Mechanism of NADH transfer between alcohol dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase.
Steady-state and transient-state kinetic experiments have been performed to test the proposal that there is a direct (channelled) transfer of NADH from glyceraldehyde-3-phosphate dehydrogenase to alcohol dehydrogenase. The results lend no support to this proposal, but can be best explained in terms of a free-diffusion mechanism for NADH transfer between the two enzymes.
Martínez Arias
W
W
Avdelningen för Biokemi, Kemicentrum, Lunds Universitet, Lund, Sweden.
Pettersson
G
G
D000426:Alcohol Dehydrogenase / Q000378:metabolism*; D000818:Animals; D001547:Benzaldehydes / Q000378:metabolism; D002384:Catalysis; D004058:Diffusion; D005399:Fishes; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D009132:Muscles / Q000201:enzymology; D009243:NAD / Q000378:metabolism*; D011485:Protein Binding; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet
D001547:Benzaldehydes; D009243:NAD; D000426:Alcohol Dehydrogenase; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; C032175:benzaldehyde