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Literature summary extracted from

  • Crehuet, R.; Field, M.J.
    A transition path sampling study of the reaction catalyzed by the enzyme chorismate mutase (2007), J. Phys. Chem. B, 111, 5708-5718.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.4.99.5 Performance of molecular dynamics simulations for the three enzyme-ligand complexes(CHOR,PRE and TSA) in addition to the TPS calculations. 8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid as a TSA. The principal component analysis (PCA) to analyze structures is used Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.4.99.5 Chorismate Bacillus subtilis
-
 Prephenate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.4.99.5 Bacillus subtilis P19080 There are four published structures of the Bacillus subtilis wild-type chroismate mutase (CM) with Protein Data Bank (PDB) codes 1COM, 2CHS, 2CHT, and 1DBF
-

Reaction

EC Number Reaction Comment Organism Reaction ID
5.4.99.5 Chorismate = prephenate The active site of the enzyme which is found in a pocket formed by two different chains is shown. Applying the TPS method of Chandler and co-workers to study the chorismate to prephenate reaction Bacillus subtilis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.99.5 Chorismate
-
 Bacillus subtilis Prephenate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
5.4.99.5 chorismate mutase
-
 Bacillus subtilis