Purification and properties of gamma-oxalomesaconate hydratase from Pseudomonas ochraceae grown with phthalate.
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.
D001426:Bacterial Proteins; D004589:Electrophoresis, Disc; D004790:Enzyme Induction; D006836:Hydro-Lyases / Q000096:biosynthesis / Q000302:isolation & purification*; D007700:Kinetics; D009904:Optical Rotation; D010795:Phthalic Acids / Q000494:pharmacology*; D011549:Pseudomonas / Q000201:enzymology*; D013379:Substrate Specificity
D001426:Bacterial Proteins; D010795:Phthalic Acids; C032279:phthalic acid; D006836:Hydro-Lyases; C045057:ligJ protein, Pseudomonas ochraceae