Structural properties of long- and short-chain alcohol dehydrogenases. Contribution of NAD+ to stability
- 1 June 1991
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 276 (2) , 433-438
- https://doi.org/10.1042/bj2760433
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- Prokaryotic 20β‐hydroxysteroid dehydrogenase is an enzyme of the ‘short‐chain, non‐metalloenzyme’ alcohol dehydrogenase typeFEBS Letters, 1990
- Ligand-induced biphasic protein denaturation.Journal of Biological Chemistry, 1990
- Purification and structural characterization of placental NAD+-linked 15-hydroxyprostaglandin dehydrogenase. The primary structure reveals the enzyme to belong to the short-chain alcohol dehydrogenase familyBiochemistry, 1990
- Tryptophan luminescence from liver alcohol dehydrogenase in its complexes with coenzyme. A comparative study of protein conformation in solutionBiochemistry, 1990
- Conformational stability of globular proteinsTrends in Biochemical Sciences, 1990
- Complete amino acid sequence of human placental 17β‐hydroxysteroid dehydrogenase deduced from cDNAFEBS Letters, 1988
- [14]Determination and analysis of urea and guanidine hydrochloride denaturation curvesPublished by Elsevier ,1986
- Determination of some biochemical and structural features of alcohol dehydrogenases from Drosophila simulans and Drosophila virilis. Comparison of their properties with the Drosophila melanogaster Adhs enzymeBiochemical Journal, 1981
- DROSOPHILA ALCOHOL DEHYDROGENASE - PURIFICATION AND PARTIAL CHARACTERIZATION1968
- Studies on the Mechanism of Enzyme-Catalyzed Oxidation Reduction Reactions.* V. An Exchange Reaction Catalyzed by Liver Alcohol DehydrogenaseBiochemistry, 1962