A novel archaebacterial NAD+‐dependent alcohol dehydrogenase
Open Access
- 1 September 1987
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 167 (3) , 475-479
- https://doi.org/10.1111/j.1432-1033.1987.tb13361.x
Abstract
An NAD+‐dependent alcohol dehydrogenase (alcohol:NAD+ oxidoreductase, EC 1.1.1.1) was detected in cellular extracts of the extreme thermophilic archaebacterium Sulfolobus solfataricus. The enzyme was purified to homogeneity and shown to be a dimer with a native molecular mass of 71 kDa by sucrose gradient centrifugation and SDS electrophoresis. The enzyme has a broad substrate specificity that includes linear and branched primary alcohols, linear and cyclic secondary alcohols, linear and cyclic ketones and anisaldehyde. The enzyme has an extraordinary thermophilicity and a remarkable thermostability, and appears to have some properties and a structure different from those previously described for thermophilic alcohol dehydrogenases.This publication has 21 references indexed in Scilit:
- Organic synthesis with enzymes. 3. TBADH-catalyzed reduction of chloro ketones. Total synthesis of (+)-(S,S)-(cis-6-methyltetrahydropyran-2-yl)acetic acid: a civet constituentJournal of the American Chemical Society, 1986
- Structure and properties of a thermophilic and thermostable DNA polymerase isolated from Sulfolobus solfataricusSystematic and Applied Microbiology, 1986
- Purification and properties of an alcohol dehydrogenase from Sporotrichum pulverulentumEnzyme and Microbial Technology, 1986
- Enzymes in organic synthesis. 34. Preparations of enantiomerically pure exo- and endo-bridged bicyclic [2.2.1] and [2.2.2] chiral lactones via stereospecific horse liver alcohol dehydrogenase catalyzed oxidations of meso diolsJournal of the American Chemical Society, 1985
- New molecular forms of human liver alcohol dehydrogenase: isolation and characterization of ADHIndianapolis.Proceedings of the National Academy of Sciences, 1980
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Rapid purification of lactate dehydrogenase from rat liver and hepatoma: A new approachArchives of Biochemistry and Biophysics, 1974
- Horse Liver Alcohol DehydrogenaseEuropean Journal of Biochemistry, 1970
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964
- Yeast Alcohol Dehydrogenase. III. Relation of Alcohol Structure to Activity1Journal of the American Chemical Society, 1957