EC Number |
Activating Compound |
Reference |
---|
4.2.1.28 | ATP |
- |
650799 |
4.2.1.28 | ATP |
absolutely required for the reactivation of the inactivated holoenzyme by the reactivating factor |
649870 |
4.2.1.28 | ATP |
needed for reactivation |
673603 |
4.2.1.28 | diol dehydratase-reactivating factor |
activates inactive enzymeCN-Cbl complexes, dimeric (alphabbeta) structurea large subunit of 64 kDa and a small subunit of 14 kDa |
673603 |
4.2.1.28 | diol dehydratase-reactivating factor |
activates inactive enzymeCN-Cbl complexes, dimeric (alphabeta) structurea large subunit of 64000 Da and a small subunit of 14000 Da |
673603 |
4.2.1.28 | diol dehydratase-reactivating factor |
both dehydratase-reactivating factors exist as alpha2beta2 heterotetramers, DdrA or GdrA and DdrB or GdrB, respectively. The diol dehydratase DD-reactivating factor reactivates the inactivated holoenzyme in the presence of ATP and Mg2+ by mediating the exchange of the tightly bound damaged cofactor for free intact coenzyme, overview. Mechanism of the reactivation of inactivated holoenzymes by reactivating factors, overview. The enzyme does not form a complex with the reactivating factor while it exists as an active holoenzyme. The reactivating factor binds ATP and hydrolyzes it to ADP by its own weak ATPase activity. The resulting ADP-bound form of the reactivating factor has a high affinity for the enzyme, and interacts with the inactivated holoenzyme to form a tight apoenzyme/reactivating factor complex, with the concomitant release of the damaged cofactor. The reactivating factor reverts to a low-affinity form through the replacement of bound ADP by free ATP, resulting in the dissociation of the apoenzyme/reactivating factor complex into apoenzyme and the reactivating factor, kinetics, overview |
714968 |
4.2.1.28 | dithiothreitol |
activates, 900% stimulation at 1 mM |
5628, 5636 |
4.2.1.28 | more |
ADP and ATP analogues are not able to substitute ATP significantly |
649870 |
4.2.1.28 | oxygen |
anaerobically no activity |
672269 |