Purification and properties of rat brain succinic semialdehyde dehydrogenase.
Succinic semialdehyde dehydrogenase from rat brain has been purified to electrophoretic homogeneity. It has a molecular weight of about 140, 000 and is composed of two apparently identical subunits. The reaction catalized by the pure protein is entirely dependent on endogenous --SH groups. The Kim (limits) for NAD and succinic semialdehyde are 2 X 10(-5) M and 1 X 10(-4) M respectively at the optimum pH of 8.6. Inhibition studies show that the reaction mechanism is a compulsory ordered on where NAD binds first followed by succinic semialdehyde.
D000445:Aldehyde Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism; D000447:Aldehydes / Q000494:pharmacology; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001921:Brain / Q000201:enzymology*; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D046911:Macromolecular Substances; D008433:Mathematics; D008623:Mercaptoethanol / Q000494:pharmacology; D008970:Molecular Weight; D051381:Rats; D013329:Structure-Activity Relationship; D013386:Succinates
D000447:Aldehydes; D000596:Amino Acids; D046911:Macromolecular Substances; D013386:Succinates; D008623:Mercaptoethanol; D000445:Aldehyde Oxidoreductases