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Literature summary 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

EC Number Protein Variants Comment Organism
5.3.3.2 Q154N active site mutant Staphylococcus aureus

Organism

EC Number Organism UniProt Comment Textmining
5.3.3.2 Staphylococcus aureus
-
-
-

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

EC Number Cofactor Comment Organism Structure
5.3.3.2 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