Glutamate synthase (NADH) from lupin nodules. Specificity of the 2-oxoglutarate site.
The binding of substrate analogues including potential alternative substrates, to glutamate synthase (NADH) (L-glutamate: NAD+ oxidoreductase (transaminating) E.C. 1.4.1.14) has been investigated by studying competitive inhibition with respect ot 2-oxoglutarate. Binding requires two terminal carboxyl groups on a C5 straight chain molecule although some C4 molecules bind weakly. Bulky substituents at C2 decrease or prevent binding. Glutarate, the most potent inhibitor, binds much less tightly than the substrate. A 2-oxo group in a molecule other than the substrate does not appear to contribute significantly to binding. None of the analogues was able to act as an alternative substrate.
D005970:Glutamate Synthase / Q000378:metabolism*; D007656:Ketoglutaric Acids / Q000494:pharmacology; D007700:Kinetics; D009243:NAD; D010084:Oxidation-Reduction; D010944:Plants / Q000201:enzymology*; D013329:Structure-Activity Relationship; D000637:Transaminases / Q000378:metabolism*
D007656:Ketoglutaric Acids; D009243:NAD; D005970:Glutamate Synthase; D000637:Transaminases