Carboxypeptidase E
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.17 Metallocarboxypeptidases > 3.4.17.10 carboxypeptidase E
Carboxypeptidase E (carboxypeptidase H) is a zinc enzyme activated by Co2+, inhibited by 1,10-phenanthroline and other chelators, pH optimum 5.6, located in secretory-cell storage granules and active in processing of protein hormones and bioactive peptides, in peptidase family M14; it releases C-terminal arginine or lysine residues from polypeptides. By removing C-terminal basic residues from prohormones it generates bioactive peptide hormones. It appears in viruses and cellular organisms.
Carboxypeptidase E (carboxypeptidase H) is a zinc enzyme activated by Co2+, inhibited by 1,10-phenanthroline and other chelators, pH optimum 5.6, located in secretory-cell storage granules and active in processing of protein hormones and bioactive peptides, in peptidase family M14; it releases C-terminal arginine or lysine residues from polypeptides. By removing C-terminal basic residues from prohormones it generates bioactive peptide hormones. It appears in viruses and cellular organisms.
References:
Biomedical Dictionary
The Biomedical Dictionary is a comprehensive and professional collection of biological academic terms and subject datas. All explanations are supported by authoritative books or high impact factor literatures, and you can acquire accurate explanations of the biomedical terms you want to know.
Molarity Calculator
Dilution Calculator
