Investigation of intermediates and transition states in the catalytic mechanisms of active site substituted cobalt(II), nickel(II), zinc(II), and cadmium(II) horse liver alcohol dehydrogenase.
Abstract: No abstract available
Publication Date: 1982-01-19 PubMed ID: 7041961DOI: 10.1021/bi00531a024Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
- Research Support
- U.S. Gov't
- Non-P.H.S.
Cite This Article
APA
Dunn MF, Dietrich H, MacGibbon AK, Koerber SC, Zeppezauer M.
(1982).
Investigation of intermediates and transition states in the catalytic mechanisms of active site substituted cobalt(II), nickel(II), zinc(II), and cadmium(II) horse liver alcohol dehydrogenase.
Biochemistry, 21(2), 354-363.
https://doi.org/10.1021/bi00531a024 Publication
Researcher Affiliations
MeSH Terms
- Alcohol Oxidoreductases / metabolism
- Animals
- Cadmium / metabolism
- Catalysis
- Cations, Divalent
- Cobalt / metabolism
- Horses
- Hydrogen-Ion Concentration
- Kinetics
- Liver / enzymology
- Nickel / metabolism
- Zinc / metabolism
Citations
This article has been cited 9 times.- Piersma SR, Norin A, de Vries S, Jörnvall H, Duine JA. Inhibition of nicotinoprotein (NAD+-containing) alcohol dehydrogenase by trans-4-(N,N-dimethylamino)-cinnamaldehyde binding to the active site. J Protein Chem 2003 Jul;22(5):457-61.
- Kleifeld O, Shi SP, Zarivach R, Eisenstein M, Sagi I. The conserved Glu-60 residue in Thermoanaerobacter brockii alcohol dehydrogenase is not essential for catalysis. Protein Sci 2003 Mar;12(3):468-79.
- Bogin O, Peretz M, Burstein Y. Thermoanaerobacter brockii alcohol dehydrogenase: characterization of the active site metal and its ligand amino acids. Protein Sci 1997 Feb;6(2):450-8.
- Ryde U. The coordination of the catalytic zinc in alcohol dehydrogenase studied by combined quantum-chemical and molecular mechanics calculations. J Comput Aided Mol Des 1996 Apr;10(2):153-64.
- Jeffery J, Chesters J, Mills C, Sadler PJ, Jörnvall H. Sorbitol dehydrogenase is a zinc enzyme. EMBO J 1984 Feb;3(2):357-60.
- Schneider G, Eklund H, Cedergren-Zeppezauer E, Zeppezauer M. Crystal structures of the active site in specifically metal-depleted and cobalt-substituted horse liver alcohol dehydrogenase derivatives. Proc Natl Acad Sci U S A 1983 Sep;80(17):5289-93.
- Makinen MW, Maret W, Yim MB. Neutral metal-bound water is the base catalyst in liver alcohol dehydrogenase. Proc Natl Acad Sci U S A 1983 May;80(9):2584-8.
- Bauer R, Adolph HW, Andersson I, Danielsen E, Formicka G, Zeppezauer M. Coordination geometry for cadmium in the catalytic zinc site of horse liver alcohol dehydrogenase: studies by PAC spectroscopy. Eur Biophys J 1991;20(4):215-21.
- Jacobi T, Kratzer DA, Plapp BV. Substitution of both histidines in the active site of yeast alcohol dehydrogenase 1 exposes underlying pH dependencies. Chem Biol Interact 2024 May 1;394:110992.
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