Kinetics of the carboxypeptidase A-catalyzed hydrolysis of α-(benzoylamino)cinnamoyl derivatives of various amino acids

Junghun Suh, Minhaeng Cho

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Kinetics of the carboxypeptidase A-catalyzed hydrolysis of α-(benzoylamino)cinnamoyl derivatives of various amino acids were measured. The C-terminal amino acid residue of the amide substrates were phenylalanine (Phe), p-substituted phenylalanines (p-OH, p-NO2, p-Cl, p-I, p-CH3p-C2H5, and p-CH(CH3)2), tryptophan (Trp), and phenylglycine(phenylGly). Introduction of the p-OH, p-Cl, p-NO2, or p-CH3 group to the leaving Phe did not lead to considerable changes in the reactivity, while that of the p-I or p-C2H5 group decreased the reactivity remarkably and that of the p-CH(CH3)2 group abolished the reactivity. Substitution of Trp for the leaving Phe did not alter the reactivity appreciably, whereas that of phenylGly for the leaving Phe reduced the reactivity to a large degree. The seemingly scattered pattern of the structure-reactivity relationship was explained by assuming that the hydrophobic pocket in the active site of the enzyme has limited height, which is comparable to the thickness of the benzene ring.

Original languageEnglish
Pages (from-to)276-282
Number of pages7
JournalBioorganic Chemistry
Volume18
Issue number3
DOIs
Publication statusPublished - 1990 Sep
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Drug Discovery
  • Organic Chemistry

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