Title : Carboxypeptidase O is a glycosylphosphatidylinositol-anchored intestinal peptidase with acidic amino acid specificity.

Pub. Date : 2011 Nov 11

PMID : 21921028






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 CPO was purified by affinity chromatography, and the purified enzyme was able to cleave proteins and synthetic peptides with greatest activity toward acidic C-terminal amino acids unlike other CPA-like enzymes. Peptides carboxypeptidase O Homo sapiens
2 CPO displayed a neutral pH optimum and was inhibited by common metallocarboxypeptidase inhibitors as well as citrate. Citric Acid carboxypeptidase O Homo sapiens
3 CPO was modified by attachment of a glycosylphosphatidylinositol membrane anchor to the C terminus of the protein. Glycosylphosphatidylinositols carboxypeptidase O Homo sapiens
4 These results suggest that CPO cleaves acidic amino acids from dietary proteins and peptides, thus complementing the actions of well known digestive carboxypeptidases CPA and CPB. Acids carboxypeptidase O Homo sapiens
5 These results suggest that CPO cleaves acidic amino acids from dietary proteins and peptides, thus complementing the actions of well known digestive carboxypeptidases CPA and CPB. cpb carboxypeptidase O Homo sapiens