Time-dependent inhibition of γ-aminobutyric acid aminotransferase, by 3-hydroxybenzylhydrazine

Eric S. Lightcap*, Mark Hans Hopkins, Gregory T. Olson, Richard B. Silverman

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


γ-Aminobutyric acid (GABA) aminotransferase is a pyridoxal 5′-phosphate (PLP)-dependent enzyme that catalyzes the conversion of GABA into succinic semialdehyde. Hydrazine analogues have long been known to act as inactivators of PLP-dependent enzymes, including GABA aminotransferase, however, no studies of the molecular mechanism of inactivation of PLP-dependent enzymes by hydrazines have been reported. 3-Hydroxybenzylhydrazine is shown to be a potent in vitro time-dependent inhibitor of pig brain GABA aminotransferase. UV-visible and 1H NMR studies, both with GABA aminotransferase and with PLP as a chemical model for the enzyme-catalyzed reaction, indicate that 3-hydroxybenzylhydrazine reacts both enzymatically and nonenzymatically to form the 3-hydroxybenzylhydrazone of PLP without tautomerization.

Original languageEnglish (US)
Pages (from-to)579-585
Number of pages7
JournalBioorganic and Medicinal Chemistry
Issue number5
StatePublished - May 1995

ASJC Scopus subject areas

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

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