Amino acid substitutions at position 47 of human beta 1 beta 1 and beta 2 beta 2 alcohol dehydrogenases affect hydride transfer and coenzyme dissociation rate constants.-Reference-Cited by-同舟云学术

Amino acid substitutions at position 47 of human beta 1 beta 1 and beta 2 beta 2 alcohol dehydrogenases affect hydride transfer and coenzyme dissociation rate constants.

Published:1993-01 Issue:2 Volume:268 Page:892-899
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Stone C.L.,Bosron W.F.,Dunn M.F.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference31 articles.

1. ALCOHOL AND ALDEHYDE DEHYDROGENASE*

2. Kinetic and electrophoretic properties of native and recombined isoenzymes of human liver alcohol dehydrogenase

3. Human liver alcohol dehydrogenase: purification and kinetic characterization of the .beta.2.beta.2, .beta.2.beta.1, .alpha..beta.2, and .beta.2.gamma.1 "Oriental" isoenzymes

4. Purification and steady-state kinetic characterization of human liver .beta.3.beta.3 alcohol dehydrogenase

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