Substituted 4-aminobutanoic acids. Substrates for gamma-aminobutyric acid alpha-ketoglutaric acid aminotransferase.

R. B. Silverman*, M. A. Levy

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

41 Scopus citations

Abstract

Substituted 4-aminobutanoic acids were studied as potential irreversible inactivators of purified pig brain gamma-aminobutyric acid aminotransferase, the enzyme responsible for the degradation of the inhibitory neurotransmitter, gamma-aminobutyric acid. It was found that unlike the related 4-amino-5-halopentanoic acids (Silverman, R. B., and Levy, M. A. (1981) Biochemistry 20, 1197), the 4-amino-3-halobutanoic acids were substrates for this enzyme, undergoing exclusive elimination to succinic semialdehyde and producing no inactivation. The hydroxy analogue, however, underwent exclusive transamination and no succinic semialdehyde was detected. These results are discussed in terms of the nature of the substituents, the structure of the active site of gamma-aminobutyric acid aminotransferase, and the design of mechanism-based inactivators.

Original languageEnglish (US)
Pages (from-to)11565-11568
Number of pages4
JournalJournal of Biological Chemistry
Volume256
Issue number22
StatePublished - Nov 25 1981

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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