ENTRY       EC 3.4.16.4
NAME        Serine-type D-Ala-D-Ala carboxypeptidase
            DD-Peptidase
            D-Alanyl-D-alanine carboxypeptidase
CLASS       Hydrolases
            Acting on peptide bonds (peptidases)
            Serine-type carboxypeptidases
REACTION    Preferential cleavage: (Ac)2-L-Lys-D-Ala+D-Ala. Also
            transpeptidation of peptidyl-alanyl moieties that are N-acyl
            substituents of D-alanine
SUBSTRATE   Peptide
            H2O
            (Ac)2-L-Lys-D-Ala-D-Ala
PRODUCT     D-Alanine
            Peptide
            (Ac)2-L-Lys-D-Ala
INHIBITOR   Penicillin
            beta-Lactam antibiotics
COMMENT     A membrane-bound, bacterial enzyme inhibited by penicillin and
            other beta-lactam antibiotics, which acylate the active site
            serine. Distinct from zinc D-Ala-D-Ala carboxypeptidase,
            EC 3.4.17.14.
GENES       ECO: b0632(dacA) b0839(dacC)
            HIN: HI0029(dacA) HI1330(dacB)
            BSU: dacA dacB dacF
            SYN: slr0646(dacB) slr0804(dacB) slr1924
STRUCTURES  PDB: 1CEF  1CEG  2PTE  3PTE  
DBLINKS     University of Geneva ENZYME DATA BANK: 3.4.16.4
            WIT (What Is There) Metabolic Reconstruction: 3.4.16.4
            SCOP (Structural Classificaion of Proteins): 3.4.16.4
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