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Literature summary for 5.3.3.2 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

Inhibitors Comment Organism Structure
N,N-dimethyl-2-amino-1-ethyl diphosphate transition state analogue, competitive Thermus thermophilus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information substrate binds to the inactive oxidized and active reduced form of enzyme with similar affinities Thermus thermophilus
0.0056
-
isopentenyl diphosphate pH 7.0, 37°C Thermus thermophilus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ Kd value is 0.13 mM at pH 7.0, 37°C Thermus thermophilus

Organism

Organism UniProt Comment Textmining
Thermus thermophilus
-
type II enzyme, recombinant protein
-

Purification (Commentary)

Purification (Comment) Organism
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)

Renatured (Comment) Organism
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
isopentenyl diphosphate
-
Thermus thermophilus dimethylallyl diphosphate
-
?
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]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
17.9
-
isopentenyl diphosphate pH 7.0, 37°C Thermus thermophilus

Cofactor

Cofactor Comment Organism Structure
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
NADPH required for reductive activation of inactive oxidized enzyme. Kd value is 0.11 mM at pH 7.0, 37°C Thermus thermophilus