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. 1975 May;72(5):1666–1670. doi: 10.1073/pnas.72.5.1666

Amino-acid sequence of bovine carboxypeptidase B.

K Titani, L H Ericsson, K A Walsh, H Neurath
PMCID: PMC432604  PMID: 1057162

Abstract

The amino-acid sequence of bovine carboxypeptidase B [peptidyl-L-lysine(-L-arginine)hydrolase, EC 3.4.12.3] has been determined using the heavy and light chains of the enzyme isolated from spontaneously activated pancreatic juice. Comparison of the sequence with that of carboxypeptidase A shows that the two enzymes are homologous (49% identity) and that all but one of the functional residues identified in carboxypeptidase A occur in corresponding loci in carboxypeptidase B (peptidyl-L-amino acid hydrolase, EC 3.4.12.2). The exception is the replacement of Ile-255 at the bottom of the substrate binding pocket of carboxypeptidase A, by aspartic acid in carboxypeptidase B. This single change can account for the difference in specificity of the two enzymes.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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