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Literature summary for 4.8.1.2 extracted from
- Why is the oxidation state of iron crucial for the activity of heme-dependent aldoxime dehydratase? A QM/MM study (2012), J. Phys. Chem. B, 116, 9396-9408.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H299A | the mutation leads to the loss of the ability to bind heme, thus becoming inactive | Rhodococcus sp. |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rhodococcus sp. | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (E)-acetaldoxime | - |
Rhodococcus sp. | ? | - |
? |  |
| (Z)-acetaldoxime | preferred substrate | Rhodococcus sp. | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | - |
Rhodococcus sp. |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| OxdRE | - |
Rhodococcus sp. |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| heme | the heme-containing enzyme utilizes the ferrous rather than the ferric ion to catalyze the synthesis of nitriles | Rhodococcus sp. | |
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Release 2023.1 (January 2023)
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