ENTRY       EC 3.4.17.8
NAME        Muramoylpentapeptide carboxypeptidase
            D-Alanine carboxypeptidase I
CLASS       Hydrolases
            Acting on peptide bonds (peptidases)
            Metallocarboxypeptidases
REACTION    Cleavage of the bond: UDP-N-acetylmuramoyl-L-alanyl-D-gamma-
            -glutamyl-6-carboxy-L-lysyl-D-alanyl+D-alanine
SUBSTRATE   UDP-N-acetylmuramoyl-L-Ala-D-gamma-Glu-6-carboxy-L-Lys-(D-Ala)2
            H2O
PRODUCT     UDP-N-acetylmuramoyl-L-Ala-D-gamma-Glu-6-carboxy-L-Lys-D-Ala
            D-Alanine
INHIBITOR   Penicillin
            Cephalosporin
EFFECTOR    Divalent metal
COMMENT     A bacterial enzyme that requires a divalent cation for activity.
            Does not cleave the C-terminal D-alanine from the product of the
            above reaction, UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-
            -6-carboxy-L-lysyl-D-alanine. Competitively inhibited by
            penicillins and cephalosporins. Formerly EC 3.4.12.6.
PATHWAY     PATH: MAP00550  Peptideglycan biosynthesis
STRUCTURES  PDB: 0ZGP  1LBU  
DBLINKS     University of Geneva ENZYME DATA BANK: 3.4.17.8
            WIT (What Is There) Metabolic Reconstruction: 3.4.17.8
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