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Results 1 - 10 of 29 > >>
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Reference
-999
-
more
stopped-flow kinetics of enzyme interaction with L-alanine and D-alanine, steady-state kinetics and thermodynamics
-999
-
more
the recombinant KAPA synthase obeys Michaelis-Menten kinetics with respect to pimeloyl-CoA and L-Ala
0.001
-
pimeloyl-CoA
-
0.0013
-
(S)-8-amino-7-oxononanoic acid
calculated from the competitive and uncompetitive constants and the substrate concentration determined in inhibitor experiments, 37°C, pH 8.6
0.0014
-
S-adenosyl-L-methionine
calculated from the competitive and uncompetitive constants and the substrate concentration determined in inhibitor experiments, 37°C, pH 8.6
0.0015
-
pimeloyl-CoA
-
0.0015
-
pimeloyl-CoA
pH 7.7, 25°C, recombinant enzyme
0.0016
-
pimeloyl-CoA
pH 7.5, 30°C, recombinant enzyme
0.002
-
L-alanine
-
0.01
-
pimeloyl-CoA
5-aminolevulinate synthase-fusion protein (single chain chimeric dimer), pH 7.5, 30°C
Results 1 - 10 of 29 > >>