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Literature summary 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
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.28 | ATP | absolutely required for the reactivation of the inactivated holoenzyme by the reactivating factor | Klebsiella oxytoca |  |
| 4.2.1.28 | additional information | ADP and ATP analogues are not able to substitute ATP significantly | Klebsiella oxytoca |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.2.1.28 | expression in Escherichia coli | Klebsiella oxytoca |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.1.28 | Klebsiella oxytoca | - |
- |
- |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.28 | 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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Release 2023.1 (January 2023)
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