Factors affecting coenzyme binding and subunit interactions in glyceraldehyde-3-phosphate dehydrogenase.
There is no evidence, at pH 9.4, of negative cooperativity in the binding of NAD+ or NADH to rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phorphorylating), EC 1.2.1.12) nor in the binding of acetyl pyridine adenine dinucleotide at pH 7.6 and ph 9.4. The binding of NAD+ to carboxymethylated enzyme at pH 7.6 and pH 9.4 also occurs without cooperativity. The possible implications of these findings for the involvement of ionising groups in the enzyme in the subunit interactions responsible for negative cooperativity, previously reported for coenzyme binding at pH 7.4--8.6, are discussed.
D000478:Alkylation; D000818:Animals; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D009132:Muscles / Q000201:enzymology; D009243:NAD / Q000031:analogs & derivatives / Q000378:metabolism* / Q000494:pharmacology; D011485:Protein Binding; D011817:Rabbits
D046911:Macromolecular Substances; D009243:NAD; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases