EC Number   |
Cofactor |
Reference |
|---|
    5.4.99.2 | 5'-deoxyadenosylcobalamin |
P-loop GTPase MeaB increases affinity of the mutase for cofactor twofold, in presence of MeaB and GDP, affinity decreases fivifold |
678210 |
| 5.4.99.2 | 5'-deoxyadenosylcobalamin |
the 5'-deoxyadenosyl vitamin B12 orAdoCbl, methylmalonyl-CoA mutase (MCM) requires 5'-deoxyadenosylcobalamin as a cofactor |
747314 |
| 5.4.99.2 | 5'-deoxyadenosylcobalamin |
the apoenzyme is converted to a holoenzyme by incubation for 4 h at 4°C with 0.01 mM 5'-deoxyadenosylcobalamin, the purified enzyme contains one mole of prosthetic 5'-deoxyadenosylcobalamin per mole of subunit |
701956 |
| 5.4.99.2 | adenosylcobalamin |
- |
3514, 649513, 649878, 649904, 649999, 650005, 652093, 652252, 652521, 662325, 690428, 704291, 704957, 705936, 715560, 716097 |
| 5.4.99.2 | adenosylcobalamin |
active form of vitamin B12 |
746727 |
| 5.4.99.2 | adenosylcobalamin |
AdoCbl, dependent on |
747783 |
| 5.4.99.2 | adenosylcobalamin |
AdoCbl, the enzyme converts methylmalonyl-CoA to succinyl-CoA employing highly reactive radicals from its cofactor adenosylcobalamin to perform its reaction. Formation and accumulation of OH2Cbl, the oxidized form of the AdoCbl cofactor formed during catalysis, is the cause of hMCM inactivation. GTPase hMMAA is able to remove the damaged cofactor through GTP hydrolysis |
747209 |
| 5.4.99.2 | adenosylcobalamin |
binding analysis with recombinant wild-type and mutant enzymes, overview |
727036 |
| 5.4.99.2 | adenosylcobalamin |
dependent on |
692859, 694024, 726874, 727246 |
| 5.4.99.2 | adenosylcobalamin |
dependent on adenosylcobalamin as prosthetic group, under cobalamin-deficient conditions, (R)-2-methylmalonyl-CoA and its precursor, propionyl-CoA, increase as a result of a decrease in the catalytic activity of MCM due to deficiency of adenosylcobalamin |
691535 |
