Characterization of the different spectral forms of glutamate 1-semialdehyde aminotransferase by mass spectrometry

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From: Biochemistry(Vol. 34, Issue 49)
Publisher: American Chemical Society
Document Type: Article
Length: 74 words

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Abstract :

The 338 nm absorption maximum in glutamate 1-semialdehyde aminotransferase is associated with pyridoxamine phosphate, while absorption at 418 nm is due to pyroxidal phosphate bound by a Schiff base to Lys. These were the findings when yellow, colorless and pink forms of the native enzyme from Synechococcus were obtained by treatment with 4,5-dioxovalerate, 4,5-diaminovalerate and acetylenic gamma-aminobutyric acid (GABA). A likely mechanism for the covalent binding of acetylenic GABA to the protein is proposed.

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Gale Document Number: GALE|A18087736