Stereospecificity of hydrogen transfer of aldehyde reductase

Experientia
B WermuthJ P von Wartburg

Abstract

Aldehyde reductase from human liver catalyzes the hydrogen transfer from the pro-4R position on the dihydronicotinamide ring of the coenzyme to the re face of the carbonyl carbon atom of the substrate.

References

Jun 19, 1986·Biochimica Et Biophysica Acta·T NakayamaH Sawada
Feb 1, 1992·Archives of Biochemistry and Biophysics·H OritaniI Ohya
Jan 1, 1986·Archives of Biochemistry and Biophysics·A HaraH Sawada
Dec 1, 1995·Xenobiotica; the Fate of Foreign Compounds in Biological Systems·U Breyer-Pfaff, K Nill
Jan 1, 1989·Drug Metabolism Reviews·N E SladekG J Landkamer

Citations

Jan 11, 1977·Biochimica Et Biophysica Acta·H B FeldmanB R Landau
Feb 9, 1979·Biochimica Et Biophysica Acta·B WermuthJ P von Wartburg
Sep 15, 1951·Klinische Wochenschrift·T BUCHER, H REDETZKI

Related Concepts

Molecular Stereochemistry
Dihydronicotinamide
AKR1A1 gene
Aldehyde Oxidoreductases
Substrate Specificity
NADP
Oxidation-Reduction
Aldehyde Reductase
Liver
Coenzymes

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