Irreversible inactivation of pig brain γ-aminobutyric acid-α-ketoglutarate transaminase by 4-amino-5-halopentanoic acids

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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

38 Scopus citations

Abstract

γ-Aminobutyric acid-α-ketoglutarate transaminase from pig brain is irreversibly inactivated by 4-amino-5-halopentanoic acids. Protection from inactivation by the natural substrates, the pH dependence of inactivation and the incorporation of 1.7 moles of radioactive inhibitor per mole of enzyme from (S)-[U-14C]-4-amino-5-chloropentanoic acid suggest a covalent adduct at the active site of the enzyme. A mechanism-based inactivation is proposed.

Original languageEnglish (US)
Pages (from-to)250-255
Number of pages6
JournalTopics in Catalysis
Volume95
Issue number1
DOIs
StatePublished - 1980

Keywords

  • GABA
  • GABA-T
  • GAD
  • NADP
  • NADP
  • PLP
  • Pyr in Scheme 1 represents the substituted pyridine nucleus in PLP
  • SSADH
  • glutamate decarboxylase E.C. 4.1.1.14
  • nicotinamide adenosine triphosphate
  • oxidoreductase E.C. 1.2.1.16
  • pyridoxal phosphate
  • succinic semialdehyde
  • α-KG
  • α-ketoglutaric acid
  • γ-aminobutyric acid
  • γ-aminobutyric acid-α-ketoglutarate transaminase E.C. 2.6.1.19

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Biophysics
  • Molecular Biology

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