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Literature summary extracted from

  • Rauch, G.; Ehammer, H.; Bornemann, S.; Macheroux, P.
    Mutagenic analysis of an invariant aspartate residue in chorismate synthase supports its role as an active site base (2007), Biochemistry, 46, 3768-3774.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.3.5
-
Neurospora crassa

Protein Variants

EC Number Protein Variants Comment Organism
4.2.3.5 D367A comparable to the wild-type enzyme with respect to substrate and cofactor binding, but activity significantly lower Neurospora crassa
4.2.3.5 D367N comparable to the wild-type enzyme with respect to substrate and cofactor binding, but activity significantly lower Neurospora crassa

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.3.5 dioxygen inactivation Neurospora crassa

Organism

EC Number Organism UniProt Comment Textmining
4.2.3.5 Neurospora crassa
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.3.5 5-enolpyruvylshikimate 3-phosphate
-
Neurospora crassa chorismate + phosphate
-
?

Synonyms

EC Number Synonyms Comment Organism
4.2.3.5 chorismate synthase
-
Neurospora crassa

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.3.5 FMN essential for catalytic activity Neurospora crassa