UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine + di-trans,poly-cis-undecaprenyl phosphate = UMP + N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol. [EC:2.7.8.13, MetaCyc:PHOSNACMURPENTATRANS-RXN]

UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity is a key enzyme in the biosynthesis of peptidoglycan, the primary component of bacterial cell walls. It catalyzes the transfer of the pentapeptide-linked UDP-N-acetylmuramic acid (UDP-MurNAc-pentapeptide) from a soluble donor molecule to the lipid carrier undecaprenyl phosphate (undecaprenyl-P). This reaction results in the formation of a lipid-linked precursor, UDP-MurNAc-pentapeptide-undecaprenyl-P, which is essential for the subsequent steps in peptidoglycan biosynthesis. The transferase activity is highly specific for both the pentapeptide-linked UDP-MurNAc and the lipid carrier undecaprenyl-P. The active site of the enzyme likely contains specific binding sites for both substrates, ensuring precise recognition and transfer of the pentapeptide moiety. This transferase activity is crucial for maintaining bacterial cell wall integrity and is therefore a target for antibiotic development. Inhibition of this enzyme can lead to disruption of peptidoglycan synthesis, ultimately leading to cell lysis and bacterial death.'
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Proteins (1)

Compounds (2)