The β1 domain of protein G can replace the chorismate mutase domain of the T-protein
Author:
Funder
PAPIIT
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/j.febslet.2012.01.033/fullpdf
Reference19 articles.
1. Cohesion group approach for evolutionary analysis of TyrA, a protein family with wide-ranging substrate specificities;Bonner;Microbiol. Mol. Biol. Rev.,2008
2. Mapping of chorismate mutase and prephenate dehydrogenase domains in the Escherichia coli T-protein;Chen;Eur. J. Biochem.,2003
3. The structure of Haemophilus influenzae prephenate dehydrogenase suggests unique features of bifunctional TyrA enzymes;Chiu;Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun.,2010
4. Chorismate mutase-prephenate dehydrogenase from Escherichia coli: cooperative effects and inhibition by l-tyrosine;Christopherson;Arch. Biochem. Biophys.,1985
5. Identifying groups involved in the binding of prephenate to prephenate dehydrogenase from Escherichia coli;Christendat;Biochemistry,1999
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