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Literature summary extracted from

  • Vamvaca, K.; Jelesarov, I.; Hilvert, D.
    Kinetics and thermodynamics of ligand binding to a molten globular enzyme and its native counterpart (2008), J. Mol. Biol., 382, 971-977.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.99.5 expressed in Escherichia coli Methanocaldococcus jannaschii

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.4.99.5 prephenate
-
Methanocaldococcus jannaschii

Organism

EC Number Organism UniProt Comment Textmining
5.4.99.5 Methanocaldococcus jannaschii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.99.5
-
Methanocaldococcus jannaschii

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
5.4.99.5 dimer the dimeric chorismate mutase is a thermostable and conventionally folded enzyme, X-ray chrystallography Methanocaldococcus jannaschii
5.4.99.5 monomer monomeric chorismate mutase combines high catalytic activity with the characteristics of a molten globule, X-ray crystallography Methanocaldococcus jannaschii

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
5.4.99.5 0.07
-
prephenate dimeric chorismate mutase, at 20°C Methanocaldococcus jannaschii
5.4.99.5 0.17
-
prephenate monomeric chorismate mutase, at 20°C Methanocaldococcus jannaschii