Pyruvate Dehydrogenase, Substrate Specificity and Product Inhibition
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چکیده
منابع مشابه
Substrate specificity of the pyruvate dehydrogenase complex from Escherichia coli.
The investigation of the substrate specificity of the pyruvate dehydrogenase complex from Escherichia coli allows a description of the binding region of pyruvate. Substrate analogs with electronegative substitutions in the methyl group show a strong competitive inhibition of the overall reaction of the pyruvate dehydrogenase complex. The most efficient inhibitor is fluoropyruvate which has a mo...
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Pyruvate has been shown to both stimulate and inhibit kidney pyruvate dehydrogenase, (PDH,) kinase activity. The present study investigates the inhibitory effect of pyruvate under conditions in which the stimulatory effect is invariant. Inhibition of PDH, kinase activity by dichloroacetate, a pyruvate analog, is also characterized. Both pyruvate and dichloroacetate are uncompetitive, hyperbolic...
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The mechanism for the inhibition of pyruvate dehydrogenase complex from bovine heart by moniliformin was investigated. Thiamin pyrophosphate proved to be necessary for the inhibitory action of moniliformin. The inhibition reaction was shown to be time-dependent and to follow first-order and saturation kinetics. Pyruvate protected the pyruvate dehydrogenase complex against moniliformin inactivat...
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In the direction of reductive condensation of alpha-ketoglutarate and lysine, saccharopine dehydrogenase (N6-(glutar-2-yl)-L-lysine:NAD oxidoreductase (lysine-forming) is inhibited by high concentrations of alpha-ketoglutarate and lysine, but not by NADH. NAD+ and saccharopine show no substrate inhibition in the reverse direction. Substrate inhibition by alpha-ketoglutarate and lysine is linear...
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Kinetic studies of the cleavage of dehydroepiandrosterone-sulfate (i) and androstenediol-3-sulfate by a particulate enzyme preparation from a rat testicular microsomal fraction gave K m values of 2.04 x 10-6M for DHA-S and 0.935 x 10-6M for androstenediol-3-sulfate with identical Vma x values° Inhibition studies with equimolar concentrations of substrate and inhibitor demonstrated that 5~-andro...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1969
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1969.tb00559.x