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.
In enzymology, a shikimate dehydrogenase (EC 1.1.1.25) is an enzyme that catalyzes the chemical reaction
In enzymology, a dTDP-4-dehydrorhamnose reductase (EC 1.1.1.133) is an enzyme that catalyzes the chemical reaction
In enzymology, a dTDP-6-deoxy-L-talose 4-dehydrogenase (EC 1.1.1.134) is an enzyme that catalyzes the chemical reaction
In enzymology, an UDP-N-acetylglucosamine 6-dehydrogenase (EC 1.1.1.136) is an enzyme that catalyzes the chemical reaction
In enzymology, an aspartate-semialdehyde dehydrogenase is an enzyme that is very important in the biosynthesis of amino acids in prokaryotes, fungi, and some higher plants. It forms an early branch point in the metabolic pathway forming lysine, methionine, leucine and isoleucine from aspartate. This pathway also produces diaminopimelate which plays an essential role in bacterial cell wall formation. There is particular interest in ASADH as disabling this enzyme proves fatal to the organism giving rise to the possibility of a new class of antibiotics, fungicides, and herbicides aimed at inhibiting it.
In enzymology, a saccharopine dehydrogenase (NADP+, L-glutamate-forming) (EC 1.5.1.10) is an enzyme that catalyzes the chemical reaction
In enzymology, a saccharopine dehydrogenase (NADP+, L-lysine-forming) (EC 1.5.1.8) is an enzyme that catalyzes the chemical reaction
In enzymology, an UDP-N-acetylglucosamine 2-epimerase is an enzyme that catalyzes the chemical reaction
In enzymology, an UDP-N-acetylglucosamine 4-epimerase is an enzyme that catalyzes the chemical reaction
In enzymology, an UDP-N-acetylglucosamine 1-carboxyvinyltransferase is an enzyme that catalyzes the first committed step in peptidoglycan biosynthesis of bacteria:
In enzymology, a dolichyl-phosphate alpha-N-acetylglucosaminyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a lactosylceramide 1,3-N-anning-beta-D-glrofelucosaminyltlolferase is an enzyme that catalyzes the chemical reaction
In enzymology, a lipopolysaccharide N-acetylglucosaminyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a N-acetyllactosaminide 3-alpha-galactosyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a phosphatidylinositol N-acetylglucosaminyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a protein N-acetylglucosaminyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, an UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase is an enzyme that catalyzes the chemical reaction
In enzymology, an UDP-N-acetylglucosamine—lysosomal-enzyme N-acetylglucosaminephosphotransferase is an enzyme that catalyzes the chemical reaction
In enzymology, an UDP-N-acetylglucosamine diphosphorylase is an enzyme that catalyzes the chemical reaction
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. PMID4717533.
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. PMID4394163.
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. PMID11699883.
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