O-acetylserine sulfhydrylase and S-sulfocysteine synthase activities of Chromatium vinosum |
| |
Authors: | Gabriele Hensel Hans G. Trüper |
| |
Affiliation: | (1) Institut für Mikrobiologie, Rheinische Friedrich-Wilhelms-Universität, Meckenheimer Allee 168, D-5300 Bonn 1, Federal Republic of Germany |
| |
Abstract: | Two proteins containing O-acetylserine sulfhydrylase activity were purified from Chromatium vinosum. Their separation was carried out by DE52 or Ecteola cellulose chromatography. While protein I with a molecular weight of 56,000 had only O-acetylserine sulfhydrylase activity, protein II with a molecular weight of 50,000 possessed S-sulfocysteine synthase activity in addition. It was not possible to separate the two activities of protein II by electrophoretic methods. The reaction rate of protein II with sulfide and O-acetylserine was twice as high as that with thiosulfate and O-acetylserine. When extracts of sulfate-grown cells were purified the major O-acetylserine activity was always associated with protein II. Regulatory and kinetic phenomena of the two activities were studied. |
| |
Keywords: | Chromatium vinosum Sulfur metabolism O-Acetylserine sulfhydrylase S-Sulfocysteine synthase Cysteine biosynthesis |
本文献已被 SpringerLink 等数据库收录! |