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Literature summary extracted from

  • Ladner, J.E.; Reddy, P.; Davis, A.; Tordova, M.; Howard, A.J.; Gilliland, G.L.
    The 1.30 A resolution structure of the Bacillus subtilis chorismate mutase catalytic homotrimer (2000), Acta Crystallogr. Sect. D, 56, 673-683.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.99.5 expression in Escherichia coli Bacillus subtilis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.4.99.5 hanging drop vapor-diffusion method at room temperature and high ionic strength, orthorhombic space group P212121 with a: 52.2 A, b: 83.8 A, c: 86.0 A, nine sulfate ions, five glycerol molecules, 424 water molecules 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 biosynthesis of aromatic amino acids Prephenate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.4.99.5 Bacillus subtilis P19080
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.99.5
-
 Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.99.5 Chorismate
-
 Bacillus subtilis Prephenate
-
 ?
5.4.99.5 Chorismate biosynthesis of aromatic amino acids Bacillus subtilis Prephenate
-
 ?

Subunits

EC Number Subunits Comment Organism
5.4.99.5 trimer alpha3, crystallization studies Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
5.4.99.5 chorismate mutase
-
 Bacillus subtilis