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Carboxypeptidase A (CPA) contains a zinc (Zn 2+) metal center in a tetrahedral geometry with amino acid residues in close proximity around zinc to facilitate catalysis and binding. Out of the 307 amino acids bonded in a peptide chain, the following amino acid residues are important for catalysis and binding; Glu-270, Arg-71, Arg-127, Asn-144 ...
A carboxypeptidase (EC number 3.4.16 - 3.4.18) is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide. This is in contrast to an aminopeptidases , which cleave peptide bonds at the N-terminus of proteins.
71791 Ensembl n/a ENSMUSG00000039070 UniProt Q9UI42 Q6P8K8 RefSeq (mRNA) NM_016352 NM_001163446 NM_027926 RefSeq (protein) NP_001156918 NP_057436 NP_082202 Location (UCSC) n/a Chr 6: 30.57 – 30.59 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Carboxypeptidase A4 is an enzyme that in humans is encoded by the CPA4 gene. This gene is a member of the carboxypeptidase A/B subfamily ...
Their findings established that L-benzylsuccinic acid is bound at a single locus at the active site of carboxypeptidase A. The authors discussed but dismissed the suggestion that the carboxylate function might bind to the catalytically functional zinc ion present at the active site. Later however this was found to be the case.
Carboxypeptidase A1 is an enzyme that in humans is encoded by the CPA1 gene. [5] Three different forms of human pancreatic procarboxypeptidase A have been isolated. The A1 and A2 forms are monomeric proteins with different biochemical properties. Carboxypeptidase A1 is a monomeric pancreatic exopeptidase. It is involved in zymogen inhibition. [5]
In carboxypeptidase A, the active site is accessible to large substrates like the bulky C-terminal residue of polypeptides, whereas the C-domain sterically hinders access to the active site in aspartoacylase. Instead, the N-domain and C-domain of aspartoacylase form a deep narrow channel that leads to the active site.
AE binding protein 1 is a member of carboxypeptidase A protein family. The protein may function as a transcriptional repressor and play a role in adipogenesis and smooth muscle cell differentiation. Studies in mice suggest that the AEBP1 gene that encodes the protein functions in wound healing and abdominal wall development.
The structure of the complex between bovine carboxypeptidase A and the 39-amino-acid carboxypeptidase A inhibitor from potatoes has been determined at 2.5-Angstrom resolution. [ 3 ] The potato inhibitor is synthesised as a precursor, having a 29 amino acid N-terminal signal peptide, a 27 amino acid pro-peptide, the 39 amino acid mature ...