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Literature summary for 4.2.3.5 extracted from

  • Ahn, H.J.; Yoon, H.J.; Lee, B.2nd.; Suh, S.W.
    Crystal structure of chorismate synthase: a novel FMN-binding protein fold and functional insights (2004), J. Mol. Biol., 336, 903-915.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of chorismate synthase in both FMN-bound and FMN-free form. It is a tetrameric enzyme, with each monomer possessing a novel beta-alpha-beta sandwich fold Helicobacter pylori

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
O5-(1-carboxyvinyl)-3-phosphoshikimate Helicobacter pylori
-
chorismate + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Helicobacter pylori P56122
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
O5-(1-carboxyvinyl)-3-phosphoshikimate
-
Helicobacter pylori chorismate + phosphate
-
?

Cofactor

Cofactor Comment Organism Structure
FMNH2 required. The unique FMN-binding site is formed largely by a single subunit, with a small contribution from a neighboring subunit. The isoalloxazine ring of the bound FMN is significantly non-planar Helicobacter pylori