UDP-N-acetylmuramate dehydrogenase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: UDP-N-acetylmuramate + NADP+ = UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + NADPH + H+. [EC:1.3.1.98]

UDP-N-acetylmuramate dehydrogenase activity is a crucial enzyme involved in the biosynthesis of peptidoglycan, a major component of bacterial cell walls. This enzyme catalyzes the NADPH-dependent oxidation of UDP-N-acetylmuramate (UDP-MurNAc) to UDP-N-acetylmuramic acid 6-phosphate (UDP-MurNAc-6-P). This reaction is essential for the formation of the precursor molecule that is incorporated into peptidoglycan. The enzyme utilizes NADPH as a reducing agent, transferring electrons from NADPH to the substrate, UDP-MurNAc. This transfer of electrons results in the oxidation of UDP-MurNAc to UDP-MurNAc-6-P, which is subsequently used in the next step of peptidoglycan synthesis. This enzymatic activity is highly specific for UDP-MurNAc, ensuring that the correct substrate is used in the biosynthetic pathway. The precise mechanism of the reaction involves the formation of an enzyme-substrate complex, followed by the transfer of electrons from NADPH to UDP-MurNAc. The enzyme's active site contains residues that are essential for binding both the substrate and the cofactor, NADPH. This catalytic activity is crucial for bacterial cell wall formation, which is essential for bacterial survival and growth. Thus, UDP-N-acetylmuramate dehydrogenase activity is a critical target for antibacterial drug development, as inhibitors of this enzyme can effectively block bacterial cell wall synthesis and lead to bacterial death.'
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Proteins (1)

Compounds (1)