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3.4.16.2: lysosomal Pro-Xaa carboxypeptidase

This is an abbreviated version!
For detailed information about lysosomal Pro-Xaa carboxypeptidase, go to the full flat file.

Word Map on EC 3.4.16.2

Reaction

Cleavage of a -Pro-/-Xaa bond to release a C-terminal amino acid =

Synonyms

aminoacylproline carboxypeptidase, angiotensinase C, carboxypeptidase, carboxypeptidase A6, Carboxypeptidase P, Carboxypeptidase R, carboxypeptidase, aminoacylproline, carboxypeptidase, peptidylprolylamino acid, CPA6, CPP, EC 3.4.12.4, endothelial cell prekallikrein activator, HUVEC PK activator, lysosomal carboxypeptidase, lysosomal carboxypeptidase C, lysosomal Pro-X carboxypeptidase, matrix PK activator, PCP, PKA, plasma carboxypeptidase, plasma procarboxypeptidase B, PRCP, procarboxypeptidase U, proline carboxypeptidase, proline-specific carboxypeptidase P, prolyl carboxypeptidase, prolyl-carboxypeptidase, prolylcarboxypeptidase, serine protease prolylcarboxypeptidase, TAFI, thrombin-activatable fibrinolysis inhibitor

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.16 Serine-type carboxypeptidases
                3.4.16.2 lysosomal Pro-Xaa carboxypeptidase

Crystallization

Crystallization on EC 3.4.16.2 - lysosomal Pro-Xaa carboxypeptidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization of glycosylated human PrCP from stably transformed CHO cells is described. Purified PrCP yields crystals belonging to space group R32, with unit-cell parameters a = b = 181.14, c = 240.13 A, that diffract to better than 2.8 A resolution