Two components of chorismate mutase in Brevibacterium flavum.

@article{Shiio1979TwoCO,
  title={Two components of chorismate mutase in Brevibacterium flavum.},
  author={I Shiio and Shinji Sugimoto},
  journal={Journal of biochemistry},
  year={1979},
  volume={86 1},
  pages={17-25}
}
Chorismate mutase of Brevibacterium flavum, a common enzyme in phenylalanine and tyrosine biosynthesis, was separted into two different component, A and B, with molecular weights of 250,000 and 25,000, respectively, by ammonium sulfate fractionation or gel-filtration. Both components were essential for the enzymatic activity. In the presence of the reaction substrate, chorismate, the two components associated reversibly to give an active enzyme complex with a molecular weight of 320,000… CONTINUE READING

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