiella pneumoniae and plasmid pUR400, which encode the sucrose transport protein Enzyme II Scr of the phosphotransferase system and a sucrose-6-phosphate invertase. Mol. Gen. Genet. 250 (1996) 197–206. [PMID: 8628219]
6.	Jiang, L., Cai, J., Wang, J., Liang, S., Xu, Z. and Yang, S.T. Phosphoenolpyruvate-dependent phosphorylation of sucrose by Clostridium tyrobutyricum ZJU 8235: evidence for the phosphotransferase transport system. Bioresour. Technol. 101 (2010) 304–309. [DOI] [PMID: 19726178]

[EC 2.7.1.211 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.211]

2.7.3.9

Accepted name:

phosphoenolpyruvate—protein phosphotransferase

Reaction:

phosphoenolpyruvate + protein histidine = pyruvate + protein N^π-phospho-L-histidine

Other name(s):

phosphoenolpyruvate sugar phosphotransferase enzyme I; phosphopyruvate-protein factor phosphotransferase; phosphopyruvate-protein phosphotransferase; sugar-PEP phosphotransferase enzyme I; phosphoenolpyruvate:protein-L-histidine N-pros-phosphotransferase

Systematic name:

phosphoenolpyruvate:protein-L-histidine N^π-phosphotransferase

Comments:

Enzyme I of the phosphotransferase system (cf. EC 2.7.1.69 protein-N^π-phosphohistidine—sugar phosphotransferase). Acts only on histidine residues in specific phosphocarrier proteins of low molecular mass (9.5 kDa) involved in bacterial sugar transport. A similar reaction, where the protein is the enzyme EC 2.7.9.2 pyruvate, water dikinase, is part of the mechanism of that enzyme.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-17-4

References:

1.	Postma, P.W. and Roseman, S. The bacterial phosphoenolpyruvate: sugar phosphotransferase system. Biochim. Biophys. Acta 457 (1976) 213–257. [PMID: 187249]

[EC 2.7.3.9 created 1972]

2.7.7.68

Accepted name:

2-phospho-L-lactate guanylyltransferase

Reaction:

(2S)-2-phospholactate + GTP = (2S)-lactyl-2-diphospho-5′-guanosine + diphosphate

For diagram of coenzyme F₄₂₀ biosynthesis, click here

Other name(s):

cofC (gene name) (ambiguous)

Systematic name:

GTP:2-phospho-L-lactate guanylyltransferase

Comments:

This enzyme is involved in the biosynthesis of coenzyme F₄₂₀, a redox-active cofactor, in all methanogenic archaea. cf. EC 2.7.7.105, phosphoenolpyruvate guanylyltransferase and EC 2.7.7.106, 3-phospho-(R)-glycerate guanylyltransferase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Grochowski, L.L., Xu, H. and White, R.H. Identification and characterization of the 2-phospho-L-lactate guanylyltransferase involved in coenzyme F₄₂₀ biosynthesis. Biochemistry 47 (2008) 3033–3037. [DOI] [PMID: 18260642]
2.	Braga, D., Last, D., Hasan, M., Guo, H., Leichnitz, D., Uzum, Z., Richter, I., Schalk, F., Beemelmanns, C., Hertweck, C. and Lackner, G. Metabolic pathway rerouting in Paraburkholderia rhizoxinica evolved long-overlooked derivatives of coenzyme F₄₂₀. ACS Chem. Biol. 14 (2019) 2088–2094. [PMID: 31469543]

[EC 2.7.7.68 created 2010, revised 2019, modified 2020]

2.7.7.104

Accepted name:

2-hydroxyethylphosphonate cytidylyltransferase

Reaction:

2-hydroxyethylphosphonate + CTP = cytidine 5′-{[hydroxy(2-hydroxyethyl)phosphonoyl]phosphate} + diphosphate

Other name(s):

Fom1

Systematic name:

CTP:2-hydroxyethylphosphonate cytidylyltransferase

Comments:

The enzyme, isolated from the bacterium Streptomyces wedmorensis, is involved in fosfomycin biosynthesis. The enzyme also is active as EC 5.4.2.9 phosphoenolpyruvate mutase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

Cho, S.H., Kim, S.Y., Tomita, T., Shiraishi, T., Park, J.S., Sato, S., Kudo, F., Eguchi, T., Funa, N., Nishiyama, M. and Kuzuyama, T. Fosfomycin biosynthesis via transient cytidylylation of 2-hydroxyethylphosphonate by the bifunctional Fom1 enzyme. ACS Chem. Biol. 12 (2017) 2209–2215. [PMID: 28727444]

[EC 2.7.7.104 created 2020]

2.7.7.105

Accepted name:

phosphoenolpyruvate guanylyltransferase

Reaction:

phosphoenolpyruvate + GTP = enolpyruvoyl-2-diphospho-5′-guanosine + diphosphate

For diagram of coenzyme F₄₂₀ biosynthesis, click here

Other name(s):

fbiD (gene name)

Systematic name:

GTP:phosphoenolpyruvate guanylyltransferase

Comments:

This enzyme is involved in the biosynthesis of coenzyme F₄₂₀, a redox-active cofactor, in mycobacteria. cf. EC 2.7.7.68, 2-phospho-L-lactate guanylyltransferase and EC 2.7.7.106, 3-phospho-(R)-glycerate guanylyltransferase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Bashiri, G., Antoney, J., Jirgis, E.NM., Shah, M.V., Ney, B., Copp, J., Stuteley, S.M., Sreebhavan, S., Palmer, B., Middleditch, M., Tokuriki, N., Greening, C., Scott, C., Baker, E.N. and Jackson, C.J. A revised biosynthetic pathway for the cofactor F₄₂₀ in prokaryotes. Nat. Commun. 10:1558 (2019). [DOI] [PMID: 30952857]
2.	Braga, D., Last, D., Hasan, M., Guo, H., Leichnitz, D., Uzum, Z., Richter, I., Schalk, F., Beemelmanns, C., Hertweck, C. and Lackner, G. Metabolic pathway rerouting in Paraburkholderia rhizoxinica evolved long-overlooked derivatives of coenzyme F₄₂₀. ACS Chem. Biol. 14 (2019) 2088–2094. [PMID: 31469543]

[EC 2.7.7.105 created 2020]

2.7.7.106

Accepted name:

3-phospho-D-glycerate guanylyltransferase

Reaction:

3-phospho-D-glycerate + GTP = 3-(D-glyceryl)-diphospho-5′-guanosine + diphosphate

Other name(s):

cofC (gene name) (ambiguous)

Systematic name:

GTP:3-phospho-D-glycerate guanylyltransferase

Comments:

The enzyme, characterized from the Gram-negative bacterium Paraburkholderia rhizoxinica, participates in the biosynthesis of 3PG-factor 420. The enzyme can also accept 2-phospho-L-lactate and phosphoenolpyruvate, but activity is much higher with 3-phospho-D-glycerate. cf. EC 2.7.7.68, 2-phospho-L-lactate guanylyltransferase and EC 2.7.7.105, phosphoenolpyruvate guanylyltransferase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

Braga, D., Last, D., Hasan, M., Guo, H., Leichnitz, D., Uzum, Z., Richter, I., Schalk, F., Beemelmanns, C., Hertweck, C. and Lackner, G. Metabolic pathway rerouting in Paraburkholderia rhizoxinica evolved long-overlooked derivatives of coenzyme F₄₂₀. ACS Chem. Biol. 14 (2019) 2088–2094. [PMID: 31469543]

[EC 2.7.7.106 created 2020]

2.7.8.28

Accepted name:

2-phospho-L-lactate transferase

Reaction:

(1) (2S)-lactyl-2-diphospho-5′-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + factor 420-0
(2) enolpyruvoyl-2-diphospho-5′-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + dehydro factor 420-0
(3) 3-[(R)-glyceryl]-diphospho-5′-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + 3PG-factor 420-0

For diagram of coenzyme F₄₂₀ biosynthesis, click here

Glossary:

factor 420 = coenzyme F₄₂₀ = N-(N-{O-[5-(8-hydroxy-2,4-dioxo-2,3,4,10-tetrahydropyrimido[4,5-b]quinolin-10-yl)-5-deoxy-L-ribityl-1-phospho]-(S)-lactyl}-γ-L-glutamyl)-L-glutamate
dehydro coenzyme F₄₂₀-0 = 7,8-didemethyl-8-hydroxy-5-deazariboflavin 5′-(1-carboxyvinyl)phosphate
GMP = guanosine 5′-phosphate

Other name(s):

cofD (gene name); fbiA (gene name); LPPG:Fo 2-phospho-L-lactate transferase; LPPG:7,8-didemethyl-8-hydroxy-5-deazariboflavin 2-phospho-L-lactate transferase; lactyl-2-diphospho-(5′)guanosine:Fo 2-phospho-L-lactate transferase

Systematic name:

(2S)-lactyl-2-diphospho-5′-guanosine:7,8-didemethyl-8-hydroxy-5-deazariboflavin 2-phospho-L-lactate transferase

Comments:

This enzyme is involved in the biosynthesis of factor 420, a redox-active cofactor, in methanogenic archaea and certain bacteria. The specific reaction catalysed in vivo is determined by the availability of substrate, which in turn is determined by the enzyme present in the organism - EC 2.7.7.68, 2-phospho-L-lactate guanylyltransferase, EC 2.7.7.105, phosphoenolpyruvate guanylyltransferase, or EC 2.7.7.106, 3-phospho-D-glycerate guanylyltransferase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Graupner, M., Xu, H. and White, R.H. Characterization of the 2-phospho-L-lactate transferase enzyme involved in coenzyme F₄₂₀ biosynthesis in Methanococcus jannaschii. Biochemistry 41 (2002) 3754–3761. [DOI] [PMID: 11888293]
2.	Forouhar, F., Abashidze, M., Xu, H., Grochowski, L.L., Seetharaman, J., Hussain, M., Kuzin, A., Chen, Y., Zhou, W., Xiao, R., Acton, T.B., Montelione, G.T., Galinier, A., White, R.H. and Tong, L. Molecular insights into the biosynthesis of the F₄₂₀ coenzyme. J. Biol. Chem. 283 (2008) 11832–11840. [DOI] [PMID: 18252724]
3.	Braga, D., Last, D., Hasan, M., Guo, H., Leichnitz, D., Uzum, Z., Richter, I., Schalk, F., Beemelmanns, C., Hertweck, C. and Lackner, G. Metabolic pathway rerouting in Paraburkholderia rhizoxinica evolved long-overlooked derivatives of coenzyme F₄₂₀. ACS Chem. Biol. 14 (2019) 2088–2094. [PMID: 31469543]

[EC 2.7.8.28 created 2010, modified 2020]

2.7.9.1

Accepted name:

pyruvate, phosphate dikinase

Reaction:

ATP + pyruvate + phosphate = AMP + phosphoenolpyruvate + diphosphate

Other name(s):

pyruvate, orthophosphate dikinase; pyruvate-phosphate dikinase (phosphorylating); pyruvate, phosphate dikinase; pyruvate-inorganic phosphate dikinase; pyruvate-phosphate dikinase; pyruvate-phosphate ligase; pyruvic-phosphate dikinase; pyruvic-phosphate ligase; pyruvate, Pi dikinase; PPDK

Systematic name:

ATP:pyruvate, phosphate phosphotransferase

Links to other databases:

BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9027-40-1

References:

1.	Hatch, M.D. and Slack, C.R. A new enzyme for the interconversion of pyruvate and phosphopyruvate and its role in the C4 dicarboxylic acid pathway of photosynthesis. Biochem. J. 106 (1968) 141–146. [PMID: 4305612]
2.	Reeves, R.E. A new enzyme with the glycolytic function of pyruvate kinase. J. Biol. Chem. 243 (1968) 3202–3204. [PMID: 4297474]
3.	Reeves, R.E. Pyruvate, phosphate dikinase from Bacteroides symbiosus. Biochem. J. 125 (1971) 531–539. [PMID: 5144757]
4.	Reeves, R.E., Menzies, R.A. and Hsu, D.S. The pyruvate-phosphate dikinase reaction. The fate of phosphate and the equilibrium. J. Biol. Chem. 243 (1968) 5486–5491. [PMID: 4302788]

[EC 2.7.9.1 created 1972]

2.7.9.2

Accepted name:

pyruvate, water dikinase

Reaction:

ATP + pyruvate + H₂O = AMP + phosphoenolpyruvate + phosphate

For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here

Other name(s):

phosphoenolpyruvate synthase; pyruvate-water dikinase (phosphorylating); PEP synthetase; phosphoenolpyruvate synthase; phoephoenolpyruvate synthetase; phosphoenolpyruvic synthase; phosphopyruvate synthetase

Systematic name:

ATP:pyruvate, water phosphotransferase

Comments:

A manganese protein.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9013-09-6

References:

1.	Berman, K.M. and Cohn, M. Phosphoenolpyruvate synthetase of Escherichia coli. Purification, some properties, and the role of divalent metal ions. J. Biol. Chem. 245 (1970) 5309–5318. [PMID: 4319237]
2.	Berman, K.M. and Cohn, M. Phosphoenolpyruvate synthetase. Partial reactions studied with adenosine triphosphate analogues and the inorganic phosphate-H₂18O exchange reaction. J. Biol. Chem. 245 (1970) 5319–5325. [PMID: 4319238]
3.	Cooper, R.A. and Kornberg, H.L. Net formation of phosphoenolpyruvate from pyruvate by Escherichia coli. Biochim. Biophys. Acta 104 (1965) 618–620. [DOI] [PMID: 5322808]
4.	Cooper, R.A. and Kornberg, H.L. Phosphoenolpyruvate synthetase. Methods Enzymol. 13 (1969) 309–314.

[EC 2.7.9.2 created 1976]

2.7.9.4

Accepted name:

α-glucan, water dikinase

Reaction:

ATP + α-glucan + H₂O = AMP + phospho-α-glucan + phosphate

Other name(s):

starch-related R1 protein; GWD

Systematic name:

ATP:α-glucan, water phosphotransferase

Comments:

Requires Mg²⁺. ATP appears to be the only phosphate donor. No activity could be detected using GTP, UTP, phosphoenolpyruvate or diphosphate [1]. The protein phosphorylates glucans exclusively on O-6 of glucosyl residues [2]. The protein phosphorylates itself with the β-phosphate of ATP, which is then transferred to the glucan [1].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 664327-94-0

References:

1.	Ritte, G., Lloyd, J.R., Eckermann, N., Rottmann, A., Kossmann, J. and Steup, M. The starch-related R1 protein is an α-glucan, water dikinase. Proc. Natl. Acad. Sci. USA 99 (2002) 7166–7171. [DOI] [PMID: 12011472]
2.	Ritte, G., Heydenreich, M., Mahlow, S., Haebel, S., Kötting, O. and Steup, M. Phosphorylation of C6- and C3-positions of glucosyl residues in starch is catalysed by distinct dikinases. FEBS Lett. 580 (2006) 4872–4876. [DOI] [PMID: 16914145]

[EC 2.7.9.4 created 2002]

3.1.3.9

Accepted name:

glucose-6-phosphatase

Reaction:

D-glucose 6-phosphate + H₂O = D-glucose + phosphate

Other name(s):

glucose 6-phosphate phosphatase

Systematic name:

D-glucose-6-phosphate phosphohydrolase

Comments:

Wide distribution in animal tissues. Also catalyses potent transphosphorylations from carbamoyl phosphate, hexose phosphates, diphosphate, phosphoenolpyruvate and nucleoside di- and triphosphates, to D-glucose, D-mannose, 3-methyl-D-glucose or 2-deoxy-D-glucose [cf. EC 2.7.1.62 (phosphoramidate—hexose phosphotransferase), EC 2.7.1.79 (diphosphate—glycerol phosphotransferase) and EC 3.9.1.1 (phosphoamidase)].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9001-39-2

References:

1.	Anchors, J.M. and Karnovsky, N.L. Purification of cerebral glucose-6-phosphatase. An enzyme involved in sleep. J. Biol. Chem. 250 (1975) 6408–6416. [PMID: 169241]
2.	Colilla, W., Jorgenson, R.A. and Nordlie, R.C. Mammalian carbamyl phosphate : glucose phosphotransferase and glucose-6-phosphate phosphohydrolase: extended tissue distribution. Biochim. Biophys. Acta 377 (1975) 117. [DOI] [PMID: 164220]
3.	Nordlie, R.C. Glucose-6-phosphatase, hydrolytic and synthetic activities. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 4, Academic Press, New York, 1971, pp. 543–610.
4.	Nordlie, R.C. Metabolic regulation by multifunctional glucose-6-phosphatase. Curr. Top. Cell. Regul. 8 (1974) 33. [PMID: 4370737]

[EC 3.1.3.9 created 1961]

3.1.3.16

Accepted name:

protein-serine/threonine phosphatase

Reaction:

[a protein]-serine/threonine phosphate + H₂O = [a protein]-serine/threonine + phosphate

Other name(s):

phosphoprotein phosphatase (ambiguous); protein phosphatase-1; protein phosphatase-2A; protein phosphatase-2B; protein phosphatase-2C; protein D phosphatase; phosphospectrin phosphatase; casein phosphatase; Aspergillus awamori acid protein phosphatase; calcineurin; phosphatase 2A; phosphatase 2B; phosphatase II; phosphatase IB; phosphatase C-II; polycation modulated (PCM-) phosphatase; phosphopyruvate dehydrogenase phosphatase; phosphatase SP; branched-chain α-keto acid dehydrogenase phosphatase; BCKDH phosphatase; 3-hydroxy 3-methylglutaryl coenzymeA reductase phosphatase; HMG-CoA reductase phosphatase; phosphatase H-II; phosphatase III; phosphatase I; protein phosphatase; phosphatase IV; phosphoprotein phosphohydrolase

Systematic name:

protein-serine/threonine-phosphate phosphohydrolase

Comments:

A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes that have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48 protein-tyrosine-phosphatase). The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1, phosphoamidase).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-75-6

References:

1.	Deutscher, J., Kessler, U. and Hengstenberg, W. Streptococcal phosphoenolpyruvate: sugar phosphotransferase system: purification and characterization of a phosphoprotein phosphatase which hydrolyzes the phosphoryl bond in seryl-phosphorylated histidine-containing protein. J. Bacteriol. 163 (1985) 1203–1209. [PMID: 2993239]
2.	Ingebritsen, T.S. and Cohen, P. The protein phosphatases involved in cellular regulation. 1. Classification and substrate specificities. Eur. J. Biochem. 132 (1983) 255–261. [DOI] [PMID: 6301824]
3.	Sundarajan, T.A. and Sarma, P.S. Substrate specificity of phosphoprotein phosphatase from spleen. Biochem. J. 71 (1959) 537–544. [PMID: 13638262]
4.	Tonks, N.K. and Cohen, P. The protein phosphatases involved in cellular regulation. Identification of the inhibitor-2 phosphatases in rabbit skeletal muscle. Eur. J. Biochem. 145 (1984) 65–70. [DOI] [PMID: 6092084]

[EC 3.1.3.16 created 1961, modified 1989, modified 2013]

3.1.3.60

Accepted name:

phosphoenolpyruvate phosphatase

Reaction:

phosphoenolpyruvate + H₂O = pyruvate + phosphate

Other name(s):

PEP phosphatase

Systematic name:

phosphoenolpyruvate phosphohydrolase

Comments:

Also acts, but more slowly, on a wide range of other monophosphates.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 122319-89-5

References:

1.	Duff, S.M.G., Lefebvre, D.D. and Plaxton, W.C. Purification and characterization of a phosphoenolpyruvate phosphatase from Brassica nigra suspension cells. Plant Physiol. 90 (1989) 734–741. [PMID: 16666836]
2.	Malhotra, O.P. and Kayastha, A.M. Chemical inactivation and active site groups of phosphoenolpyruvate-phosphatase from germinating mung beans (Vigna radiata). Plant Sci. 65 (1989) 161–170.
3.	Malhotra, O.P. and Kayastha, A.M. Isolation and characterization of phosphoenolpyruvate phosphatase from germinating mung beans (Vigna radiata). Plant Physiol. 93 (1990) 194–200. [PMID: 16667434]

[EC 3.1.3.60 created 1992]

3.11.1.3

Accepted name:

phosphonopyruvate hydrolase

Reaction:

3-phosphonopyruvate + H₂O = pyruvate + phosphate

For diagram of phosphonate metabolism, click here

Other name(s):

PPH

Comments:

Highly specific for phosphonopyruvate as substrate [2]. The reaction is not inhibited by phosphate but is inhibited by the phosphonates phosphonoformic acid, hydroxymethylphosphonic acid and 3-phosphonopropanoic acid [2]. The enzyme is activated by the divalent cations Co²⁺, Mg²⁺ and Mn²⁺. This enzyme is a member of the phosphoenolpyruvate mutase/isocitrate lyase superfamily [3].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Ternan, N.G., Hamilton, J.T. and Quinn, J.P. Initial in vitro characterisation of phosphonopyruvate hydrolase, a novel phosphate starvation-independent, carbon-phosphorus bond cleavage enzyme in Burkholderia cepacia Pal6. Arch. Microbiol. 173 (2000) 35–41. [PMID: 10648102]
2.	Kulakova, A.N., Wisdom, G.B., Kulakov, L.A. and Quinn, J.P. The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp. Pal2. J. Biol. Chem. 278 (2003) 23426–23431. [DOI] [PMID: 12697754]
3.	Chen, C.C., Han, Y., Niu, W., Kulakova, A.N., Howard, A., Quinn, J.P., Dunaway-Mariano, D. and Herzberg, O. Structure and kinetics of phosphonopyruvate hydrolase from Variovorax sp. Pal2: new insight into the divergence of catalysis within the PEP mutase/isocitrate lyase superfamily. Biochemistry 45 (2006) 11491–11504. [DOI] [PMID: 16981709]

[EC 3.11.1.3 created 2007]

4.1.1.31

Accepted name:

phosphoenolpyruvate carboxylase

Reaction:

phosphate + oxaloacetate = phosphoenolpyruvate + HCO₃^-

For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here

Other name(s):

phosphopyruvate (phosphate) carboxylase; PEP carboxylase; phosphoenolpyruvic carboxylase; PEPC; PEPCase; phosphate:oxaloacetate carboxy-lyase (phosphorylating)

Systematic name:

phosphate:oxaloacetate carboxy-lyase (adding phosphate, phosphoenolpyruvate-forming)

Comments:

This enzyme replenishes oxaloacetate in the tricarboxylic acid cycle when operating in the reverse direction. The reaction proceeds in two steps: formation of carboxyphosphate and the enolate form of pyruvate, followed by carboxylation of the enolate and release of phosphate.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9067-77-0

References:

1.	Chen, J.H. and Jones, R.F. Multiple forms of phosphoenolpyruvate carboxylase from Chlamydomonas reeinhardtii. Biochim. Biophys. Acta 214 (1970) 318–325. [DOI] [PMID: 5501374]
2.	Mazelis, M. and Vennesland, B. Carbon dioxide fixation into oxalacetate in higher plants. Plant Physiol. 32 (1957) 591–600. [PMID: 16655053]
3.	Tovar-Mendez, A., Mujica-Jimenez, C. and Munoz-Clares, R.A. Physiological implications of the kinetics of maize leaf phosphoenolpyruvate carboxylase. Plant Physiol. 123 (2000) 149–160. [PMID: 10806233]

[EC 4.1.1.31 created 1961, modified 2011]

4.1.1.32

Accepted name:

phosphoenolpyruvate carboxykinase (GTP)

Reaction:

GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO₂

Other name(s):

phosphoenolpyruvate carboxylase (ambiguous); phosphopyruvate carboxylase (ambiguous); phosphopyruvate (guanosine triphosphate) carboxykinase; phosphoenolpyruvic carboxykinase (GTP); phosphopyruvate carboxylase (GTP); phosphoenolpyruvic carboxylase (GTP); phosphoenolpyruvic carboxykinase (ambiguous); phosphoenolpyruvate carboxykinase (ambiguous); PEP carboxylase (ambiguous); GTP:oxaloacetate carboxy-lyase (transphosphorylating)

Systematic name:

GTP:oxaloacetate carboxy-lyase (adding GTP; phosphoenolpyruvate-forming)

Comments:

ITP can act as phosphate donor.

Links to other databases:

BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9013-08-5

References:

1.	Change, H.-C. and Lane, M.D. The enzymatic carboxylation of phosphoenolpyruvate. II. Purification and properties of liver mitochondrial phosphoenolpyruvate carboxykinase. J. Biol. Chem. 241 (1966) 2413–2420. [PMID: 5911620]
2.	Kurahashi, K., Pennington, R.J. and Utter, M.J. Nucleotide specificity of oxalacetic carboxylase. J. Biol. Chem. 226 (1957) 1059–1075. [PMID: 13438893]

[EC 4.1.1.32 created 1961]

4.1.1.38

Accepted name:

phosphoenolpyruvate carboxykinase (diphosphate)

Reaction:

diphosphate + oxaloacetate = phosphate + phosphoenolpyruvate + CO₂

Other name(s):

phosphopyruvate carboxylase (ambiguous); PEP carboxyphosphotransferase (ambiguous); PEP carboxykinase (ambiguous); phosphopyruvate carboxykinase (pyrophosphate); PEP carboxylase (ambiguous); phosphopyruvate carboxykinase (ambiguous); phosphoenolpyruvic carboxykinase (ambiguous); phosphoenolpyruvic carboxylase (ambiguous); phosphoenolpyruvate carboxytransphosphorylase (ambiguous); phosphoenolpyruvate carboxykinase (ambiguous); phosphoenolpyruvic carboxykinase; phosphoenolpyruvic carboxylase; PEPCTrP; phosphoenolpyruvic carboxykinase (pyrophosphate); phosphoenolpyruvic carboxylase (pyrophosphate); phosphoenolpyruvate carboxylase (ambiguous); phosphoenolpyruvate carboxyphosphotransferase (ambiguous); phosphoenolpyruvic carboxytransphosphorylase (ambiguous); phosphoenolpyruvate carboxylase (pyrophosphate); phosphopyruvate carboxylase (pyrophosphate); diphosphate:oxaloacetate carboxy-lyase (transphosphorylating)

Systematic name:

diphosphate:oxaloacetate carboxy-lyase (transphosphorylating; phosphoenolpyruvate-forming)

Comments:

Also catalyses the reaction: phosphoenolpyruvate + phosphate = pyruvate + diphosphate.

Links to other databases:

BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9013-12-1

References:

1.	Lochmuller, H., Wood, H.G. and Davis, J.J. Phosphoenolpyruvate carboxytransphosphorylase. II. Crystallization and properties. J. Biol. Chem. 241 (1966) 5678–5691. [PMID: 4288896]

[EC 4.1.1.38 created 1965]