Purification and molecular cloning of an intracellular 3-hydroxybutyrate-oligomer hydrolase from Paucimonas lemoignei.
An intracellular 3-hydroxybutyrate-oligomer hydrolase was purified from a poly(3-hydroxybutyrate)-degrading bacterium, Paucimonas lemoignei. It hydrolyzed the 3-hydroxybutyrate dimer with the highest specific activity of any of the enzymes reported so far. The gene was cloned and sequenced. The deduced amino acid sequence showed that the enzyme is a homolog of the PhaZc of Ralstonia eutropha H16.
Uchino
Keiichi
K
Laboratory of Molecular Microbiology, Department of Biological Sciences, Faculty of Science, Kanagawa University, 2946 Tsuchiya, Hiratsuka, Kanagawa 259-1293, Japan.
Katsumata
Yoko
Y
Takeda
Tomoko
T
Arai
Hiroki
H
Shiraki
Mari
M
Saito
Terumi
T
D020155:3-Hydroxybutyric Acid / Q000737:chemistry*; D019117:Burkholderia / Q000201:enzymology* / Q000235:genetics; D003001:Cloning, Molecular / Q000379:methods*; D019281:Dimerization; D004789:Enzyme Activation; D004795:Enzyme Stability; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D006867:Hydrolases / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity; D014162:Transfection / Q000379:methods*
D011994:Recombinant Proteins; D006867:Hydrolases; D020155:3-Hydroxybutyric Acid