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Literature summary for 5.3.3.2 extracted from

  • Kittleman, W.; Thibodeaux, C.J.; Liu, Y.N.; Zhang, H.; Liu, H.W.
    Characterization and mechanistic studies of type II isopentenyl diphosphate:dimethylallyl diphosphate isomerase from Staphylococcus aureus (2007), Biochemistry, 46, 8401-8413.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.3.3.2

Inhibitors

Inhibitors Comment Organism Structure
O2 the overall reaction is sensitive to O2 Staphylococcus aureus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0048
-
 isopentenyl diphosphate aerobic, presence of NADPH, pH 7.0, 37°C Staphylococcus aureus
0.012
-
 isopentenyl diphosphate aerobic, presence of dithionite, pH 7.0, 37°C Staphylococcus aureus
0.0168
-
 isopentenyl diphosphate anaerobic, presence of NADPH, pH 7.0, 37°C Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
-
 type II enzyme
-
Staphylococcus aureus IDI-2
-
 type II enzyme
-

Renatured (Commentary)

Renatured (Comment) Organism
reconstitution of apo-enzyme with 5-deaza-FMN results in an inactive enzyme, whereas reconstitution with 1-deaza-FMN leads to full recovery of activity Staphylococcus aureus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
isopentenyl diphosphate
-
 Staphylococcus aureus dimethylallyl diphosphate
-
 ?
isopentenyl diphosphate
-
 Staphylococcus aureus IDI-2 dimethylallyl diphosphate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.065
-
 isopentenyl diphosphate aerobic, presence of NADPH, pH 7.0, 37°C Staphylococcus aureus
0.57
-
 isopentenyl diphosphate aerobic, presence of dithionite, pH 7.0, 37°C Staphylococcus aureus
0.69
-
 isopentenyl diphosphate anaerobic, presence of NADPH, pH 7.0, 37°C Staphylococcus aureus

Cofactor

Cofactor Comment Organism Structure
FMN FMN must be in reduced state to be catalytically active Staphylococcus aureus
NADPH needed only in catalytic amounts to activate the enzyme for multiple turnovers. Hydride transfer from NADPH to reduce FMN is pro-S stereospecific Staphylococcus aureus