Thermostable NAD^+-Dependent (R)-Specific Secondary Alcohol Dehydrogenase from Cholesterol-Utilizing Burkholderia sp. AIU 652
スポンサーリンク
概要
- 論文の詳細を見る
An alcohol dehydrogenase produced by Burkholderia sp. AIU 652, which was isolated with a cholesterol medium, was purified to homogeneity and characterized. The enzyme had broad substrate specificity, and the best reaction was the reversible oxidation of 2-propanol to acetone and 2-butanol to 2-butanone. The K_m values for secondary alcohols and ketones were much lower than those for primary alcohols or diols. In addition, the enzyme oxidized R-(-)-alcohols in preference to S-(+)-alcohols, and utilized NAD^+, but not NADP^+ as the cofactor. The molecular mass was 150 kDa with four identical subunits, and the activity was inhibited by o-phenanthroline, 8-hy-droxyquinoline, and α,α'-dipyridyl. Thus, this enzyme was classified into a group of NAD^+-dependent R-(-)-specific secondary alcohol dehydrogenases. However, this enzyme was better than the previously reported NAD^+-dependent R-(-)-specific secondary alcohol dehydrogenases for chiral chemical synthesis in terms of substrate specificity, stereospecificity, and thermostability. This enzyme might be applicable as an effective biocatalyst for the production of chiral alcohols and related compounds.
- 社団法人日本生物工学会の論文
- 2003-10-25
著者
-
Isobe Kimiyasu
Department of Agro-bioscience, Faculty of Agriculture, Iwate University
-
Isobe Kimiyasu
Department Of Agro-bioscience Faculty Of Agriculture Iwate University
-
WAKAO NORIO
Department of Agro-bioscience, Faculty of Agriculture, Iwate University
-
Wakao Norio
Department Of Agro-bioscience Faculty Of Agriculture Iwate University
関連論文
- Production and characterization of alcohol oxidase from Penicillium purpurescens AIU 063(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Purification and Characterization of a New Aldehyde Oxidase from Pseudomonas sp. AIU 362(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Superoxide Dismutases Exhibit Oxidase Activity on Aldehyde Alcohols Similar to Alcohol Oxidase from Paenibacillus sp. AIU 311(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Analysis of Selective Production of N^α-Benzyloxycarbonyl-L-Aminoadipate-δ-Semialdehyde and N^α-Benzyloxycarbonyl-L-Aminoadipic Acid by Rhodococcus sp. AIU Z-35-1(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Purification and Characterization of a Dehydrogenase Catalyzing Conversion of N^α-Benzyloxycarbonyl-L-Aminoadipic-δ-Semialdehyde to N^α-Benzyloxycarbonyl-L-Aminoadipic Acid from Rhodococcus sp. AIU Z-35-1(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNO
- Characterization of N^α-Benzyloxycarbonyl-L-Lysine Oxidizing Enzyme from Rhodococcus sp. AIU Z-35-1(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Purification and Characterization of a Novel Alcohol Oxidase from Paenibacillus sp. AIU 311(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- A New Microbial Method for More Efficient Production of N^α-Benzyloxycarbonyl-L-Aminoadipate δ-Semialdehyde and N^α-Benzyloxycarbonyl-D-Aminoadipate δ-Semialdehyde(MICROBIAL PHYSIOLOGY AND BIOTECHNOLOGY)
- Purification and Some Properties of Cholesterol Oxidase Stable in Detergents from γ-Proteobacterium Y-134
- Crystallization and Some Properties of D-Lactate Dehydrogenase from Staphylococcus sp. LDH-1
- Production of Catalase by Fungi Growing at Low pH and High Temperature(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Identification and Characterization of Enzyme Catalyzing Conversion of N^α-Benzyloxycarbonyl-L-Aminoadipic-δ-Semialdehyde to N^α-Benzyloxycarbonyl-L-Aminoadipic Acid in Aspergillus niger AKU 3302(MICROBIAL PHYSIOLOGY AND BIOTECHNOLOGY)
- Thermostable NAD^+-Dependent (R)-Specific Secondary Alcohol Dehydrogenase from Cholesterol-Utilizing Burkholderia sp. AIU 652
- The Second Cholesterol Oxidase Produced by γ-Proteobacterium Y-134(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Enhanced Growth of Acidocella facilis and Related Acidophilic Bacteria at High Concentrations of Aluminum
- Nucleotide Sequences of Genes Coding for Photosynthetic Reaction Centers and Light-Harvesting Proteins of Acidiphilium rubrum and Related Aerobic Acidophilic Bacteria
- Purification and characterization of an L-amino acid oxidase from Pseudomonas sp. AIU 813(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Purification and Characterization of a New Aldehyde Oxidase from Pseudomonas sp. AIU 362
- Characterization and application of a L-specific amino acid oxidase from Rhodococcus sp. AIU LAB-3(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Characterization of new β-galactosidase from acidophilic fungus, Teratosphaeria acidotherma AIU BGA-1(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Purification and characterization of an L-amino acid oxidase from Pseudomonas sp. AIU 813
- Acidophilic fungus, Teratosphaeria acidotherma AIU BGA-1, produces multiple forms of intracellular β-galactosidase(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Differential Determination Procedure for Putrescine, Spermidine and Spermine with Polyamine Oxidase from Fungi and Putrescine Oxidase
- Characterization of a novel L-amino acid oxidase with protein oxidizing activity from Penicillium steckii AIU 027(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Characterization and application of aminoamide-oxidizing enzyme from Aspergillus carbonarius AIU 205(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)