maleylpyruvate and maleic-acid

HbzF from Pseudomonas alcaligenes NCIMB 9867 was purified to homogeneity as a His-tagged protein and likely a dimer by SDS-PAGE and gel filtration. This protein was demonstrated to be a novel maleylpyruvate hydrolase, catalyzing direct hydrolysis of maleylpyruvate to maleate and pyruvate, and belongs to the fumarylacetoacetate hydrolase superfamily. This study reveals the genetic determinate for the direct maleylpyruvate hydrolysis in the gentisate pathway, complementary to the well-studied maleylpyruvate isomerization route.

Topics: Chromatography, Gel; DNA, Bacterial; Electrophoresis, Polyacrylamide Gel; Hydrolases; Hydrolysis; Maleates; Metabolic Networks and Pathways; Molecular Sequence Data; Molecular Weight; Pimelic Acids; Protein Multimerization; Pseudomonas alcaligenes; Pyruvic Acid; Sequence Analysis, DNA