Martínez Arias W, Pettersson G
Avdelningen för Biokemi, Kemicentrum, Lunds Universitet, Lund, Sweden.
Eur J Biochem. 1997 Nov 15;250(1):158-62. doi: 10.1111/j.1432-1033.1997.00158.x.
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.