Mapping of chorismate mutase and prephenate dehydrogenase domains in the Escherichia coli T-protein
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1046/j.1432-1033.2003.03438.x/fullpdf
Reference22 articles.
1. Characterisation of the subunits of chorismate mutase-prephenate dehydrogenase from E. coli K12;Koch;Biochim. Biophys. Acta,1971
2. The binding of tyrosine and NAD+ to chorismate mutase/prephenate dehydrogenase from Escherichia coli K12 and the effects of these ligands on the activity and self association of the enzyme;Hudson;J. Biol. Chem.,1983
3. Regulation of phenylalanine biosynthesis. Calorimetric studies on the E. coli P-protein and its regulatory domain;Pohnert;Biochemistry,1999
4. Chorismate mutase-prephenate dehydratase from Escherichia coli: study of catalytic and regulatory domains using genetically engineered proteins;Zhang;J. Biol. Chem.,1998
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