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Reaction of p-azidophenacyl lodoacetate, a photolabile reagent, with yeast alcohol dehydrogenase

โœ Scribed by Susan H. Hixson; Susan F. Burroughs; Theresa M. Caputo; Barbara B. Crapster; Mary V. Daly; Allison W. Lowrie; Margery L. Wasko


Book ID
115703956
Publisher
Elsevier Science
Year
1979
Tongue
English
Weight
551 KB
Volume
192
Category
Article
ISSN
0003-9861

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โœ Shiou-Chuan Tsai; Judith P. Klinman ๐Ÿ“‚ Article ๐Ÿ“… 2003 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 277 KB

In order to understand the influence of protein dynamics on enzyme catalysis and hydrogen tunneling, the horse liver alcohol dehydrogenase (HLADH) catalyzed oxidation of benzyl alcohol was studied at sub-zero temperatures. Previous work showed that wild type HLADH has significant kinetic complexity