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Kinetic studies with rat-brain succinic-semialdehyde dehydrogenase.

Authors: Rivett, AJ  Tipton, KF 
Citation: Rivett AJ and Tipton KF, Eur J Biochem. 1981 Jun;117(1):187-93.
Pubmed: (View Article at PubMed) PMID:7262085

A simple procedure is described that gives an approximately 100-fold purification of rat brain succinic-semialdehyde dehydrogenase with a high yield. The enzyme exhibits a relatively low Km value for succinic semialdehyde (2.5 microM) and is inhibited by high concentrations of that substrate in an uncompetitive manner with respect to NAD+ (Ki = 150 microM). p-Hydroxybenzaldehyde was shown to give competitive inhibition with respect to succinic semialdehyde and uncompetitive inhibition with respect to NAD+. Initial rate studies in the presence of a fixed concentration of this inhibitor allowed a more accurate estimation of the kinetic parameters for the uninhibited reaction. The results of these studies, together with analysis of the dead-end inhibition by AMP and the effects of NAD+ and 3-acetylpyridine--adenine dinucleotide as alternative acceptors in the reaction, were consistent with the enzyme-catalysed reaction obeying a compulsory-order mechanism in which NAD+ was the first substrate to bind to the enzyme and NADH was the last product to dissociate from it.


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RGD Object Information
RGD ID: 1600512
Created: 2007-03-12
Species: All species
Last Modified: 2007-03-12
Status: ACTIVE


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