The isolation and characterization of 3-phosphoglycerate dehydrogenase from peas.
1. 3-Phosphoglycerate dehydrogenase was purified 400-fold from crude extracts of etiolated pea epicotyls. 2. Michaelis constants were determined for all four substrates. 3. Loss of sensitivity to inhibition by l-serine occurs on purification. 4. The purified enzyme is inhibited by thiol-group reagents and, with N-ethyl-maleimide, protection is afforded by 3-phosphoglycerate though not by NAD(+).
D000429:Alcohol Oxidoreductases; D005033:Ethylmaleimide / Q000494:pharmacology; D005994:Glycerophosphates; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009243:NAD / Q000494:pharmacology; D009249:NADP / Q000494:pharmacology; D010088:Oxidoreductases / Q000037:antagonists & inhibitors; D010944:Plants / Q000201:enzymology*; D012694:Serine / Q000494:pharmacology
D005994:Glycerophosphates; D009243:NAD; D012694:Serine; D009249:NADP; D010088:Oxidoreductases; D000429:Alcohol Oxidoreductases; D005033:Ethylmaleimide