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Literature summary for 5.4.99.5 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)

Cloned (Comment) Organism
expressed in Escherichia coli Methanocaldococcus jannaschii

Inhibitors

Inhibitors Comment Organism Structure
prephenate
-
Methanocaldococcus jannaschii

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Methanocaldococcus jannaschii

Substrates and Products (Substrate)

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

Subunits

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

Ki Value [mM]

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