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Literature summary for 4.2.1.28 extracted from
- Mechanism of reactivation of coenzyme B12-dependent diol dehydratase by a molecular chaperone-like reactivating factor (1999), Biochemistry, 38, 13170-13178.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| ATP | absolutely required for the reactivation of the inactivated holoenzyme by the reactivating factor | Klebsiella oxytoca |  |
| additional information | ADP and ATP analogues are not able to substitute ATP significantly | Klebsiella oxytoca |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Klebsiella oxytoca |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Klebsiella oxytoca | - |
- |
- |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| coenzyme B12 | adenosylcobalamin. Glycerol-inactivated and oxygen inactivated enzyme undergoes rapid reactivation in the presence of the reactivating factor, the cofactor, ATP and Mg2+ | Klebsiella oxytoca | |
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