PMID: 7028484Sep 1, 1981Paper

Kinetic studies of the reduction of succinic semialdehyde by rat-brain aldehyde reductase

European Journal of Biochemistry
A J Rivett, K F Tipton

Abstract

Initial rate studies have been used to investigate the kinetic mechanism followed by the purified high-Km (AR1) form of rat brain aldehyde reductase at pH 7.0. The effects of varying the aldehyde and NADPH concentrations, together with the inhibition given by the products of the reaction, are consistent with the reduction of succinic semialdehyde and p-nitrobenzaldehyde following an ordered reaction mechanism involving the formation of an intermediate ternary complex and in which NADPH is the first substrate to bind to the enzyme. Both these aldehyde substrates inhibit the enzyme at higher concentrations. This inhibition, which is uncompetitive with respect to NADPH, suggests that many previous studies on the specificity of this enzyme, that have been based on the activity determined at a single arbitrary concentration of each substrate, may have given erroneous results.

References

Oct 15, 1975·Biochemical Pharmacology·M M RisJ P Von Wartburg
Feb 1, 1979·The Biochemical Journal·W S Davidson, T G Flynn
Dec 1, 1979·Journal of Molecular Evolution·W S Davidson, T G Flynn
Dec 1, 1976·The Biochemical Journal·A J Turner, P E Hick
Oct 15, 1973·Biochemical Pharmacology·V G Erwin, R A Deitrich
Nov 1, 1974·The Biochemical Journal·A J TurnerK F Tipton
Apr 1, 1980·European Journal of Biochemistry·G Branlant, J F Biellmann
Feb 1, 1981·The Biochemical Journal·F F Morpeth, F M Dickinson
Apr 1, 1981·Biochemical Pharmacology·A J RivettK F Tipton
Jun 1, 1981·European Journal of Biochemistry·A J Rivett, K F Tipton
Aug 1, 1953·The Biochemical Journal·M DIXON

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Citations

Feb 1, 2011·Chemico-biological Interactions·Samar Alzeer, Elizabeth M Ellis
Mar 1, 1988·Archives of Biochemistry and Biophysics·A BhatnagarS K Srivastava

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