An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.
Common name: UDP-N-acetylglucosamine 1-carboxyvinyltransferase
Reaction: phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine
For diagram 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
Systematic name: phosphoenolpyruvate:UDP-N-acetyl-D-glucosamine 1-carboxyvinyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, WIT, 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]
Common name: adenylate dimethylallyltransferase
Reaction: dimethylallyl diphosphate + AMP = diphosphate + N6-(dimethylallyl)adenosine 5'-phosphate
Other name(s): cytokinin synthase; isopentenyltransferase; 2-isopentenyl-diphosphate:AMP δ2-isopentenyltransferase; adenylate isopentenyltransferase
Systematic name: dimethylallyl-diphosphate:AMP dimethylallyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 72840-95-0
References:
1. Chen, C.-M. and Melitz, D.K. Cytokinin biosynthesis in a cell-free system from cytokinin-autotrophic tobacco tissue cultures. FEBS Lett. 107 (1979) 15-20. [PMID: 499537]
Common name: cysteine synthase
Reaction: O3-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
Other name(s): O-acetyl-L-serine sulfhydrylase; O-acetyl-L-serine sulfohydrolase; O-acetylserine (thiol)-lyase; O-acetylserine (thiol)-lyase A; O-acetylserine sulfhydrylase; O3-acetyl-L-serine acetate-lyase (adding hydrogen-sulfide); acetylserine sulfhydrylase; cysteine synthetase
Systematic name: O3-acetyl-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase
Comments: A pyridoxal-phosphate protein. Some alkyl thiols, cyanide, pyrazole and some other heterocyclic compounds can act as acceptors. Not identical with EC 2.5.1.51 (β-pyrazolylalanine synthase), EC 2.5.1.52 (L-mimosine synthase) and EC 2.5.1.53 (uracilylalanine synthase).
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37290-89-4
References:
1. Becker, M.A., Kredich, N.M. and Tomkins, G.M. The purification and characterization of O-acetylserine sulfhydrylase-A from Salmonella typhimurium. J. Biol. Chem. 244 (1969) 2418-2427. [PMID: 4891157]
2. Hara, S., Payne, M.A., Schnackerz, K.D. and Cook, P.F. A rapid purification procedure and computer-assisted sulfide ion selective electrode assay for O-acetylserine sulfhydrylase from Salmonella typhimurium. Protein Expr. Purif. 1 (1990) 70-76. [PMID 2152186]
3. Ikegami, F., Kaneko, M., Lambein, F., Kuo, Y.-H. and Murakoshi, I. Difference between uracilylalanine synthases and cysteine synthases in Pisum sativum. Phytochemistry 26 (1987) 2699-2704.
4. Murakoshi, I., Kaneko, M., Koide, C. and Ikegami, F. Enzymatic-synthesis of the neuroexcitatory amino-acid quisqualic by cysteine synthase. Phytochemistry 25 (1986) 2759-2763.
5. Tai, C.H., Burkhard, P., Gani, D., Jenn, T., Johnson, C. and Cook, P.F. Characterization of the allosteric anion-binding site of O-acetylserine sulfhydrylase. Biochemistry 40 (2001) 7446-7452. [PMID: 11412097]
6. Bettati, S., Benci, S., Campanini, B., Raboni, S., Chirico, G., Beretta, S., Schnackerz, K.D., Hazlett, T.L., Gratton, E. and Mozzarelli, A. Role of pyridoxal 5'-phosphate in the structural stabilization of O-acetylserine sulfhydrylase. J. Biol. Chem. 275 (2000) 40244-40251. [PMID: 10995767]
Common name: cystathionine γ-synthase
Reaction: O-succinyl-L-homoserine + L-cysteine = cystathionine + succinate
For diagram click here.
Other name(s): O-succinyl-L-homoserine succinate-lyase (adding cysteine); O-succinylhomoserine (thiol)-lyase; homoserine O-transsuccinylase; O-succinylhomoserine synthase; O-succinylhomoserine synthetase; cystathionine synthase; cystathionine synthetase; homoserine transsuccinylase
Systematic name: O4-succinyl-L-homoserine:L-cysteine S-(3-amino-3-carboxypropyl)transferase
Comments: A pyridoxal-phosphate protein. Also reacts with hydrogen sulfide and methanethiol as replacing agents, producing homocysteine and methionine, respectively. In the absence of thiol, can also catalyse α,γ-elimination to form 2-oxobutanoate, succinate and ammonia.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9030-70-0
References:
1. Flavin, M. and Slaughter, C. Enzymatic synthesis of homocysteine or methionine directly from O-succinyl-homoserine. Biochim. Biophys. Acta 132 (1967) 400-405. [PMID: 5340123]
2. Kaplan, M.M. and Flavin, M. Cystathionine γ-synthetase of Salmonella. Catalytic properties of a new enzyme in bacterial methionine biosynthesis. J. Biol. Chem. 241 (1966) 4463-4471. [PMID: 5922970]
3. Wiebers, J.L. and Garner, H.R. Homocysteine and cysteine synthetases of Neurospora crassa. Purification, properties, and feedback control of activity. J. Biol. Chem. 242 (1967) 12-23. [PMID: 6016326]
4. Wiebers, J.L. and Garner, H.R. Acyl derivatives of homoserine as substrates for homocysteine synthesis in Neurospora crassa, yeast, and Escherichia coli. J. Biol. Chem. 242 (1967) 5644-5649.
5. Clausen, T., Huber, R., Prade, L., Wahl, M.C. and Messerschmidt, A. Crystal structure of Escherichia coli cystathionine γ-synthase at 1.5 Å resolution. EMBO J. 17 (1998) 6827-6838. [PMID: 9843488]
6. Ravanel, S., Gakiere, B., Job, D. and Douce, R. Cystathionine γ-synthase from Arabidopsis thaliana: purification and biochemical characterization of the recombinant enzyme overexpressed in Escherichia coli. Biochem. J. 331 (1998) 639-648. [PMID: 9531508]
Common name: O-acetylhomoserine aminocarboxypropyltransferase
Reaction: O-acetyl-L-homoserine + methanethiol = L-methionine + acetate
For diagram click here.
Other name(s): O-acetyl-L-homoserine acetate-lyase (adding methanethiol); O-acetyl-L-homoserine sulfhydrolase; O-acetylhomoserine (thiol)-lyase; O-acetylhomoserine sulfhydrolase; methionine synthase
Systematic name: O-acetyl-L-homoserine:methanethiol 3-amino-3-carboxypropyltransferase
Comments: Also reacts with other thiols and H2S, producing homocysteine or thioethers. The name methionine synthase is more commonly applied to EC 2.1.1.13 5-methyltetrahydrofolate-homocysteine S-methyltransferase. The enzyme from baker's yeast also catalyses the reaction of EC 2.5.1.47 cysteine synthase, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37290-90-7
References:
1. Kerr, D. O-Acetylhomoserine sulfhydrylase (Neurospora). Methods Enzymol. 17B (1971) 446-450.
2. Smith, I.K. and Thompson, J.F. Utilization of S-methylcysteine and methylmercaptan by methionineless mutants of Neurospora and the pathway of their conversion to methionine. II. Enzyme studies. Biochim. Biophys. Acta 184 (1969) 130-138. [PMID: 5791104]
3. Yamagata, S. and Takeshima, K. O-Acetylserine and O-acetylhomoserine sulfhydrylase of yeast. Further purification and characterization as a pyridoxal enzyme. J. Biochem. (Tokyo) 80 (1976) 777-785. [PMID: 795806]
4. Yamagata, S. O-Acetylserine and O-acetylhomoserine sulfhydrylase of yeast. Subunit structure. J. Biochem. (Tokyo) 80 (1976) 787-797. [PMID: 795807]
5. Yamagata, S., Takeshima, K. and Naikai, N. Evidence for the identity of O-acetylserine sulfhydrylase with O-acetylhomoserine sulfhydrylase in yeast. J. Biochem. (Tokyo) 75 (1974) 1221-1229. [PMID: 4609980]
6. Yamagata, S. Roles of O-acetyl-L-homoserine sulfhydrylases in micro-organisms. Biochimie 71 (1989) 1125-1143. [PMID: 2517474]
7. Shimizu, H., Yamagata, S., Masui, R., Inoue, Y., Shibata, T., Yokoyama, S., Kuramitsu, S. and Iwama, T. Cloning and overexpression of the oah1 gene encoding O-acetyl-L-homoserine sulfhydrylase of Thermus thermophilus HB8 and characterization of the gene product. Biochim. Biophys. Acta 1549 (2001) 61-72. [PMID: 11566369]
Common name: zeatin 9-aminocarboxyethyltransferase
Reaction: O-acetyl-L-serine + zeatin = lupinate + acetate
For diagram click here.
Glossary:
lupinic acid
zeatin
Other name(s): β-(9-cytokinin)-alanine synthase; β-(9-cytokinin)alanine synthase; O-acetyl-L-serine acetate-lyase (adding N6-substituted adenine); lupinate synthetase; lupinic acid synthase; lupinic acid synthetase
Systematic name: O3-acetyl-L-serine:zeatin 2-amino-2-carboxyethyltransferase
Comments: The enzyme acts not only on zeatin but also on other N6-substituted adenines. The reaction destroys their cytokinin activity and forms the corresponding 3-(adenin-9-yl)-L-alanine.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 62683-23-2
References:
1. Entsch, B., Parker, C.W. and Letham, D.S. An enzyme from lupin seeds forming alanine derivatives of cytokinins. Phytochemistry 22 (1983) 375-381.
2. Mok, D.W.S. and Mok, M.C. Cytokinin metabolism and action. Ann. Rev. Plant Physiol. Plant Mol. Biol. 52 (2001) 89-118.
Common name: β-pyrazolylalanine synthase
Reaction: O-acetyl-L-serine + pyrazole = 3-(pyrazol-1-yl)-L-alanine + acetate
Other name(s): β-(1-pyrazolyl)alanine synthase; β-pyrazolealanine synthase; β-pyrazolylalanine synthase (acetylserine); O3-acetyl-L-serine acetate-lyase (adding pyrazole); BPA-synthase; pyrazolealanine synthase; pyrazolylalaninase
Systematic name: O3-acetyl-L-serine:pyrazole 1-(2-amino-2-carboxyethyl)transferase
Comments: The enzyme is highly specific for acetylserine and pyrazole. Not identical with EC 2.5.1.52 L-mimosine synthase.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37290-81-6
References:
1. Murakoshi, I., Ikegami, F., Hinuma, Y. and Hanma, Y. Purification and characterization of β-(pyrazol-1-yl)-L-alanine synthase from Citrullus vulgaris. Phytochemistry 23 (1984) 973-977.
2. Murakoshi, I., Ikegami, F., Hinuma, Y. and Hanma, Y. Purification and characterization of L-mimosine synthase from Leucaena leucocephala. Phytochemistry 23 (1984) 1905-1908.
3. Murakoshi, I., Kuramoto, H. and Haginiwa, J. The enzymic synthesis of β-substituted alanines. Phytochemistry 11 (1972) 177-182.
4. Noji, M., Murakoshi, I. and Saito K. Evidence for identity of β-pyrazolealanine synthase with cysteine synthase in watermelon: formation of β-pyrazole-alanine by cloned cysteine synthase in vitro and in vivo. Biochem. Biophys. Res. Commun. 197 (1993) 1111-1117. [PMID: 8280125]
Common name: L-mimosine synthase
Reaction: O3-acetyl-L-serine + 3,4-dihydroxypyridine = 3-(3,4-dihydroxypyridin-1-yl)-L-alanine + acetate
Other name(s): O3-acetyl-L-serine acetate-lyase (adding 3,4-dihydroxypyridin-1-yl)
Systematic name: O3-acetyl-L-serine:3,4-dihydroxypyridine 1-(2-amino-2-carboxyethyl)transferase
Comments: Brings about the biosynthesis of L-mimosine in Mimosa and Leucaena sp. Not identical with EC 2.5.1.51 β-pyrazolylalanine synthase.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 93229-75-5
References:
1. Murakoshi, I., Ikegami, F., Hinuma, Y. and Hanma, Y. Purification and characterization of L-mimosine synthase from Leucaena leucocephala. Phytochemistry 23 (1984) 1905-1908.
Common name: uracilylalanine synthase
Reaction: O3-acetyl-L-serine + uracil = 3-(uracil-1-yl)-L-alanine + acetate
Other name(s): O3-acetyl-L-serine acetate-lyase (adding uracil); isowillardiine synthase; willardiine synthase
Systematic name: O3-acetyl-L-serine:uracil 1-(2-amino-2-carboxyethyl)transferase
Comments: Both L-willardiine and L-isowillardiine are produced in the reaction. Not identical with EC 2.5.1.47 cysteine synthase.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 113573-73-2
References:
1. Ahmmad, M.A.S., Maskall, C.S. and Brown, E.G. Partial-purification and properties of willardiine and synthase activity from Pisum sativum. Phytochemistry 23 (1984) 265-270.
2. Ikegami, F., Kaneko, M., Lambein, F., Kuo, Y.-H. and Murakoshi, I. Difference between uracilylalanine synthases and cysteine synthases in Pisum sativum. Phytochemistry 26 (1987) 2699-2704.
3. Murakoshi, I., Ikegami, F., Ookawa, N., Ariki, T., Haginiwa, J., Kuo, Y.-H. and Lambein, F. Biosynthesis of the uracilylalanines willardiine and isowillardiine in higher plants. Phytochemistry 17 (1978) 1571-1576.
Common name: 3-deoxy-7-phosphoheptulonate synthase
Reaction: phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate + phosphate
For diagram click here and mechanism 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, WIT, 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.
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. [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]
Common name: 3-deoxy-8-phosphooctulonate synthase
Reaction: phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 2-dehydro-3-deoxy-D-octonate 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, WIT, 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.
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. [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. [PMID: 11371194]
Common name: N-acetylneuraminate synthase
Reaction: phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O = phosphate + N-acetylneuraminate
For diagram 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, WIT, 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.
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. [PMID: 9438985]
Common name: N-acylneuraminate-9-phosphate synthase
Reaction: phosphoenolpyruvate + N-acyl-D-mannosamine 6-phosphate + H2O = N-acylneuraminate 9-phosphate + phosphate
For diagram 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, WIT, 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.
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. [PMID: 10873658]
Common name: holo-ACP synthase
Reaction: 2'-(5"-triphosphoribosyl)-3'-dephospho-CoA + apo-citrate lyase = holo-citrate lyase + diphosphate
Other name(s): 2'-(5"-phosphoribosyl)-3'-dephospho-CoA transferase; 2'-(5"-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate lyase; CitX
Systematic name: 2'-(5"-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate lyase adenylyltransferase
Comments: Requires Mg2+. The enzyme from Escherichia coli can also use ATP, CTP, GTP and UTP as a substrate in vitro. The corresponding mononucleotides are transferred to serine-14 of the acyl carrier protein of citrate lyase with release of diphosphate; the linkage to serine is via a phosphodiester bond.
References:
1. Schneider, K., Dimroth, P. and Bott, M. Biosynthesis of the prosthetic group of citrate lyase. Biochemistry 39 (2000) 9438-9450. [PMID: 10924139]
2. Schneider, K., Dimroth, P. and Bott, M. Identification of triphosphoribosyl-dephospho-CoA as precursor of the citrate lyase prosthetic group. FEBS Lett. 483 (2000) 165-168. [PMID: 11042274]
Common name: phospho-N-acetylmuramoyl-pentapeptide-transferase
Reaction: UDPMur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
For diagram click here.
Other names: MraY transferase; UDP-MurNAc-L-Ala-D-γ-Glu-L-Lys-D-Ala-D-Ala:C55-isoprenoid alcohol transferase; UDP-MurNAc-Ala-γDGlu-Lys-DAla-DAla:undecaprenylphosphate transferase; phospho-N-acetylmuramoyl pentapeptide translocase; phospho-MurNAc-pentapeptide transferase; phospho-NAc-muramoyl-pentapeptide translocase (UMP); phosphoacetylmuramoylpentapeptide translocase; phosphoacetylmuramoylpentapeptidetransferase
Systematic name: UDPMurAc(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala):undecaprenyl-phosphate phospho-N-acetylmuramoyl-pentapeptide-transferase
Comments: In Gram-negative and some Gram-positive organisms the L-lysine is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm), which is combined with adjacent residues through its L-centre. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, click here).
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9068-50-2
References:
1. Heydanek, M.G., Jr. and Neuhaus, F.C. The initial stage in peptidoglycan synthesis. IV. Solubilization of phospho-N-acetylmuramyl-pentapeptide translocase. Biochemistry 8 (1969) 1474-1481. [PMID: 5805290]
2. Higashi, Y., Strominger, J.L. and Sweeley, C.C. Structure of a lipid intermediate in cell wall peptidoglycan synthesis: a derivative of a C55 isoprenoid alcohol. Proc. Natl. Acad. Sci. USA 57 (1967) 1878-1884. [PMID: 5231417]
3. Struve, W.G., Sinha, R.K. and Neuhaus, F.C. On the initial stage in peptidoglycan synthesis. Phospho-N-acetylmuramyl-pentapeptide translocase (uridine monophosphate). Biochemistry 5 (1966) 82-93. [PMID: 5938956]
4. van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503-519. [PMID: 11699883]
Common name: triphosphoribosyl-dephospho-CoA synthase
Reaction: ATP + 3-dephospho-CoA = 2'-(5"-triphosphoribosyl)-3'-dephospho-CoA + adenine
Other name(s): 2'-(5"-triphosphoribosyl)-3-dephospho-CoA synthase; ATP:dephospho-CoA 5-triphosphoribosyl transferase; CitG
Systematic name: ATP:3-dephospho-CoA 5"-triphosphoribosyltransferase
Comments: ATP cannot be replaced by GTP, CTP, UTP, ADP or AMP. 2'-(5"-Triphosphoribosyl)-3'-dephospho-CoA is the precursor of the phosphoribosyl-3-dephospho-CoA prosthetic group of the acyl carrier protein subunit of EC 4.1.3.6, citrate (pro-3S) lyase.
References:
1. Schneider, K., Dimroth, P. and Bott, M. Biosynthesis of the prosthetic group of citrate lyase. Biochemistry 39 (2000) 9438-9450. [PMID: 10924139]
2. Schneider, K., Dimroth, P. and Bott, M. Identification of triphosphoribosyl-dephospho-CoA as precursor of the citrate lyase prosthetic group. FEBS Lett. 483 (2000) 165-168. [PMID: 11042274]
Common 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. The protein phosphorylates glucans at both the C-6 and C-3 position of the glucosyl residues. The protein phosphorylates itself with the β-phosphate of ATP, which is then transferred to the glucan.
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. [PMID: 12011472]
Common name: glutaconate CoA-transferase
Reaction: acetyl-CoA + (E)-glutaconate = acetate + glutaconyl-1-CoA
Systematic name: acetyl-CoA:(E)-glutaconate CoA-transferase
Comments: Glutarate, (R)-2-hydroxyglutarate, propenoate and propanoate, but not (Z)-glutaconate, can also act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, UM-BBD, WIT, CAS registry number: 79078-99-2
References:
1. Buckel, W.S., Dorn, U. and Semmler, R. Glutaconate CoA-transferase from Acidaminococcus fermentans. Eur. J. Biochem. 118 (1981) 315-321. [PMID: 6945182]