| UDP-N-acetylmuramate dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 UDP-N-acetylenolpyruvoylglucosamine reductase homodimer, Mycobacterium tuberculosis | |||||||||
| Identifiers | |||||||||
| EC no. | 1.3.1.98 | ||||||||
| CAS no. | 39307-28-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, an UDP-N-acetylmuramate dehydrogenase (EC 1.3.1.98) is an enzyme that catalyzes the chemical reaction
- UDP-N-acetyl-alpha-D-muramate + NADP+ UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH + H+
Thus, the two substrates of this enzyme are UDP-N-acetyl-alpha-D-muramate and NADP+, whereas its 3 products are UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is UDP-N-acetyl-alpha-D-muramate: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-lactylglucose:NADP-oxidoreductase. This enzyme participates in aminosugars metabolism. It employs one cofactor, FAD.
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.
References
- 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 (14): 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 (19): 5012–6. PMID 4394163.
- van Heijenoort J (2001). "Recent advances in the formation of the bacterial peptidoglycan monomer unit". Nat. Prod. Rep. 18 (5): 503–19. doi:10.1039/a804532a. PMID 11699883.