Protein Family Models

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)

Date:

2024-08-14

chorismate mutase catalyzes the interconversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis

Date:

2019-05-16

This model represents one of two separate clades of the chorismate mutase domain of the gamma and beta and epsilon proteobacterial "P-protein" which contains an N-terminal chorismate mutase domain and a C-terminal prephenate dehydratase domain. It is also found in Aquifex aolicus.

Gene:

pheA

Date:

2024-05-30