Title of article
Isolation and characterization of the product of inactivation of γ-aminobutyric acid aminotransferase by gabaculine Original Research Article
Author/Authors
Mengmeng Fu، نويسنده , , Richard B. Silverman، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 1999
Pages
10
From page
1581
To page
1590
Abstract
Gabaculine (5-amino-1,3-cyclohexadienylcarboxylic acid, ), 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.
Keywords
?-Aminobutyric acid aminotransferase , gabaculine , pyridoxal 5?-phosphate , Electrospray mass spectrometry
Journal title
Bioorganic and Medicinal Chemistry
Serial Year
1999
Journal title
Bioorganic and Medicinal Chemistry
Record number
1302365
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