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Your query returned 5 entries. Printable version

1.3.1.98

Accepted name:

UDP-N-acetylmuramate dehydrogenase

Reaction:

UDP-N-acetyl-α-D-muramate + NADP⁺ = UDP-N-acetyl-3-O-(1-carboxyvinyl)-α-D-glucosamine + NADPH + H⁺

Other name(s):

MurB reductase; UDP-N-acetylenolpyruvoylglucosamine reductase; UDP-N-acetylglucosamine-enoylpyruvate reductase; UDP-GlcNAc-enoylpyruvate reductase; uridine diphosphoacetylpyruvoylglucosamine reductase; uridine diphospho-N-acetylglucosamine-enolpyruvate reductase; uridine-5′-diphospho-N-acetyl-2-amino-2-deoxy-3-O-lactylglucose:NADP-oxidoreductase

Systematic name:

UDP-N-acetyl-α-D-muramate:NADP⁺ oxidoreductase

Comments:

A flavoprotein (FAD). NADH can to a lesser extent replace NADPH.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39307-28-3

References:

1.	Taku, A. and Anwar, R.A. Biosynthesis of uridine diphospho-N-acetylmuramic acid. IV. Activation of uridine diphospho-N-acetylenolpyruvylglucosamine reductase by monovalent cations. J. Biol. Chem. 248 (1973) 4971. [PMID: 4717533]
2.	Taku, A., Gunetileke, K.G. and Anwar, R.A. Biosynthesis of uridine diphospho-N-acetylmuramic acid. 3. Purification and properties of uridine diphospho-N-acetylenolpyruvyl-glucosamine reductase. J. Biol. Chem. 245 (1970) 5012–5016. [PMID: 4394163]
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 1.3.1.98 created 1976 as EC 1.1.1.158, modified 1983, modified 2002, transferred 2013 to EC 1.3.1.98]

2.7.1.221

Accepted name:

N-acetylmuramate 1-kinase

Reaction:

ATP + N-acetyl-D-muramate = ADP + N-acetyl-α-D-muramate 1-phosphate

Glossary:

N-acetyl-D-muramate = 3-O-[(1R)-1-carboxyethyl]-2-acetoxy-2-deoxy-D-glucopyranose

Other name(s):

amgK (gene name)

Systematic name:

ATP:N-acetyl-D-muramate 1-phosphotransferase

Comments:

The enzyme, characterized from Pseudomonas species, participates in a peptidoglycan salvage pathway.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Gisin, J., Schneider, A., Nagele, B., Borisova, M. and Mayer, C. A cell wall recycling shortcut that bypasses peptidoglycan de novo biosynthesis. Nat. Chem. Biol. 9 (2013) 491–493. [DOI] [PMID: 23831760]

[EC 2.7.1.221 created 2017]

2.7.7.99

Accepted name:

N-acetyl-α-D-muramate 1-phosphate uridylyltransferase

Reaction:

UDP + N-acetyl-α-D-muramate 1-phosphate = UDP-N-acetyl-α-D-muramate + phosphate

Glossary:

N-acetyl-α-D-muramate = 3-O-[(1R)-1-carboxyethyl]-2-acetoxy-2-deoxy-D-glucopyranose

Other name(s):

murU (gene name)

Systematic name:

UDP:N-acetyl-α-D-muramate 1-phosphate uridylyltransferase

Comments:

The enzyme, characterized from Pseudomonas species, participates in a peptidoglycan salvage pathway.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Gisin, J., Schneider, A., Nagele, B., Borisova, M. and Mayer, C. A cell wall recycling shortcut that bypasses peptidoglycan de novo biosynthesis. Nat. Chem. Biol. 9 (2013) 491–493. [DOI] [PMID: 23831760]
2.	Renner-Schneck, M., Hinderberger, I., Gisin, J., Exner, T., Mayer, C. and Stehle, T. Crystal structure of the N-acetylmuramic acid α-1-phosphate (MurNAc-α1-P) uridylyltransferase MurU, a minimal sugar nucleotidyltransferase and potential drug target enzyme in Gram-negative pathogens. J. Biol. Chem. 290 (2015) 10804–10813. [DOI] [PMID: 25767118]

[EC 2.7.7.99 created 2017]

6.3.2.8

Accepted name:

UDP-N-acetylmuramate—L-alanine ligase

Reaction:

ATP + UDP-N-acetyl-α-D-muramate + L-alanine = ADP + phosphate + UDP-N-acetyl-α-D-muramoyl-L-alanine

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

Other name(s):

MurC synthetase; UDP-N-acetylmuramoyl-L-alanine synthetase; uridine diphospho-N-acetylmuramoylalanine synthetase; UDP-N-acetylmuramoylalanine synthetase; L-alanine-adding enzyme; UDP-acetylmuramyl-L-alanine synthetase; UDPMurNAc-L-alanine synthetase; L-Ala ligase; uridine diphosphate N-acetylmuramate:L-alanine ligase; uridine 5′-diphosphate-N-acetylmuramyl-L-alanine synthetase; uridine-diphosphate-N-acetylmuramate:L-alanine ligase; UDP-MurNAc:L-alanine ligase; alanine-adding enzyme; UDP-N-acetylmuramyl:L-alanine ligase; UDP-N-acetylmuramate:L-alanine ligase (ADP-forming)

Systematic name:

UDP-N-acetyl-α-D-muramate:L-alanine ligase (ADP-forming)

Comments:

Involved in the synthesis of a cell-wall peptide in bacteria.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9023-52-3

References:

1.	Ito, E. and Strominger, J.L. Enzymatic synthesis of the peptide in bacterial uridine nucleotides. I. Enzymatic addition of L-alanine, D-glutamic acid, and L-lysine. J. Biol. Chem. 237 (1962) 2689–2695.
2.	Nathenson, S.G., Strominger, J.L. and Ito, E. Enzymatic synthesis of the peptide in bacterial uridine nucleotides. IV. Purification and properties of D-glutamic acid-adding enzyme. J. Biol. Chem. 239 (1964) 1773–1776. [PMID: 14213349]
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 6.3.2.8 created 1965, modified 2002]

6.3.2.45

Accepted name:

UDP-N-acetylmuramate—L-alanyl-γ-D-glutamyl-meso-2,6-diaminoheptanedioate ligase

Reaction:

ATP + UDP-N-acetyl-α-D-muramate + L-alanyl-γ-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-γ-D-glutamyl-meso-2,6-diaminoheptanedioate

Glossary:

meso-2,6-diaminoheptanedioate = meso-2,6-diaminopimelate

Other name(s):

murein peptide ligase; Mpl; yjfG (gene name); UDP-MurNAc:L-Ala-γ-D-Glu-meso-A2pm ligase; UDP-N-acetylmuramate:L-alanyl-γ-D-glutamyl-meso-diaminopimelate ligase

Systematic name:

UDP-N-acetylmuramate:L-alanyl-γ-D-glutamyl-meso-2,6-diaminoheptanedioate ligase2015

Comments:

The enzyme catalyses the reincorporation into peptidoglycan of the tripeptide L-alanyl-γ-D-glutamyl-2,6-meso-diaminoheptanedioate released during the maturation and constant remodeling of this bacterial cell wall polymer that occur during cell growth and division. The enzyme can also use the tetrapeptide L-alanyl-γ-D-glutamyl-meso-2,6-diaminoheptanedioyl-D-alanine or the pentapeptide L-alanyl-γ-D-glutamyl-meso-2,6-diaminoheptanedioyl-D-alanyl-D-alanine in vivo and in vitro. Requires Mg²⁺.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Mengin-Lecreulx, D., van Heijenoort, J. and Park, J.T. Identification of the mpl gene encoding UDP-N-acetylmuramate: L-alanyl-γ-D-glutamyl-meso-diaminopimelate ligase in Escherichia coli and its role in recycling of cell wall peptidoglycan. J. Bacteriol. 178 (1996) 5347–5352. [DOI] [PMID: 8808921]
2.	Herve, M., Boniface, A., Gobec, S., Blanot, D. and Mengin-Lecreulx, D. Biochemical characterization and physiological properties of Escherichia coli UDP-N-acetylmuramate:L-alanyl-γ-D-glutamyl-meso-diaminopimelate ligase. J. Bacteriol. 189 (2007) 3987–3995. [DOI] [PMID: 17384195]

[EC 6.3.2.45 created 2014]