Comments (originally from EcoCyc) 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.
- EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- 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
- 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
- Duggleby, RG et al. (1978) Chorismate mutase-prephenate dehydratase from Escherichia coli: active sites of a bifunctional enzyme. Biochemistry 17 1548-54 PubMed
- 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
- 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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