Related Experiment Video
Updated: Oct 7, 2026

A Toolkit to Enable Hydrocarbon Conversion in Aqueous Environments
Published on: October 2, 2012
Genetic and biochemical characterization of a short-chain alcohol dehydrogenase from the hyperthermophilic archaeon
J van der Oost1, W G Voorhorst, S W Kengen
1Laboratory of Microbiology, Wageningen University, the Netherlands. john.vanderoost@algemeen.micr.wag-ur.nl
Abstract:
The gene encoding a short-chain alcohol dehydrogenase, AdhA, has been identified in the hyperthermophilic archaeon Pyrococcus furiosus, as part of an operon that encodes two glycosyl hydrolases, the beta-glucosidase CelB and the endoglucanase LamA. The adhA gene was functionally expressed in Escherichia coli, and AdhA was subsequently purified to homogeneity. The quaternary structure of AdhA is a dimer of identical 26-kDa subunits. AdhA is an NADPH-dependent oxidoreductase that converts alcohols to the corresponding aldehydes/ketones and vice versa, with a rather broad substrate specificity. Maximal specific activities were observed with 2-pentanol (46 U x mg(-1)) and pyruvaldehyde (32 U x mg(-1)) in the oxidative and reductive reaction, respectively. AdhA has an optimal activity at 90 degrees C, at which temperature it has a half life of 22.5 h. The expression of the adhA gene in P. furiosus was demonstrated by activity measurements and immunoblot analysis of cell extracts. A role of this novel type of archaeal alcohol dehydrogenase in carbohydrate fermentation is discussed.
Related Concept Videos
Diversity of Archaea IV
Diversity of Archaea III
Hyperthermophilic Bacteria
Diversity of Archaea I
Microbial Fermentation
Overview of Archaea

