Skip to Content
MilliporeSigma
  • The human beta 3 alcohol dehydrogenase subunit differs from beta 1 by a Cys for Arg-369 substitution which decreases NAD(H) binding.

The human beta 3 alcohol dehydrogenase subunit differs from beta 1 by a Cys for Arg-369 substitution which decreases NAD(H) binding.

Biochemical and biophysical research communications (1987-08-14)
J C Burnell, L G Carr, F E Dwulet, H J Edenberg, T K Li, W F Bosron
ABSTRACT

The beta 3 beta 3 (formerly called beta Indianapolis) and beta 1 beta 1 isoenzymes of human alcohol dehydrogenase differ substantially in their catalytic properties. Specifically, the KM value for NAD+ of beta 3 beta 3 is 70 times greater than that of beta 1 beta 1, and the Ki value for NADH is 35 times greater than that of beta 1 beta 1. To identify the structural basis of these catalytic differences, we sequenced regions of the beta 3 subunit and the beta 3 gene. beta 3 differs from beta 1 by the substitution of Cys for Arg-369. Based on x-ray crystallography of horse ADH, Arg-369 should interact with the nicotinamide phosphate moiety of NAD(H). The Cys for Arg-369 substitution would decrease the enzyme's affinity for coenzyme and, thus, account for the observed kinetic differences between beta 3 beta 3 and beta 1 beta 1.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Alcohol Dehydrogenase from Saccharomyces cerevisiae, powder, ≥300 units/mg protein, mol wt ~141,000 (four subunits)
Sigma-Aldrich
Alcohol Dehydrogenase from Saccharomyces cerevisiae
Sigma-Aldrich
Alcohol Dehydrogenase from Saccharomyces cerevisiae, ≥300 units/mg protein, lyophilized powder (contains buffer salts), Mw 141-151 kDa
Sigma-Aldrich
Alcohol Dehydrogenase equine, recombinant, expressed in E. coli, ≥0.5 U/mg