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Literature summary for 5.4.99.5 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)

Cloned (Comment) Organism
expression in Escherichia coli Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment) Organism
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Chorismate Bacillus subtilis biosynthesis of aromatic amino acids Prephenate
-
?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P19080
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-

Purification (Commentary)

Purification (Comment) Organism
-
Bacillus subtilis

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
trimer alpha3, crystallization studies Bacillus subtilis

Synonyms

Synonyms Comment Organism
chorismate mutase
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Bacillus subtilis