Glutamate 1-semialdehyde aminotransferase: anomalous enantiomeric reaction and enzyme mechanism

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Date: Nov. 17, 1992
From: Biochemistry(Vol. 31, Issue 45)
Publisher: American Chemical Society
Document Type: Article
Length: 80 words

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Abstract :

The enantiomeric reaction of glutamate 1-semialdehyde aminotransferase (GSA-AT) with the (R) enantiomer of GSA was investigated. Addition of (R,S)-GSA to the aminotransferase resulted in the transformation of the enzyme into pyridoxal-P or internal aldimine form instead of the original pyridoxamine-P. Treatment with (R,S)-4, 5-diaminovalerate (DAVA) remove this effect on the enzyme by GSA and promotes initial rates of 5-aminolevulinate. The results suggested an anomalous reactivity of (R)-GSA towards GSA-AT and a rate-limiting activity of DAVA for the anomalous enantiomeric reaction.

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Gale Document Number: GALE|A14258094