Purification and molecular cloning of an intracellular 3-hydroxybutyrate-oligomer hydrolase from Paucimonas lemoignei

J Biosci Bioeng. 2007 Sep;104(3):224-6. doi: 10.1263/jbb.104.224.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3-Hydroxybutyric Acid / chemistry*
  • Burkholderia / enzymology*
  • Burkholderia / genetics
  • Cloning, Molecular / methods*
  • Dimerization
  • Enzyme Activation
  • Enzyme Stability
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Hydrolases / chemistry*
  • Hydrolases / genetics
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Substrate Specificity
  • Transfection / methods*

Substances

  • Recombinant Proteins
  • Hydrolases
  • 3-Hydroxybutyric Acid