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Novel substrates of yeast alcohol dehydrogenase — 3. 4-dimethylamino-cinnamaldehyde and chloroacetaldehyde
Authors:
V. Leskovac a;
S. Trivi
b;
J. Zeremski c;
B. Stan
i d;
B. M. Anderson e
b;
J. Zeremski c;
B. Stani d;
B. M. Anderson e
| Affiliations: | a Faculty of Technology Novi Sad, Novi Sad, Yugoslavia |
| b Faculty of Science Novi Sad, Yugoslavia | |
| c Faculty of Technology Beograd, Yugoslavia | |
| d Faculty of Agriculture Novi Sad, Yugoslavia | |
| e Virginia Polytechnic Institute and State University, Virginia, USA |
DOI:
10.1080/15216549700204151
Publication Frequency:
12 issues per year
Subjects:
Cell Biology;
Molecular Biology;
Formats available:
HTML
(English)
:
PDF
(English)
Previously published as:
Biochemistry and Molecular Biology International
(1039-9712)
until 1998
The circumstances under which this title is published have changed:
Reason for change: Changed publisher
Now published by: Wiley-Blackwell Publishing Ltd
Date of change: 2008
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Abstract
4-Dimethylamino-trans-cinnamaldehyde and chloroacetaldehyde are novel substrates of yeast alcohol dehydrogenase (EC 1.1.1.1). In the present work, we have reported the steady-state kinetic constants for both substrates, and their chemical reactions with the enzyme protein itself. Both substrates are potentially useful for biotechnology, chemoenzyme syntheses and analytical biochemistry.
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