EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
---|
2.3.1.20 | -999 |
- |
more |
- |
486497 |
2.3.1.20 | -999 |
- |
more |
acyl-CoA substrate binding kinetics of the recombinant N-terminal fragment, overview |
672791 |
2.3.1.20 | -999 |
- |
more |
isozyme BnaC.DGAT1.a exhibits positive cooperativity. The folded section of the enzyme is important to maintain high acyl-CoA affinity at the active site and activity. Kinetics of wild-type and enzyme mutants, Michaelis-Menten kinetic model |
758047 |
2.3.1.20 | -999 |
- |
more |
kinetic analysis of lipidated BnaDGAT1. BnaDGAT1 exhibits cooperative substrate binding behavior with oleoyl-CoA |
758018 |
2.3.1.20 | -999 |
- |
more |
kinetics of wax synthase activity, overview |
756245 |
2.3.1.20 | -999 |
- |
more |
Michaelis-Menten kinetics |
757051, 757183 |
2.3.1.20 | -999 |
- |
more |
Michaelis-Menten or allosteric sigmoidal kinetics |
757545 |
2.3.1.20 | -999 |
- |
more |
the flux control coefficient is 0.12 in oil palm |
673535 |
2.3.1.20 | -999 |
- |
more |
the flux control coefficient is 0.74 in olive |
673535 |
2.3.1.20 | -999 |
- |
more |
the N-terminal regions of Brassica napus DGAT1 enzymes binds acyl-CoA in a sigmoidal fashion, suggesting positive cooperative binding |
757544 |