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Literature summary for 1.14.13.242 extracted from
- Hydroxylation and ring-opening mechanism of an unusual flavoprotein monooxygenase, 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase a theoretical study (2010), Chemistry, 16, 2557-2566 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mesorhizobium loti | Q988D3 | - |
- |
| Mesorhizobium loti MAFF 303099 | Q988D3 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase | - |
Mesorhizobium loti |
| MHPCO | - |
Mesorhizobium loti |
| mlr6788 | - |
Mesorhizobium loti |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | conversion of 2-methyl-3-hydroxypyridine-5-carboxylic acid to alpha-(N-acetylaminomethylene)succinic acid is the essential ring-opening step in the bacterial degradation of vitamin B6. The rearomatisation of the hydroxylated intermediate occurs spontaneously in aqueous solution. This implies that the ring-opening process occurs inside the enzyme's active site. Proposal of two pathways with reasonable energy barriers | Mesorhizobium loti |
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