Site-site interactions in the liver alcohol dehydrogenase catalytic mechanism
- 1 May 1979
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 18 (11), 2346-2354
- https://doi.org/10.1021/bi00578a033
Abstract
No abstract availableThis publication has 8 references indexed in Scilit:
- Effect of pH on the Process of Ternary‐Complex Interconversion in the liver‐Alcohol‐Dehydrogenase ReactionEuropean Journal of Biochemistry, 1978
- Evidence for site equivalence in the reaction mechanism of horse liver alcohol dehydrogenase with aromatic substrates at alkaline pHBiochemistry, 1977
- Kinetics of native and activated isozymes of horse liver alcohol dehydrogenaseBiochemistry, 1977
- The Transient‐State Kinetics of Two‐Substrate Enzyme Systems Operating by an Ordered Ternary‐Complex MechanismEuropean Journal of Biochemistry, 1976
- Kinetic Transients in the Reduction of Aldehydes Catalysed by Liver Alcohol DehydrogenaseEuropean Journal of Biochemistry, 1976
- Kinetic Studies with Liver Alcohol Dehydrogenase*Biochemistry, 1965
- Product Inhibition Studies on Yeast and Liver Alcohol Dehydrogenases*Biochemistry, 1963
- LIVER ALCOHOL DEHYDROGENASE-DPN-PYRAZOLE COMPLEX - A MODEL OF A TERNARY INTERMEDIATE IN ENZYME REACTION1963