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 dedu...

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Veröffentlicht in:	Journal of bioscience and bioengineering 2007-09, Vol.104 (3), p.224-226
Hauptverfasser:	Uchino, Keiichi, Katsumata, Yoko, Takeda, Tomoko, Arai, Hiroki, Shiraki, Mari, Saito, Terumi
Format:	Artikel
Sprache:	eng
Schlagworte:	3-hydroxybutyrate-oligomer hydrolase 3-Hydroxybutyric Acid - chemistry AMINO ACID SEQUENCES BACTERIA Biological and medical sciences Biotechnology Burkholderia - enzymology Burkholderia - genetics CLONACION MOLECULAR CLONAGE MOLECULAIRE Cloning, Molecular - methods Dimerization Enzyme Activation Enzyme Stability Escherichia coli - enzymology Escherichia coli - genetics Fundamental and applied biological sciences. Psychology gene cloning HIDROLASAS HYDROLASE HYDROLASES Hydrolases - chemistry Hydrolases - genetics MOLECULAR CLONING Paucimonas lemoignei PhaZc PURIFICACION PURIFICATION Ralstonia eutropha Recombinant Proteins - chemistry Recombinant Proteins - metabolism SECUENCIAS DE AMINOACIDOS SEQUENCE D'ACIDES AMINES Substrate Specificity Transfection - methods
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Zusammenfassung:	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.
ISSN:	1389-1723 1347-4421
DOI:	10.1263/jbb.104.224