EC Number   |
Cofactor |
Reference |
|---|
    5.4.99.1 | 5'-deoxyadenosylcobalamin |
dependent on |
728191 |
| 5.4.99.1 | 5'-deoxyadenosylcobalamin |
i.e. coenzyme B12, required for activity |
714983 |
| 5.4.99.1 | adenosylcobalamin |
- |
716014, 716116 |
| 5.4.99.1 | adenosylcobalamin |
dependent on |
692318, 702376 |
| 5.4.99.1 | adenosylcobalamin |
dependent on, binding structure, modeling, overview |
727661 |
| 5.4.99.1 | adenosylcobalamin |
enzyme is dependent on, KM for wild-type enzyme is 0.0055 mM |
650824 |
| 5.4.99.1 | adenosylcobalamin |
investigation of photolysis by transient absorption spectroscopy. Metal-to-ligand charge transfer intermediate decays to form cob(II)alamin with a time constand of 105 ps |
662705 |
| 5.4.99.1 | adenosylcobalamin |
kinetics of homolysis and recombination, ultrafast spectroscopic experiments, no significant activation of coenzyme in absence of substrate |
661930 |
| 5.4.99.1 | adenosylcobalamin |
Km-value for wild-type enzyme is 0.005 mM. No cob(II)alamin detected in UV-visible spectrum of mutant enzymes R100M and R100Y. In mutant enzyme R100K cob(II)alamin accumulates to a concentration similar to that of the wild-type enzyme, homolysis of the coenzyme is slower by an order of magnitude, compared to wild-type enzyme. Mutant does not exhibit the very large deuterium isotope effects that are observed for homolysis of the coenzyme when the wild-type enzyme is reacted with deuterated substrates |
650247 |
| 5.4.99.1 | adenosylcobalamin |
study of Co-C bond activation, cofactor/active site interactions give rise to a fairly uniform stabilization of the Co 3d orbitals |
661176 |
