PMID: 9432004Feb 7, 1998Paper

Mechanism of NADH transfer between alcohol dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase

European Journal of Biochemistry
W Martínez Arias, G Pettersson

Abstract

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.

References

Oct 1, 1979·European Journal of Biochemistry·J Kvassman, G Pettersson
Jan 15, 1991·Proceedings of the National Academy of Sciences of the United States of America·X M WuP B Chock
Dec 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·P B Chock, H Gutfreund
Mar 1, 1988·European Journal of Biochemistry·J KvassmanU Ryde-Pettersson

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Citations

Jul 4, 2002·FEBS Letters·U KalnenieksU Marjutina

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