Alcohol dehydrogenase (ADH2) from a mutant strain of Candida guilliermondii A80-03: purification and characterization.
Alcohol dehydrogenase ADH2 was purified twice from Candida guilliermondii strain A80-03, by ion exchange column chromatography on DEAE-Toyopearl 650M. The enzyme was a dimer of M(r) 98,500. ADH2 had a broad substrate specificity, oxidizing secondary alcohols as well as primary alcohols. The enzyme was sensitive to several inhibitors, such as metal chelators and thiol reagents. Kinetic studies suggested that ADH2 oxidized ethanol by an iso ordered sequential mechanism.
Indrati
R
R
Laboratory of Microbial Biochemistry, Faculty of Applied Biological Science, Hiroshima University, Higashi, Japan.
Ohta
Y
Y
D000426:Alcohol Dehydrogenase / Q000037:antagonists & inhibitors / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D000438:Alcohols / Q000378:metabolism; D002175:Candida / Q000201:enzymology* / Q000235:genetics; D002412:Cations / Q000494:pharmacology; D002614:Chelating Agents / Q000494:pharmacology; D002846:Chromatography, Affinity; D005656:Fungal Proteins / Q000037:antagonists & inhibitors / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D010084:Oxidation-Reduction; D013379:Substrate Specificity; D013438:Sulfhydryl Compounds / Q000494:pharmacology; D013696:Temperature
D000438:Alcohols; D002412:Cations; D002614:Chelating Agents; D005656:Fungal Proteins; D013438:Sulfhydryl Compounds; D000426:Alcohol Dehydrogenase