Structural evolution of an enzyme specificity. The structure of rat carboxypeptidase A2 at 1.9-A resolution

Faming, Z., Kobe, B., Stewart, C. B., Rutter, W. J. and Goldsmith, E. J. (1991) Structural evolution of an enzyme specificity. The structure of rat carboxypeptidase A2 at 1.9-A resolution. The Journal of Biological Chemistry, 266 36: 24606-24612.

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Author Faming, Z.
Kobe, B.
Stewart, C. B.
Rutter, W. J.
Goldsmith, E. J.
Title Structural evolution of an enzyme specificity. The structure of rat carboxypeptidase A2 at 1.9-A resolution
Journal name The Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
1083-351X
Publication date 1991-12-25
Sub-type Article (original research)
Open Access Status File (Publisher version)
Volume 266
Issue 36
Start page 24606
End page 24612
Total pages 7
Place of publication Bethesda, MD, USA
Publisher American Society for Biochemistry and Molecular Biology
Language eng
Subject 060112 Structural Biology (incl. Macromolecular Modelling)
Abstract The structure of rat carboxypeptidase A2 (CPA2), which has a unique specificity for tryptophan-containing COOH-terminal peptides, has been determined in an unliganded state at 1.9-A resolution and refined to a crystallographic R-factor of 18.3%. Comparison of the structure of CPA2 with that of bovine carboxypeptidase A (referred to here as CPA1) reveals that the specificity of the former for larger amino acids probably arises from two amino acid replacements within the binding cavity (Thr268----Ala and Leu203----Met), coupled with differences in the positions of conserved residues in a surface loop on one face of the specificity pocket. The position of the reactive-site surface loop may be affected also by a disulfide bridge between Cys210 and Cys244. In this unliganded form of the enzyme, Tyr248 takes up a position interior to the specificity pocket and is distinct from that observed in bovine CPA1. The structural differences between CPA1 and CPA2 correlate strongly with crystallographically determined temperature factors and thus appear to be largest where the enzyme is flexible.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
 
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