EC Number   |
Cofactor |
Reference |
|---|
   4.3.1.7 | adenosylcobalamin |
- |
661707, 680355, 680364, 682751, 704316, 704362, 729253 |
| 4.3.1.7 | adenosylcobalamin |
dependent on |
34374, 34381, 34384, 661191 |
| 4.3.1.7 | adenosylcobalamin |
Km 0.0005 mM |
34384 |
| 4.3.1.7 | adenosylcobalamin |
marked angular strains and tensile forces induced by tight enzyme-coenzyme interactions are responsible for breaking the coenzyme-Co-C bond. A major structural change upon substrate binding is not observed with this particular enzyme. Glu287, one of the substrate-binding residues, has a direct contact with the ribose group of the modeled adenosylcobalamin, which may contribute to the substrate-induced additional labilization of the Co-C bond |
715530 |
| 4.3.1.7 | adenosylcobalamin |
pulsed-laser photolysis of substrate-triggered cleavage of the cobalt-carbon bond and formation of the cob(II)alamin-5'-deoxyadenosyl radical pair in the adenosylcobalamin-dependent ethanolamine ammonia-lyase. Visible absorption spectra of holo-ethanolamine ammonia-lyase and ternary complex are comparable, indicating that the binding of substrate does not labilize the cofactor cobalt-carbon bond by significantly distorting the equilibrium structure. Following the substrate trigger, the protein interacts with the cofactor to contiguously guide the cleavage of the Co-C bond, at every step along the cleavage coordinate, starting from the equilibrium configuration of the ternary complex. The cleavage is represented by a diagonal trajectory across a free energy surface, that is defined by chemical, Co-C separation, and protein configuration coordinates |
715302 |
| 4.3.1.7 | adenosylcobalamin |
the holoenzyme of adenosylcobalamin-dependent ethanolamine ammonia lyase undergoes suicidal inactivation during catalysis as well as inactivation in the absence of substrate. The inactivation involves the irreversible cleavage of the Co-C bond of the coenzyme. Inactivated holoenzyme undergoes rapid and continuous reactivation in the presence of ATP, Mg2+ and free adensosylcobalamin. EutA is essential for reactivation. Reactivation and activation occur through the exchange of modified coenzyme for free intact adenosylcobalamin |
662021 |
| 4.3.1.7 | adenosylcobalamin |
vitamine B12 coenzyme |
692739 |
| 4.3.1.7 | cobamide |
5,6-dimethylbenzimidazolylcobamide coenzyme, Km: 0.00082 mM, and benzimidazolylcobamide, Km: 0.0004 mM, are active as cofactors |
34376 |
| 4.3.1.7 | cobamide |
dependent on |
34370, 34375 |
| 4.3.1.7 | cobamide |
Km-value for alpha-(5,6-dimethylbenzimidazolyl)cobamide coenzyme: 0.0015 mM, Km-value for alpha-(benzimidazolyl)cobamide coenzyme: 0.00019 mM, Km-value for alpha-(adenylyl)cobamide coenzyme: 0.00077 mM |
34375 |
