Abstract
Summary Cysteine synthase (O-acetyl-L-serine sulfhydrolase; EC 4.2.99.9) was isolated from the cyanobacterium Synechococcus 6301. Isoenzymes could be separated by DEAE-cellulose chromatography and by electrophoretic separation on disc gels and by carrier-free electrophoresis. Both enzymes had a molecular weight of 56,000, a pH optimum of 7.5, and a temperature optimum of 50 °C. K m -values for both isoenzymes were found to be around 0.8 mM for sulfide and 0.7 mM for O-acetyl-L-serine. Both isoenzymes catalyzed an isotopic exchange reaction between cysteine and sulfide with pH optima around 9. A model for the cysteine synthase reaction is presented.
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