Catalytic inhibition of γ-aminobutyric acid-α-ketoglutarate transaminase of bacterial origin by 4-aminohex-5-ynoic acid, a substrate analog
γ-Aminobutyric acid-α-ketoglutarate transaminase from Pseudomonas fluorescens is irreversibly inhibited by 4-aminohex-5-yhoic acid, a new structural analog of GABA. The fact that this inhibition requires the pyridoxal form of the holoenzyme, and the formation of a Michaelis complex is in support of...
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Veröffentlicht in: | Biochemical and biophysical research communications 1975-11, Vol.67 (1), p.301-306 |
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Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
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Online-Zugang: | Volltext |
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Zusammenfassung: | γ-Aminobutyric acid-α-ketoglutarate transaminase from
Pseudomonas fluorescens
is irreversibly inhibited by 4-aminohex-5-yhoic acid, a new structural analog of GABA. The fact that this inhibition requires the pyridoxal form of the holoenzyme, and the formation of a Michaelis complex is in support of a catalytic mechanism. The compound is also active
in vitro
and
in vivo
on the same enzyme from mammalian brain. |
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ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/0006-291X(75)90316-2 |