Cysteine synthase from rape leaves.
Cysteine synthase [O-Acetyl-L-serine acetate-lyase (adding hydrogen-sulfide) EC 4.2.99.8] has been highly purified from the extract of rape, Brassica chinensis var. Komatsuna. The purified preparation appeared to be homogeneous on Sephadex G-100 gel filtration and dodecylsulfate-polyacrylamide gel electrophoresis, showing a molecular weight of about 62,000. The latter method also suggested that this enzyme was composed of two identical subunits. The enzyme contained 2 moles of pyridoxal phosphate per mole of enzyme.
D002850:Chromatography, Gel; D003545:Cysteine; D007700:Kinetics; D008190:Lyases / Q000302:isolation & purification / Q000378:metabolism*; D046911:Macromolecular Substances; D008970:Molecular Weight; D010944:Plants / Q000201:enzymology; D011487:Protein Conformation; D011732:Pyridoxal Phosphate / Q000032:analysis; D012694:Serine / Q000031:analogs & derivatives / Q000378:metabolism; D013347:Subcellular Fractions / Q000201:enzymology
D046911:Macromolecular Substances; D012694:Serine; D011732:Pyridoxal Phosphate; D008190:Lyases; D003545:Cysteine