Noncovalent modulation by ATP of the acyl transfer from acyl-glyceraldehyde-3-phosphate dehydrogenase to phosphate.
The effect of ATP on the formation, spectral properties, and reactions of [beta-(2-furyl)acryloyl]glyceraldehyde-3-phosphate dehydrogenase (FA-GPDH) has been investigated. The chromophoric FA-GPDH has the advantage of providing spectrophotometric signals of the interaction of acyl enzyme with nucleotides and dinucleotides. The results are consistent with the exclusive existence of two acyl-enzyme conformations previously inferred from the interaction of the acyl enzyme with NAD+ and NADH. ATP interaction stabilizes a conformation different from that stabilized by NAD+. The inhibitory effects of ATP on these reactions are consistent with the reported inhibitory effect of ATP on the steady-state reaction with the true substrate. The physiological significance of these results to the regulation of glycolysis, via the ligand-dependent fate of 3-phosphoglycerol-GPDH, is discussed.
Malhotra
O P
OP
Institute of Molecular Biology, University of Oregon, Eugene 97403.
Bernhard
S A
SA
D000179:Acrylates / Q000378:metabolism*; D000215:Acylation; D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000818:Animals; D001149:Arsenates / Q000378:metabolism; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D066298:In Vitro Techniques; D007700:Kinetics; D009243:NAD / Q000378:metabolism; D011487:Protein Conformation / Q000187:drug effects; D013056:Spectrophotometry, Ultraviolet
D000179:Acrylates; D001149:Arsenates; D009243:NAD; C025983:beta-(2-furyl)acryloyl phosphate; D000255:Adenosine Triphosphate; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; C025657:arsenic acid