EC Number   |
Metals/Ions |
Reference |
|---|
    2.1.1.5 | K+ |
Km value around 0.1 mM. The presence of potassium ions lowers the apparent KM of the enzyme for homocysteine, but it does not affect the apparent KM for betaine or the apparent kcat for either substrate |
735230 |
| 2.1.1.5 | Zinc |
wild-type enzyme contains zinc. Mutant enzymes H338A, R346A, W352A, R361A, P362A, Y363A, N364A, P365A maintain normal or near-normal ability to bind zinc |
657666 |
| 2.1.1.5 | Zn |
BHMT-2 is a zinc metalloenzyme |
687808 |
| 2.1.1.5 | Zn |
Tyr160 is coordinated to Zn |
659712 |
| 2.1.1.5 | Zn2+ |
- |
673003, 720202 |
| 2.1.1.5 | Zn2+ |
BHMT is a zinc metalloenzyme |
687808 |
| 2.1.1.5 | Zn2+ |
BHMT-2 is a zinc metalloenzyme |
687808 |
| 2.1.1.5 | Zn2+ |
removal of Zn2+ results in loss of activity, restoration is possible |
441241 |
| 2.1.1.5 | Zn2+ |
wild-type enzyme contains catalytic active zinc which is bound by three thiolates and one hydroxyl group. Long-term exposure of BHMT to reducing agent-free buffer results in the slow, irreversible loss of its catalytic Zn and a corresponding loss of activity |
684710 |
