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Glutamate dehydrogenase substrate inhibition

The formation of abortive complexes of the type EAQ and EPB, a common cause of substrate inhibition of dehydrogenases (Section II, F), can also be detected in isotope exchange experiments by inhibition of all exchanges when the concentrations of A and Q or P and B are increased together. The complexes E NADH malate (34) and E NAD(P)H glutamate (44), for example, were detected in this way, and are probably responsible for the substrate inhibition observed in initial rate studies of these enzymes (Section II,F,1). The latter complex, but not the former. [Pg.17]

Substrate inhibition of bovine liver glutamate dehydrogenase has not been studied in such detail. It is most marked when the NAD(P) concentration is also large (11), and is relieved by ADP. This appears to be the reason why ADP activates the enzyme when large glutamate and... [Pg.27]

See other pages where Glutamate dehydrogenase substrate inhibition is mentioned: [Pg.493]    [Pg.25]    [Pg.30]    [Pg.35]    [Pg.120]    [Pg.448]    [Pg.343]    [Pg.372]    [Pg.151]    [Pg.65]    [Pg.73]    [Pg.519]    [Pg.327]    [Pg.142]    [Pg.144]    [Pg.527]    [Pg.299]    [Pg.187]    [Pg.192]    [Pg.2694]    [Pg.5608]    [Pg.80]    [Pg.223]    [Pg.315]    [Pg.19]    [Pg.345]   
See also in sourсe #XX -- [ Pg.27 ]



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Dehydrogenases glutamate dehydrogenase

Dehydrogenases substrate

Dehydrogenases substrate inhibition

Glutamate dehydrogenase

Inhibition dehydrogenase

Substrate inhibition

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