Literature summary extracted from
Rothman, S.C.; Helm, T.R.; Poulter, C.D.
Kinetic and spectroscopic characterization of type II isopentenyl diphosphate isomerase from Thermus thermophilus: evidence for formation of substrate-induced flavin species (2007), Biochemistry, 46, 5437-5445.
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
5.3.3.2 |
N,N-dimethyl-2-amino-1-ethyl diphosphate |
transition state analogue, competitive |
Thermus thermophilus |
|
KM Value [mM]
EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
---|
5.3.3.2 |
additional information |
- |
additional information |
substrate binds to the inactive oxidized and active reduced form of enzyme with similar affinities |
Thermus thermophilus |
|
5.3.3.2 |
0.0056 |
- |
isopentenyl diphosphate |
pH 7.0, 37°C |
Thermus thermophilus |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
5.3.3.2 |
Mg2+ |
Kd value is 0.13 mM at pH 7.0, 37°C |
Thermus thermophilus |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
5.3.3.2 |
Thermus thermophilus |
- |
type II enzyme, recombinant protein |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
5.3.3.2 |
recombinant protein, enzyme purified under aerobic conditions is inactive until the flavin cofactor is reduced by NADPH or dithionite or photochemically |
Thermus thermophilus |
Renatured (Commentary)
EC Number |
Renatured (Comment) |
Organism |
---|
5.3.3.2 |
enzyme purified under aerobic conditions is inactive until the flavin cofactor is reduced by NADPH or dithionite or photochemically |
Thermus thermophilus |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
5.3.3.2 |
isopentenyl diphosphate |
- |
Thermus thermophilus |
dimethylallyl diphosphate |
- |
? |
|
5.3.3.2 |
additional information |
substrate binds to the inactive oxidized and active reduced form of enzyme with similar affinities. Substrate-dependent accumulation of the neutral flavin semiquinone during both the flavoenzyme reduction and reoxidation processes |
Thermus thermophilus |
? |
- |
? |
|
Turnover Number [1/s]
EC Number |
Turnover Number Minimum [1/s] |
Turnover Number Maximum [1/s] |
Substrate |
Comment |
Organism |
Structure |
---|
5.3.3.2 |
17.9 |
- |
isopentenyl diphosphate |
pH 7.0, 37°C |
Thermus thermophilus |
|
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
5.3.3.2 |
FMN |
reduced flavin is required. The neutral semiquinone state of the flavin is stabilized thermodynamically relative to free FMN in solution. Kd value is 0.0047 mM at pH 7.0, 37°C |
Thermus thermophilus |
|
5.3.3.2 |
NADPH |
required for reductive activation of inactive oxidized enzyme. Kd value is 0.11 mM at pH 7.0, 37°C |
Thermus thermophilus |
|