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[Theoretical conformational analysis of noinvalent carboxypeptidase A complexes with inhibitors and substrates].

Authors
  • Lipkind, G M
  • Paslen, V V
Type
Published Article
Journal
Molekuliarnaia biologiia
Publication Date
Jan 01, 1980
Volume
14
Issue
5
Pages
1142–1150
Identifiers
PMID: 7421820
Source
Medline
License
Unknown

Abstract

Semi-empirical calculations of conformational properties of acetyl-L-tyrosine, glycyl-L-tyrosine, acetyl-L-alanyl-L-tyrosine and acetyl-L-alanyl-L-alanyl-tyrosine and their noncovalent complexes with carboxypeptidase A (CPA) are presented. Each of these molecules binds in the active site of CPA by only one binding mode. The substrates are practically free of intramolecular tension. It is shown that the binding of an aromatic side chain of a C-terminal residue of substrate provides productive orientation of the susceptible peptide bond. The sterochemical aspects of the interactions of Tyr-248 and Glu-270 residues with the substrates are considered.

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