Target type: molecularfunction
Catalysis of the reaction: UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine + undecaprenyl phosphate = UMP + N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine-diphosphoundecaprenol. [EC:2.7.8.13]
Phospho-N-acetylmuramoyl-pentapeptide-transferase activity is a crucial enzyme involved in the synthesis of peptidoglycan, a major component of bacterial cell walls. This activity catalyzes the transfer of a pentapeptide from a lipid-linked peptidoglycan precursor to the growing peptidoglycan chain. The process begins with the binding of UDP-N-acetylmuramyl-pentapeptide (UDP-MurNAc-pentapeptide) and undecaprenyl phosphate (C55-P), a lipid carrier, to the enzyme. The enzyme then catalyzes the transfer of the pentapeptide moiety from UDP-MurNAc-pentapeptide to C55-P, forming a lipid-linked pentapeptide. Subsequently, the enzyme facilitates the transfer of this lipid-linked pentapeptide to the growing peptidoglycan chain, extending the existing polymer. This enzymatic activity is essential for bacterial cell wall synthesis and consequently for bacterial survival. Inhibition of this activity by antibiotics, such as penicillin, disrupts cell wall formation and leads to bacterial cell death, making this a valuable therapeutic target.'
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Protein | Definition | Taxonomy |
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Phospho-N-acetylmuramoyl-pentapeptide-transferase | A phospho-N-acetylmuramoyl-pentapeptide-transferase that is encoded in the genome of Escherichia coli K-12. [PRO:DNx, UniProtKB:P0A6W3] | Escherichia coli K-12 |
Compound | Definition | Classes | Roles |
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phenylalanine arginine beta-naphthylamide | phenylalanine arginine beta-naphthylamide: a drug efflux pump inhibitor; structure in first source | peptide | |
capuramycin | capuramycin: from Streptomyces griseus 446-S3; structure given in first source |