Purification and properties of gamma-oxalomesaconate hydratase from Pseudomonas ochraceae grown with phthalate

Biochem Biophys Res Commun. 1985 Apr 16;128(1):271-7. doi: 10.1016/0006-291x(85)91674-2.


Pseudomonas ochraceae produced inducibly a hydro-lyase which catalyzes the reversible conversion of gamma-oxalomesaconate into (-)-gamma-oxalocitramalate. The enzyme has been purified to homogeneity from the bacteria grown with phthalate. The enzyme was a dimeric protein (pI=4.9) with a Mr of 68,000 and showed a high specificity for gamma-oxalomesaconate (Km=14 microM) and (-)-gamma-oxalocitramalate (Km=6.4 microM). Equilibrium constant for the hydration of gamma-oxalomesaconate at pH 8.0 and 24 degrees C was 2.5. Various thiols activated the enzyme.

MeSH terms

  • Bacterial Proteins*
  • Electrophoresis, Disc
  • Enzyme Induction
  • Hydro-Lyases / biosynthesis
  • Hydro-Lyases / isolation & purification*
  • Kinetics
  • Optical Rotation
  • Phthalic Acids / pharmacology*
  • Pseudomonas / enzymology*
  • Substrate Specificity


  • Bacterial Proteins
  • Phthalic Acids
  • phthalic acid
  • Hydro-Lyases
  • ligJ protein, Pseudomonas ochraceae