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  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. (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.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0012-A4A2-6 Version Permalink: https://hdl.handle.net/21.11116/0000-0003-D1DA-B
Genre: Journal Article

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BOL047.pdf (Publisher version), 0B
 
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http://www.jbc.org/content/273/11/6248.abstract?sid=0a0fd8bb-6a36-47d8-80d8-f6f9c8d6a8b7 (Publisher version)
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 Creators:
Zhang, S., Author
Pohnert, G.1, Author           
Kongsaeree, P., Author
Wilson, D. B., Author
Clardy, J., Author
Ganem, B., Author
Affiliations:
1Department of Bioorganic Chemistry, MPI for Chemical Ecology, Max Planck Society, ou_24028              

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Free keywords: Nucleotide-sequence; phea-gene; phenylalanine; purification; conformation; quantities; mechanism; tyrosine; binding; nacl
 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

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 Dates: 1998
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: Other: BOL047
DOI: 10.1074/jbc.273.11.6248
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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 273 (11) Sequence Number: - Start / End Page: 6248 - 6253 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1