Biochemical and Genetic Characterization of a D(-)-3-Hydroxybutyrate Dehydrogenase from Acidovorax sp. Strain SA1
スポンサーリンク
概要
- 論文の詳細を見る
D(-)-3-Hydroxybutyrate dehydrogenase (BDH; EC 1.1.1.30) from a poly(D(-)-3-hydroxybutyrate) (PHB) degrading bacterium, Acidovorax sp. SA1, was purified using Toyopearl DEAE-650M, red-Sepharose CL-4B, and Q Sepharose FF. The molecular mass of the enzyme was estimated as 27 kDa by SDS-PAGE and 110 kDa by gel filtration. The gene encoding BDH was cloned and sequenced, and expressed in Eseherichia coli. The gene product was purified in two steps with a high yield. The N-terminal amino acid sequence of the enzyme purified from E. coli agreed with that of the purified enzyme from strain SA1. The BDH of strain SA1 had high amino acid sequence homology to that of Raistonia eutropha H16. The K_m values for D(-)-3-hydroxybutyrate and NAD^+ in the oxidation reaction were 4.5 × 10^<-4> M and 8.9 × 10^<-5> M, respectively. The K_m values for acetoacetate and NADH in the reduction reaction were 2.4 × 10^<-4> M and 2.9× 10^<-5> M, respectively.
- 社団法人日本生物工学会の論文
- 2004-01-25
著者
-
Saito T
National Institute Of Advanced Industrial Science And Technology (aist)
-
Saito Terumi
National Institute Of Advanced Industrial Science And Technology (aist)
-
Saito Terumi
Laboratory Of Molecular Microbiology Department Of Biological Sciences Faculty Of Science Kanagawa U
-
Saito Terumi
Laboratory Of Molecular Microbiology Department Of Biological Science Faculty Of Science Kanagawa Un
-
Takanashi Masahiko
Laboratory of Molecular Microbiology, Department of Biological Science, Faculty of Science, Kanagawa
-
Shiraki Mari
Laboratory of Molecular Microbiology, Department of Biological Science, Faculty of Science, Kanagawa
-
SHIBAHARA TADASHI
Laboratory of Molecular Microbiology, Department of Biological Sciences, Faculty of Science, Kanagaw
-
Shiraki M
Laboratory Of Molecular Microbiology Department Of Biological Science Faculty Of Science Kanagawa Un
-
Shiraki Mari
Laboratory Of Molecular Microbiology Department Of Biological Sciences Faculty Of Science Kanagawa U
-
Takahashi M
Laboratory Of Molecular Microbiology Department Of Biological Science Faculty Of Science Kanagawa Un
-
Shibahara Tadashi
Laboratory Of Molecular Microbiology Department Of Biological Sciences Faculty Of Science Kanagawa U
-
Takanashi Masahiko
Laboratory Of Molecular Microbiology Department Of Biological Science Faculty Of Science Kanagawa Un
-
Saito Takao
Department Of Chemistry National Industrial Research Institute Of Nagoya
関連論文
- An Intracellular PHB Depolymerase from the Supernatant Fraction of Ralstonia eutropha H16 Cells
- Characterization of Two 3-Hydroxybutyrate Dehydrogenases in Poly(3-Hydroxybutyrate)-Degradable Bacterium, Ralstonia pickettii T1 (MICROBIAL PHYSIOLOGY AND BIOTECHNOLOGY)
- Characterization of Third 3-Hydroxybutyrate Dehydrogenase in Ralstonia pickettii T1
- Reaction Properties of Catalytic Antibodies Encapsulated in Organo Substituted SiO_2 Sol-Gel Materials(BIOCHEMICAL ENGINEERING)
- Detoxification of Bisphenol A and Nonylphenol by Purified Extracellular Laccase from a Fungus Isolated from Soil(ENVIRONMENTAL BIOTECHNOLOGY)
- Biochemical and Genetic Characterization of a D(-)-3-Hydroxybutyrate Dehydrogenase from Acidovorax sp. Strain SA1
- Catalytic Triad of Intracellular Poly(3-Hydroxybutyrate) Depolymerase(PhaZ1) in Ralstonia eutropha H16
- Catalytic Properties of Lipases Immobilized on Various Mesoporous Silicates(Microbiology & Fermentation Technology)
- Preparation and Catalytic Performance of Lipases Encapsulated in Sol-Gel Materials(Microbiology & Fermentation Technology)
- Eficient Preparation of Optically Active Ketoprofen by Mucor javanicus Lipase Immobilized on an Inorganic Support
- Fermentative Production of (R)-(-)-3-Hydroxybutyrate Using 3-Hydroxybutyrate Dehydrogenase Null Mutant of Ralstonia eutropha and Recombinant Escherichia coli(MICROBIAL PHYSIOLOGY AND BIOTECHNOLOGY)
- Cloning and Sequencing of the Poly (3-hydroxybutyrate)(PHB) Synthase Gene from Purple Non-Sulfur Bacteria Rhodospirillum centenum and Expression of the Gene in Escherichia coli
- Purification and Molecular Cloning of an Intracellular 3-Hydroxybutyrate-Oligomer Hydrolase from Paucimonas lemoignei(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Cloning of an Intracellular D(-)-3-Hydroxybutyrate-Oligomer Hydrolase Gene from Ralstonia eutropha H16 and Identification of the Active Site Serine Residue by Site-Directed Mutagenesis
- Catalytic activity of aryl alcohol oxidase immobilized in 3D-mesoporous silicates(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Thiolysis of Poly(3-hydroxybutyrate) with Polyhydroxyalkanoate Synthase from Ralstonia eutropha