ENTRY       EC 3.4.16.1
NAME        Serine-type carboxypepetidase
            S1
            S2
            P
            Carboxypeptidase Y
            Yeast protease C
            Carboxypeptidase C
            Serine carboxypeptidase II
            Phaseolin
            Cathepsin A
CLASS       Hydrolases
            Acting on peptide bonds (peptidases)
            Serine-type carboxypeptidases
REACTION    Release of a C-terminal amino acid with broad specificity
SUBSTRATE   Peptide
            H2O
PRODUCT     Peptide
            Amino acid
INHIBITOR   Diisopropyl fluorophosphate
            Thiol-blocking reagent
COMMENT     Carboxypeptidase of broad specificity with optimum pH 4.5-6.0,
            inhibited by diisopropyl fluorophosphate, and sensitive to thiol-
            -blocking reagents. Sources include microorganisms: Penicillium
            (S1, S2, P), yeast (carboxypeptidase Y, yeast protease C,
            carboxypeptidase C), Aspergillus; higher plants: citrus
            (carboxypeptidase C), germinating barley, germinating wheat
            (serine carboxypeptidase II), germinating cotton, beans
            (phaseolin); higher animals: lysosomal carboxypeptidase A
            (cathepsin A). Not identical with serine-type endopeptidases.
            Formerly EC 3.4.12.1 and 3.4.21.13. This enzyme is probably also
            identical to lysosomal tyrosine carboxypeptidase, formerly EC
            3.4.16.3.
STRUCTURES  PDB: 1WHS  1WHT  3SC2  
DBLINKS     University of Geneva ENZYME DATA BANK: 3.4.16.1
            WIT (What Is There) Metabolic Reconstruction: 3.4.16.1
            SCOP (Structural Classificaion of Proteins): 3.4.16.1
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