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EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Reference
2.3.1.23
-999
-
more
-
486618
,
486623
2.3.1.23
-999
-
more
enzyme kinetics
755989
2.3.1.23
-999
-
more
kinetic data of soluble and liposome-bound enzyme
486624
2.3.1.23
-999
-
more
kinetic study
486625
2.3.1.23
-999
-
more
kinetics
674602
2.3.1.23
-999
-
more
Km of NBD-lyso-PC and arachidonoyl CoA by the model of Bi-Bi reaction under optimal conditions. The theoretical Km values calculated by Bi-Bi kinetic equations are more accurate than that calculated by the Michaelis-Menten equation because the apparent Km of one substrate calculated by the Michaelis-Menten equation may be influenced by the concentration of another, whereas Bi-Bi kinetic equations could overcome this disadvantage. From the Lineweaver-Burk plots, a sequential kinetic mechanism can be proposed, but only a sequential Bi-Bi kinetic mechanism can be infered
756737
2.3.1.23
0.00045
-
oleoyl-CoA
Vmax: 7.4 pmol/min/microgram protein for oleoyl-CoA
688774
2.3.1.23
0.00105
0.0057
acyl-CoA
saturated and unsaturated acyl donors, human platelets
486621
2.3.1.23
0.0012
-
oleoyl-CoA
at 20°C
486613
2.3.1.23
0.0017
-
1-acyl-sn-glycero-3-phosphocholine
-
486647
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