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  2. Carboxypeptidase - Wikipedia

    en.wikipedia.org/wiki/Carboxypeptidase

    Some, but not all, carboxypeptidases are initially produced in an inactive form; this precursor form is referred to as a procarboxypeptidase. In the case of pancreatic carboxypeptidase A, the inactive zymogen form - pro-carboxypeptidase A - is converted to its active form - carboxypeptidase A - by the enzyme trypsin. This mechanism ensures that ...

  3. Carboxypeptidase A2 - Wikipedia

    en.wikipedia.org/wiki/Carboxypeptidase_A2

    Carboxypeptidase A2 is an enzyme that in humans is encoded by the CPA2 gene. [5] [6] [7]Three different forms of human pancreatic procarboxypeptidase A have been isolated. The A1 and A2 forms are monomeric proteins with different biochemical properties.

  4. Carboxypeptidase B2 - Wikipedia

    en.wikipedia.org/wiki/Carboxypeptidase_B2

    1361 56373 Ensembl ENSG00000080618 ENSMUSG00000021999 UniProt Q96IY4 Q9JHH6 RefSeq (mRNA) NM_016413 NM_001278541 NM_001872 NM_019775 RefSeq (protein) NP_001265470 NP_001863 NP_062749 Location (UCSC) Chr 13: 46.05 – 46.11 Mb Chr 14: 75.48 – 75.52 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Carboxypeptidase B2 (CPB2), also known as carboxypeptidase U (CPU), plasma ...

  5. Carboxypeptidase A - Wikipedia

    en.wikipedia.org/wiki/Carboxypeptidase_A

    CPA-1 and CPA-2 (and, it is presumed, all other CPAs) employ a zinc ion within the protein for hydrolysis of the peptide bond at the C-terminal end of an amino acid residue.

  6. CPA3 - Wikipedia

    en.wikipedia.org/wiki/CPA3

    CPA3 has a pH optimum in the neutral to basic range. CPA3 functions together with endopeptidases secreted from mast cells such as chymases and tryptases to degrade proteins and peptides, including the apolipoprotein B component of LDL particles and angiotensin I. [9] [10] Upon mast cell activation and degranulation, CPA3, the chymases, and tryptases are released in complexes with heparin ...

  7. Robert Huber - Wikipedia

    en.wikipedia.org/wiki/Robert_Huber

    Outstanding structures are those of procarboxypeptidase, which led to the discovery of the remarkable activation mechanism of this enzyme, and of the complex of thrombin with hirudin, which showed the molecular mechanism of inhibition of blood clotting by this leech toxin.

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  9. Carboxypeptidase U - Wikipedia

    en.wikipedia.org/wiki/Carboxypeptidase_U

    Carboxypeptidase U (EC 3.4.17.20, arginine carboxypeptidase, carboxypeptidase R, plasma carboxypeptidase B, thrombin-activatable fibrinolysis inhibitor) is an enzyme ...