Category:Complex:CHORISMUTPREPHENDEHYDRAT-CPLX

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Comments (originally from EcoCyc[1][2]) The N-terminal end of this bifunctional protein specifies the chorismate mutase activity while the remainder of the sequence specifies the second enzymatic activity, prephenate dehydratase. The native enzyme is a dimer of identical subunits each containing a dehydratase active site, a mutase active site and a phenylalanine binding site.[3][4][5][6][7]


References

  1. ↑ EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  2. ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ Gething, MJ & Davidson, BE (1977) Chorismate mutase/prephenate dehydratase from Escherichia coli K12. Effects of chemical modification on the enzymic activities and allosteric inhibition. Eur. J. Biochem. 78 111-7 PubMed
  4. ↑ Hudson, GS et al. (1984) Chorismate mutase/prephenate dehydrogenase from Escherichia coli K12: purification, characterization, and identification of a reactive cysteine. Biochemistry 23 6240-9 PubMed
  5. ↑ Duggleby, RG et al. (1978) Chorismate mutase-prephenate dehydratase from Escherichia coli: active sites of a bifunctional enzyme. Biochemistry 17 1548-54 PubMed
  6. ↑ Baldwin, GS & Davidson, BE (1983) Kinetic studies on the mechanism of chorismate mutase/prephenate dehydratase from Escherichia coli K12. Biochim. Biophys. Acta 742 374-83 PubMed
  7. ↑ Gething, MJ & Davidson, BE (1977) Chorismate mutase/prephenate dehydratase from Escherichia coli K12. Modification with 5,5'-dithio-bis(2-nitrobenzoic acid). Eur. J. Biochem. 78 103-10 PubMed

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