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0.0013 - 0.388
(+)-Camphor
0.086
(R)-2-ethylhexanol
-
-
0.068
(S)-2-ethylhexanol
-
-
0.0024 - 0.0559
1-Methylimidazole
0.0046 - 0.44
3-chloroindole
additional information
additional information
-
0.0013
(+)-Camphor
recombinant wild-type enzyme
0.0016
(+)-Camphor
recombinant mutant L244A/C334A
0.03
(+)-Camphor
wild-type
0.096
(+)-Camphor
mutant T252N
0.388
(+)-Camphor
mutant T252N/V253T
0.0024
1-Methylimidazole
recombinant wild-type enzyme
0.0559
1-Methylimidazole
recombinant mutant L244A/C334A
0.0046
3-chloroindole
mutant G120A/Y179H/G248S/D297H, pH 7.4, temperature not specified in the publication
0.016
3-chloroindole
mutant T56A/N116H/D297N, pH 7.4, temperature not specified in the publication
0.026
3-chloroindole
mutant Y179H, pH 7.4, temperature not specified in the publication
0.041
3-chloroindole
mutant G60S/Y75H, pH 7.4, temperature not specified in the publication
0.09
3-chloroindole
mutant D97F/P122L/Q183L/L244Q, pH 7.4, temperature not specified in the publication
0.15
3-chloroindole
mutant G93C/K314R/L319M, pH 7.4, temperature not specified in the publication
0.44
3-chloroindole
mutant E156G/V247F/V253G/F256S, pH 7.4, temperature not specified in the publication
0.0075
imidazole
recombinant wild-type enzyme
0.3
imidazole
recombinant mutant L244A/C334A
0.077
O2
-
recombinant enzyme with His6-tag, pH 7.4, 25°C
0.083
O2
-
wild-type, pH 7.4, 25°C
additional information
additional information
kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
Km-value of putidaredoxin, 0.0038 mM, steady-state kinetics of enzyme interaction with redox partners
-
additional information
additional information
combined quantum mechanical/molecular mechanical study, molecular dynamics, overview
-
additional information
additional information
-
development of a global data fitting kinetic model that describes the time-varying concentrations of substrate and products, Michaelis-Menten kinetics
-
additional information
additional information
-
EPR/ENDOR studies of wild-type and mutant T252A enzymes
-
additional information
additional information
-
equilibrium isotope effect on O2 binding, isotope effects and transient-state kinetics, electron transfer kinetics, steady-state kinetics, recombinant His6-tagged enzyme, overview
-
additional information
additional information
-
single turnover kinetics
-
additional information
additional information
spectroscopic and stopped flow transient kinetic studies
-
additional information
additional information
stopped-flow kinetic analysis of the peracid oxidation of the wild-type enzyme and substrate-free ferric mutant enzymes overview
-
additional information
additional information
-
stopped-flow kinetics at different pH and temperature
-
additional information
additional information
-
stopped-flow kinetics of the reaction between putidaredoxin with 1,3-dimethoxy-5-methyl-1,4-benzoquinone, kinetics of the first and the second electron transfer to P450cam of wild-type and mutant enzymes
-
additional information
additional information
thermal unfolding kinetics, substrate binding kinetics
-
additional information
additional information
-
steady-state turnover activities of the P450cam catalytic cycle, overview
-
additional information
additional information
detailed comparative pre-steady-state kinetic and steady-state analysis of enzyme mutant SeP450cam C357U/R365L/E366Q and its the cysteine-containing wild-type, overview
-
additional information
additional information
enzyme-cofactor interaction kinetics of wild-type and mutant enzymes, steady-state and stopped-flow reaction kinetics, overview
-
additional information
additional information
interaction thermodynamics between Pdx and various states of P450cam constrained in different conformations, overview
-
additional information
additional information
thermodynamics of wild-type and mutant enzymes with different substrates, overview
-