The prephenate dehydrogenase component of the bifunctional T-protein in enteric bacteria can utilize L-arogenate
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(87)80771-8/fullpdf
Reference18 articles.
1. The biosynthesis of phenylalanine and tyrosine; enzymes converting chorismic acid into prephenic acid and their relationships to prephenate dehydratase and prephenate dehydrogenase
2. The evolutionary history of two bifunctional proteins that emerged in the purple bacteria
3. Chorismate Mutase-Prephenate Dehydratase from Escherichia coli K-12
4. Chorismate mutase/prephenate dehydrogenase from Escherichia coli K12: purification, characterization, and identification of a reactive cysteine
5. Tyrosine biosynthesis in aerobacter aerogenes: Purification and properties of chorismate mutase-prephenate dehydrogenase
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