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3.4.16.5: carboxypeptidase C

This is an abbreviated version!
For detailed information about carboxypeptidase C, go to the full flat file.

Word Map on EC 3.4.16.5

Reaction

release of a C-terminal amino acid with broad specificity =

Synonyms

A-type metallocarboxypeptidase, acidic serine carboxypeptidase, AtCPY, BRS1, carboxypeptidase a, carboxypeptidase A4, carboxypeptidase C, Carboxypeptidase II, carboxypeptidase Y, carboxypeptidase YSCY, carboxypeptidase-Y, Case, CatA, CathA, cathepsin A, CaY, CP-MI, CP-MIII, CP-WIII, CPA4, CPase, CPC, CPD-Y, CPW, CPY, Cpy1p, CTSA, Cxp1, deamidase, EC 3.4.12.1, EC 3.4.16.1, EC 3.4.16.3, hCath A, HPP, lysosomal carboxypeptidase A, lysosomal protective protein, MO54, More, MpiCP-1, MpiCP-2, Phaseolin, PpcA, PRC1, proCPY, protective protein cathepsin A, protective protein/cathepsin A, retinoid-inducible serine carboxypeptidase, SCP, Scpep1, Ser carboxypeptidase, Ser carboxypeptidase-like protein, serine carboxypeptidase, serine carboxypeptidase 1, serine carboxypeptidase I, serine carboxypeptidase Scpep1, SmSCP-1, TcCBP

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.16 Serine-type carboxypeptidases
                3.4.16.5 carboxypeptidase C

pH Range

pH Range on EC 3.4.16.5 - carboxypeptidase C

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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 6
Citrus sp.
-
pH 4.5: about 70% of activity maximum, pH 6: about 55% of activity maximum
5 - 6
-
pH 5.0: about 40% of maximal activity, pH 6.0: about 40% of maximal activity, hydrolysis of furyacryloyl-Phe-Ala
5 - 7
-
pH 5.0: about 45% of maximal activity, pH 7.0: about 50% of maximal activity, hydrolysis of hippuryl-L-beta-phenyllactate
5 - 9
-
pH 5.0: about 45% of maximal activity, pH 9.0: about 75% of maximal activity, hydrolysis of acetyl-Phe ethyl ester
5.5 - 8
-
pH 5.5: about 50% of maximal activity, pH 8.0: about 35% of maximal activity, hydrolysis of benzoyl-Tyr-4-nitroanilide
5.5 - 8.5
-
pH 5.5: about 50% of maximal activity, pH 8.0: about 60% of maximal activity, hydrolysis of benzyloxycarbonyl-Phe-NH2