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chorismate mutase
Chorismate mutase EC:5.4.99.5 catalyses the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. This enzyme is negatively regulated by tyrosine, tryptophan and phenylalanine [2,3]. [1]. 7971967. The crystal structure of allosteric chorismate mutase at 2.2-A resolution. Xue Y, Lipscomb WN, Graf R, Schnappauf G, Braus G;. Proc Natl Acad Sci U S A 1994;91:10814-10818. [2]. 9642265. Tyrosine and tryptophan act through the same binding site at the dimer interface of yeast chorismate mutase. Schnappauf G, Krappmann S, Braus GH;. J Biol Chem 1998;273:17012-17017. [3]. 9497350. Chorismate mutase-prephenate dehydratase from Escherichia coli. Study of catalytic and regulatory domains using genetically engineered proteins. Zhang S, Pohnert G, Kongsaeree P, Wilson DB, Clardy J, Ganem B;. J Biol Chem 1998;273:6248-6253. (from Pfam)
prephenate dehydratase domain-containing protein
This protein is involved in Phenylalanine biosynthesis. This protein catalyses the decarboxylation of prephenate to phenylpyruvate. (from Pfam)
prephenate dehydratase
Catalyzes the formation of phenylpyruvate from prephenate in phenylalanine biosynthesis
This model represents the chorismate mutase domain of the gamma and beta proteobacterial "P-protein" which contains an N-terminal chorismate mutase domain and a C-terminal prephenate dehydratase domain.
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