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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)
Catalyzes the interconversion of chorismate to prephenate
gamma subclass chorismate mutase AroQ
This exported chorismate mutase, as found in Mycobacterium tuberculosis, belongs to the gamma subclass of the AroQ type.
chorismate mutase catalyzes the interconversion of chorismate to prephenate
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