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• W2079012999 abstract "A method for the partial purification of d-3-phosphoglycerate dehydrogenase from wheat germ is reported. Substrate and coenzyme specificities have been investigated. Both the forward and reverse reactions catalyzed by the enzyme have been studied kinetically at pH 8.0 in the absence and presence of products, and the Michaelis, dissociation, and inhibition constants have been determined. The initial velocity patterns are consistent with a sequential mechanism, i.e., all substrates must add to the enzyme before any products are released. Although the results of the product-inhibition studies conform, in general, to an Ordered Bi Bi mechanism, i.e., substrates are bound only after prior binding of coenzymes, much of the kinetic data is not consistent with a strict interpretation of this mechanism. Studies on the feedback inhibition of this enzyme by l-serine are reported and demonstrate that serine only inhibits the activity in crude extracts of wheat germ but not that of the partially purified enzyme." @default.
• W2079012999 created "2016-06-24" @default.
• W2079012999 creator A5002434945 @default.
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• W2079012999 date "1970-03-01" @default.
• W2079012999 modified "2023-09-25" @default.
• W2079012999 title "Purification and properties of wheat germ d-3-phosphoglycerate dehydrogenase" @default.
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• W2079012999 doi "https://doi.org/10.1016/0003-9861(70)90414-5" @default.
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