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UDP-N-acetylmuramate dehydrogenase

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

UDP-N-acetyl-alpha-D-muramate + NADP<sup>+</sup> UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH + H<sup>+</sup>

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

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD<sup>+</sup> or NADP<sup>+</sup> as acceptor. The systematic name of this enzyme class is UDP-N-acetyl-alpha-D-muramate:NADP<sup>+</sup> 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, . 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 , , , , , , , and .

References