UDP-N-acetylmuramate dehydrogenase

From Wikipedia, the free encyclopedia

In enzymology, an UDP-N-acetylmuramate dehydrogenase (EC 1.1.1.158) is an enzyme that catalyzes the chemical reaction

UDP-N-acetylmuramate + NADP⁺ $\rightleftharpoons$ UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + NADPH + H⁺

Thus, the two substrates of this enzyme are UDP-N-acetylmuramate and NADP⁺, whereas its 3 products are UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine, NADPH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is UDP-N-acetylmuramate:NADP+ oxidoreductase. Other names in common use include 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-, and lactylglucose:NADP-oxidoreductase. This enzyme participates in aminosugars metabolism. It employs one cofactor, FAD.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1HSK, 1MBB, 1MBT, 1UXY, 2GQT, 2GQU, 2MBR, and 2Q85.

[edit] References

IUBMB entry for 1.1.1.158
BRENDA references for 1.1.1.158 (Recommended.)
PubMed references for 1.1.1.158
PubMed Central references for 1.1.1.158
Google Scholar references for 1.1.1.158
Taku A, Anwar RA (1973). "Biosynthesis of uridine diphospho-N-acetylmuramic acid. IV Activation of uridine diphospho-N-acetylenolpyruvylglucosamine reductase by monovalent cations". J. Biol. Chem. 248: 4971–6. PMID 4717533.
Taku A, Gunetileke KG, Anwar RA (1970). "Biosynthesis of uridine diphospho-N-acetylmuramic acid. 3 Purification and properties of uridine diphospho-N-acetylenolpyruvyl-glucosamine reductase". J. Biol. Chem. 245: 5012–6. PMID 4394163.
van Heijenoort J (2001). "Recent advances in the formation of the bacterial peptidoglycan monomer unit". Nat. Prod. Rep. 18: 503–19. doi:10.1039/a804532a. PMID 11699883.