The function of S1′ subsite pocket of carboxypeptidase A

Dong H. Kim, Kyung Bo Kim

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


Our study on the mechanism involved in the substrate recognition of Carboxypeptidase A using transition state analog inhibitors indicated that, on the contrary to the general believe, there is no hydrophobic interaction involved. The bulky hydrophonic moiety entered the narrow opening of the subsite pocket is held by Tyr-248 which moved from the enzyme surface until the catalytic action is over. In the binding of a ligand to Carboxypeptidase A, no hydrophobic interactions appear to be involved between the S1 ′ subsite and the side chain of the C-terminal amino acid of the ligand. Rather the side chain is held inside the pocket physically by the aromatic ring of Tyr-248.

Original languageEnglish
Pages (from-to)323-326
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Issue number6
StatePublished - 1991

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry


Dive into the research topics of 'The function of S1′ subsite pocket of carboxypeptidase A'. Together they form a unique fingerprint.

Cite this