Literature summary for 5.3.3.2 extracted from

Hemmi, H.; Ikeda, Y.; Yamashita, S.; Nakayama, T.; Nishino, T.
Catalytic mechanism of type 2 isopentenyl diphosphate:dimethylallyl diphosphate isomerase: verification of a redox role of the flavin cofactor in a reaction with no net redox change (2004), Biochem. Biophys. Res. Commun., 322, 905-910.

Search for more literature for 5.3.3.2

Inhibitors

Inhibitors	Comment	Organism	Structure
5-deaza-FMN	-	Saccharolobus shibatae

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0841	-	isopentenyl diphosphate	pH 6.0	Saccharolobus shibatae

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Saccharolobus shibatae

Organism

Organism	UniProt	Comment	Textmining
Saccharolobus shibatae	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Saccharolobus shibatae

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
isopentenyl diphosphate	-	Saccharolobus shibatae	dimethylallyl diphosphate	-	?

Synonyms

Synonyms	Comment	Organism
IDI	-	Saccharolobus shibatae

Cofactor

Cofactor	Comment	Organism	Structure
FMN	nearly no activity with the flavin analogue 5-deazaFMN	Saccharolobus shibatae
additional information	IDI showed almost the same activity in the presence of NADH or dithionite. Data indicate that the reduced form of FMN is sufficient	Saccharolobus shibatae
NAD(P)H	proposed mechanism: reduction of FMN	Saccharolobus shibatae

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.00013	-	5-deaza-FMN	-	Saccharolobus shibatae

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Release 2023.1 (January 2023)