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

Zhang, S.; Pohnert, G.; Kongsaeree, P.; Wilson, D. B.; Clardy, J.; Ganem, B.

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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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http://www.jbc.org/content/273/11/6248.abstract?sid=0a0fd8bb-6a36-47d8-80d8-f6f9c8d6a8b7
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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.

Cite as: https://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