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Kinetics and Mechanism of Methanol and Formaldehyde Interconversion and Formaldehyde Oxidation Catalyzed by Liver Alcohol Dehydrogenase

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Enzymology and Molecular Biology of Carbonyl Metabolism 3

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 284))

Abstract

Liver alcohol dehydrogenase (LADH) is a well-characterized protein. Both its primary and tertiary structures are known, as are some of the catalytic mechanisms, isozyme differences, evolutionary divergences and a number of enzymatic properties (Jörnvall, 1970; Brändén, et al., 1975; Klinman, 1981; Eklund and Brändén, 1983; Pettersson, 1987; Pocker, 1989). In contrast, relatively little is known about its interaction with methanol, although there is extensive structural homology between this compound and ethanol.

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Author information

Authors and Affiliations

  1. Department of Chemistry, University of Washington, Seattle, WA, 98195, USA

    Y. Pocker & Hong Li

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  1. Y. Pocker
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  2. Hong Li
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Editor information

Editors and Affiliations

  1. Department of Biochemistry, Purdue University, West Lafayette, Indiana, 47907, USA

    Henry Weiner

  2. Chemisches Zentrallabor, Inselspital, Bern, CH 3010, Switzerland

    Bendicht Wermuth

  3. Indiana University School of Medicine and Veterans Administration Medical Center, Indianapolis, Indiana, 46202, USA

    David W. Crabb

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© 1990 Plenum Press, New York

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Pocker, Y., Li, H. (1990). Kinetics and Mechanism of Methanol and Formaldehyde Interconversion and Formaldehyde Oxidation Catalyzed by Liver Alcohol Dehydrogenase. In: Weiner, H., Wermuth, B., Crabb, D.W. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 3. Advances in Experimental Medicine and Biology, vol 284. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5901-2_34

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  • DOI: https://doi.org/10.1007/978-1-4684-5901-2_34

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-5903-6

  • Online ISBN: 978-1-4684-5901-2

  • eBook Packages: Springer Book Archive

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