Purification and characterization of O-acetylserine sulfhydrylase of Corynebacterium glutamicum

We highly purified O-acetylserine sulfhydrylase from the glutamate-producing bacterium Corynebacterium glutamicum. The molecular mass of the purified enzyme was 34,500 as determined by SDS-polyacrylamide gel electrophoresis, and 70,800 as determined by gel filtration chromatography. It had an apparent Km of 7.0 mM for O-acetylserine and a Vmax of 435micro mol/min/mg protein. This is the first report of the cysteine biosynthetic enzyme of C. glutamicum in purified form.