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Biochim Biophys Acta. 1990 Dec 5;1041(3):305-10.

Analysis of the kinetic mechanism of halophilic NADP-dependent glutamate dehydrogenase.

Author information

  • 1Division de BioquĂ­mica, Facultad de Ciencias, Universidad de Alicante, Spain.

Abstract

The amination of 2-oxoglutarate catalyzed by NADP-specific glutamate dehydrogenase (EC 1.4.1.4, L-glutamate:NADP+ oxidoreductase (deaminating)) from Halobacterium halobium has been analyzed by initial rate, graphical analysis, and product and competitive inhibition studies. Initial rate and graphical analysis reveal that a B term (representing 2-oxoglutarate) is not statistically necessary for an initial rate equation. However, the absence of a B term does not distinguish between ordered and random binding of NADPH and ammonia. The patterns of product inhibition by NADP+ and L-glutamate, and competitive inhibition by hydroxylamine and succinate permit deduction of the kinetic mechanism as ordered, with NADPH, 2-oxoglutarate and ammonia added in that order, and L-glutamate release preceding NADP+ release.

PMID:
1980084
[PubMed - indexed for MEDLINE]
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