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Biochemistry1982; 21(2); 354-363; doi: 10.1021/bi00531a024

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

ISSN: 0006-2960
NlmUniqueID: 0370623
Country: United States
Language: English
Volume: 21
Issue: 2
Pages: 354-363

Researcher Affiliations

Dunn, M F
    Dietrich, H
      MacGibbon, A K
        Koerber, S C
          Zeppezauer, M

            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.
            1. 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.
            2. 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.
              doi: 10.1110/ps.0221603pubmed: 12592017google scholar: lookup
            3. 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.
              doi: 10.1002/pro.5560060223pubmed: 9041649google scholar: lookup
            4. 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.
              doi: 10.1007/BF00402823pubmed: 8741019google scholar: lookup
            5. Jeffery J, Chesters J, Mills C, Sadler PJ, Jörnvall H. Sorbitol dehydrogenase is a zinc enzyme. EMBO J 1984 Feb;3(2):357-60.
            6. 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.
              doi: 10.1073/pnas.80.17.5289pubmed: 6351056google scholar: lookup
            7. 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.
              doi: 10.1073/pnas.80.9.2584pubmed: 6302696google scholar: lookup
            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.
              doi: 10.1007/BF00183458pubmed: 1807973google scholar: lookup
            9. 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.
              doi: 10.1016/j.cbi.2024.110992pubmed: 38579923google scholar: lookup