On the interaction of nucleotides and glycolytic intermediates with NAD-linked alpha-ketoaldehyde dehydrogenase.
The effect of different nucleotides and glycolytic intermediates was tested on the NAD-linked and NADP-linked alpha-ketoaldehyde dehydrogenases involved in the oxidation of methylglyoxal to pyruvate. ATP, GTP, and ADP strongly inhibit the NAD-linked enzyme whereas activity of the NADP-linked enzyme remained unaltered. NADP at a concentration much below its catalytic concentration strongly inhibited the NAD-linked enzyme. This NADP inhibition decreased with decreasing of the pH of the incubation medium. Fructose 1,6-bisphosphate stimulated and glyceraldehyde 3-phosphate inhibited the activity of the NAD-linked enzyme whereas dihydroxyacetone phosphate inhibited NADP-linked activity. The stimulatory effect of fructose 1,6-bisphosphate diminished with lowering of the pH value. The various effects by several key metabolites of the glycolytic pathway indicate a possible physiological role for these enzymes.
D000244:Adenosine Diphosphate / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000494:pharmacology; D000445:Aldehyde Oxidoreductases / Q000378:metabolism*; D000818:Animals; D006019:Glycolysis; D006041:Goats; D006160:Guanosine Triphosphate / Q000494:pharmacology; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D009249:NADP / Q000494:pharmacology; D012265:Ribonucleotides / Q000494:pharmacology*; D013403:Sugar Phosphates / Q000494:pharmacology
D012265:Ribonucleotides; D013403:Sugar Phosphates; D009249:NADP; D000244:Adenosine Diphosphate; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate; D000445:Aldehyde Oxidoreductases; C021928:2-oxoaldehyde dehydrogenase (NAD+)