Purification of chorismate synthase from a cell culture of the higher plant Corydalis sempervirens Pers.
Chorismate synthase (EC 4.6.1.4) was purified from a cell suspension culture of Corydalis sempervirens almost 1000-fold to near homogeneity. The subunit Mr estimated by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate was 41,900. The Mr of the native enzyme was estimated to be 80,100 by gel filtration, suggesting a dimeric structure. Antisera directed against the 41.9-kDa protein also reacted with the native enzyme. Further confirmation of the identity of the purified protein was obtained by sequence comparison of a tryptic peptide with known sequences of the Escherichia coli and Neurospora crassa chorismate synthases.
Schaller
A
A
Institute of Plant Sciences, Swiss Federal Institute of Technology, Zurich, Switzerland.
Windhofer
V
V
Amrhein
N
N
D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000201:enzymology; D007526:Isoelectric Point; D008190:Lyases / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009492:Neurospora crassa / Q000201:enzymology; D019761:Phosphorus-Oxygen Lyases; D010944:Plants / Q000201:enzymology*; D013045:Species Specificity
D008190:Lyases; C019895:chorismate synthase; D019761:Phosphorus-Oxygen Lyases