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Chorismate mutase-prephenate dehydratase from Escherichia coli - Study of catalytic and regulatory domains using genetically engineered proteins

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Pohnert,  G.
Department of Bioorganic Chemistry, MPI for Chemical Ecology, Max Planck Society;

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Citation

Zhang, S., Pohnert, G., Kongsaeree, P., Wilson, D. B., Clardy, J., & Ganem, B. (1998). Chorismate mutase-prephenate dehydratase from Escherichia coli - Study of catalytic and regulatory domains using genetically engineered proteins. The Journal of Biological Chemistry, 273(11), 6248-6253. doi:10.1074/jbc.273.11.6248.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-A4A2-6
Abstract
The bifunctional P-protein, which plays a central role in Escherichia coli phenylalanine biosynthesis, contains two catalytic domains (chorismate mutase and prephenate dehydratase activities) as well as one R-domain (for feedback inhibition by phenylala