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Results 1 - 10 of 170 > >>
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Reference
-999
-
more
-
-999
-
more
kinetics analysis of wild-type and mutant enzymes, single and multiple turnover and stopped flow measurements, substrate protection study, overview
-999
-
more
Michaelis-Menten steady-state kinetics, overview
-999
-
more
Michaelis-Menten steady-state kinetics, two-step sequential kinetic mechanism , and thermodynamics. Both the reaction for wild-type hALAS2 and those for the X-linked protoporphyria variants comprised a single kinetic step associated with quinonoid intermediate formation followed by one decay step. Rates for the two steps range from 9.8-14.3/s and from 1.37-1.97 s for the reactions of the XLPP variants, whereas those for the wild-type hALAS2-catalyzed reaction are 6.6/s and 0.70/s
-999
-
more
overview
-999
-
more
pre-steady state and steady state kinetics, overview
-999
-
more
pre-steady-state and steady-state kinetics of wild-type and mutant enzymes, stopped-flow measurements, single and mutiple turnover rates, equilibrium dissociation constants, binding isotherms, detailed overview
0.00032
-
glycine
pH 7.5, 30°C, ALAS(K313A mutant)/ALAS
0.00045
-
glycine
pH 7.5, 30°C, ALAS/ALAS
0.00054
-
butanoyl-CoA
mutant R85L/T430V, pH 7.5, 30°C
Results 1 - 10 of 170 > >>