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Literature summary for 4.2.1.9 extracted from
- The inactivation of dihydroxy-acid dehydratase in Escherichia coli treated with hyperbaric oxygen occurs because of the destruction of its Fe-S cluster, but the enzyme remains in the cell in a form that can be reactivated (1993), J. Biol. Chem., 268, 25547-25552.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Oxidation Stability
| Oxidation Stability | Organism |
|---|---|
| inactivation by exposure to hyperbaric O2 is due to the destruction of its catalytically active 4Fe-4S cluster. Reactivation occurs by reconstitution of the enzyme's Fe-S cluster | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2,3-dihydroxy-3-methylbutanoate | - |
Escherichia coli | 2-oxoisovalerate + H2O | - |
? |  |
| 2,3-dihydroxy-3-methylpentanoate | - |
Escherichia coli | 3-methyl-2-oxopentanoate + H2O | - |
? | |
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Release 2023.1 (January 2023)
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