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Literature summary for 5.3.3.2 extracted from

  • Thibodeaux, C.J.; Chang, W.C.; Liu, H.W.
    Linear free energy relationships demonstrate a catalytic role for the flavin mononucleotide coenzyme of the type II isopentenyl diphosphate:dimethylallyl diphosphate isomerase (2010), J. Am. Chem. Soc., 132, 9994-9996.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
Q154N active site mutant Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
isopentenyl diphosphate
-
Staphylococcus aureus dimethylallyl diphosphate
-
r

Synonyms

Synonyms Comment Organism
Idi-2
-
Staphylococcus aureus
type II isopentenyl diphosphate:dimethylallyl diphosphate isomerase
-
Staphylococcus aureus

Cofactor

Cofactor Comment Organism Structure
FMN the reduced FMN coenzyme of IDI-2 functions as an acid/base catalyst, with the N5 atom of the flavin likely playing a critical role in the deprotonation of isopentenyl diphosphate en route to dimethylallyl diphosphate formation Staphylococcus aureus