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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.
    View publication on PubMedView publication on EuropePMC

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