Inhibition of 3-phosphoglycerate dehydrogenase from Pisum sativum by purine nucleotides.
The inhibition of 3-phosphoglycerate dehydrogenase from etiolated pea epicotyls by purine nucleoside di- and tri-phosphates is linear, competitive with regard to NADH, and the nucleotides are mutually exclusive in their binding. Free ATP and ADP are more effective inhibitors than are the respective magnesium complexes.
D000241:Adenosine / Q000494:pharmacology; D000249:Adenosine Monophosphate / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000494:pharmacology; D000375:Aging; D000429:Alcohol Oxidoreductases / Q000037:antagonists & inhibitors*; D001665:Binding Sites; D005988:Glyceric Acids; D006160:Guanosine Triphosphate / Q000494:pharmacology; D008274:Magnesium; D009943:Organophosphorus Compounds; D010944:Plants / Q000201:enzymology*; D011685:Purine Nucleotides / Q000494:pharmacology*; D012694:Serine / Q000494:pharmacology
D005988:Glyceric Acids; D009943:Organophosphorus Compounds; D011685:Purine Nucleotides; D000249:Adenosine Monophosphate; D012694:Serine; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate; D000429:Alcohol Oxidoreductases; D008274:Magnesium; D000241:Adenosine