Characterization of an alcohol dehydrogenase from Thermoanaerobacter ethanolicus active with ethanol and secondary alcohols

Journal Article · Fri May 29 00:00:00 EDT 1981 · Biochem. Biophys. Res. Commun.; (United States)

DOI:https://doi.org/10.1016/S0006-291X(81)80244-6· OSTI ID:5242886

Bryant, F; Ljungdahl, L G

Thermoanaerobacter ethanolicus contains a NADP-dependent alcohol dehydrogenase. Ethanol is a substrate but secondary alcohols such as 2-propanol, 2-butanol and 2-pentanol are oxidized at a faster rate. The enzyme has a molecular weight of 172,000 and consists of 4 subunits. Each subunit contains 4 zinc atoms. With ethanol the kinetics are sigmoidal; however, in the presence of pyruvate a Michaelis-Menten kinetic pattern is approached. At 70/sup 0/C and pH 9 the purified enzyme oxidizes ethanol with NADP at a rate of 13 ..mu..mol min/sup -1/ mg/sup -1/, whereas it reduces acetaldehyde with NADPH two times that rate.

• Research Organization: Univ. of Georgia, Athens
• DOE Contract Number: AS09-79ER10499
• OSTI ID: 5242886
• Journal Information: Biochem. Biophys. Res. Commun.; (United States), Vol. 100:2
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
ETHANOL
BIOSYNTHESIS
OXIDOREDUCTASES
ENZYME ACTIVITY
AEROBACTER
BIOCHEMICAL REACTION KINETICS
METABOLISM
MOLECULAR WEIGHT
NADP
OXIDATION
TEMPERATURE DEPENDENCE
ZINC
ALCOHOLS
BACTERIA
CHEMICAL REACTIONS
COENZYMES
ELEMENTS
ENZYMES
HYDROXY COMPOUNDS
KINETICS
METALS
MICROORGANISMS
NUCLEOTIDES
ORGANIC COMPOUNDS
REACTION KINETICS
SYNTHESIS
550700* - Microbiology
550500 - Metabolism
550200 - Biochemistry