UDP-N-acetylmuramate dehydrogenase

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
Search PMC articles PubMed articles NCBI proteins

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^+ ${\displaystyle \rightleftharpoons }$ 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. doi:10.1016/S0021-9258(19)43659-4. 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. doi:10.1016/S0021-9258(18)62810-8. 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.