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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

Crystallization

Crystallization on EC 3.4.16.5 - carboxypeptidase C

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of mature cathepsin A is determined to 2.8 A resolution
crystal structures show that the structure of mature Cathepsin A is identical to the structure of the precursor and that activation depends solely on the removal/disorder transition of the activation domain. The active catalytic domain is held together by a strategically located disulfide bridge, linking the loose ends that are formed after removal/disorder transition of the activation domain
sitting drop vapour diffusion method with 0.2 M potassium thiocyanate and 20% PEG 3350
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carboxypeptidase Y inhibitor IC complexed with carboxypeptidase Y, hanging-drop vapour-diffusion method
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hanging-drop vapor diffusion method, crystal strcuture of the carboxypeptidase Y inhibitor Ic in complex with carboxypeptidase Y at 2.7 A resolution
significance of Thr60 and Met398 in hydrolysis and aminolysis reactions
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