EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    2.3.1.87 | -999 |
- |
more |
AANAT2 kinetic constants as a function of temperature, overview |
720470 |
| 2.3.1.87 | -999 |
- |
more |
AANAT2 kinetics in relation to temperature, overview |
720470 |
| 2.3.1.87 | -999 |
- |
more |
apparent Km-values |
487622 |
| 2.3.1.87 | -999 |
- |
more |
both isoforms Aanat1a and Aanat1b display 2- to 3fold lower KM values for indolethylamines compared to phenylethylamines. KM for phenylethylamines is around two times lower for Aanat1a than for Aanat1b |
736685 |
| 2.3.1.87 | -999 |
- |
more |
exposing chickens to light in the middle of the night increased the apparent Km of AANAT for tryptamine by about 10fold. The Km began to increase within 5 min of exposure to light and reached a maximum at about 30 min |
675544 |
| 2.3.1.87 | -999 |
- |
more |
formation and cleavage of a disulfide bond produce active/inactive states of enzyme |
487641 |
| 2.3.1.87 | -999 |
- |
more |
kinetics of recombinant partially phosphorylated wild-type and mutant enzymes, overview |
702214 |
| 2.3.1.87 | -999 |
- |
more |
kinetics of recombinant wild-type and mutant enzymes, substrate tryptamine, overview |
704421 |
| 2.3.1.87 | -999 |
- |
more |
Michaelis-Menten kinetic analysis |
719595 |
| 2.3.1.87 | 0.00031 |
- |
acetyl-CoA |
- |
673165, 686212 |
