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EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Reference
6.3.2.12
-999
-
more
non-standard kinetics at high glutamate and ATP concentrations, being partially inhibited by increasing concentrations of its principal substrate, dihydropteroate. Binding of dihydropteroate to the catalytic and inhibitory sites exhibits dissociation constants of 0.50 microM and 1.25 microM, respectively. Under lower co-substrate concentrations, data fit the Michaelis-Menten equation
705610
6.3.2.12
0.00025
-
7,8-dihydropteroate
with addition of 100 mM K+
1015
6.3.2.12
0.0006
-
7,8-dihydropteroate
-
1006
6.3.2.12
0.00088
-
dihydropteroate
-
705610
6.3.2.12
0.00088
-
dihydropteroate
pH 10.0, 37°C
705610
6.3.2.12
0.001
-
7,8-dihydropteroate
-
1019
6.3.2.12
0.0012
-
7,8-dihydropteroate
-
1008
6.3.2.12
0.0013
-
7,8-dihydropteroate
with addition of 7.5 mM K+
1015
6.3.2.12
0.0029
-
ATP
-
1005
6.3.2.12
0.00597
-
glutamate
-
705610
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