Isolation and characterization of the product of inactivation of γ-aminobutyric acid aminotransferase by gabaculine

Mengmeng Fu, Richard B. Silverman*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

27 Scopus citations

Abstract

Gabaculine (5-amino-1,3-cyclohexadienylcarboxylic acid, 1Scheme 1), a naturally occurring neurotoxin isolated from Streptomyces toyocaenis, has been shown to be a mechanism-based inactivator of γ-aminobutyric acid aminotransferase (GABA-AT) (Rando, R. R. Biochemistry 1977, 16, 4604). Inactivation results from reaction of gabaculine with the pyridoxal 5'-phosphate (PLP) cofactor. Two HPLC systems for isolating this inactivator-PLP adduct are described as well as a detailed characterization of the adduct, including the ultraviolet-visible spectrum, electrospray mass spectra, and NMR spectrum. The same spectral characterization of the chemically synthesized gabaculine-PLP adduct is also reported. Copyright (C) 1999 Elsevier Science Ltd.

Original languageEnglish (US)
Pages (from-to)1581-1590
Number of pages10
JournalBioorganic and Medicinal Chemistry
Volume7
Issue number8
DOIs
StatePublished - Aug 1 1999

Keywords

  • Electrospray mass spectrometry
  • Gabaculine
  • Pyridoxal 5'-phosphate
  • γ-Aminobutyric acid aminotransferase

ASJC Scopus subject areas

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

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