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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Bibliographic Details
Published in:Journal of bioscience and bioengineering 2007-09, Vol.104 (3), p.224-226
Main Authors: Uchino, Keiichi, Katsumata, Yoko, Takeda, Tomoko, Arai, Hiroki, Shiraki, Mari, Saito, Terumi
Format: Article
Language:English
Subjects:
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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Description
Summary: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