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Literature summary extracted from
- X-ray analysis of butirosin biosynthetic enzyme BtrN redefines structural motifs for AdoMet radical chemistry (2013), Proc. Natl. Acad. Sci. USA, 110, 15949-15954.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.1.99.38 | in complex with AdoMet and substrate, to 1.56 A resolution. Structure displays a modification to the core AdoMet radical fold, instead of the canonical (beta/alpha)6 architecture, BtrN displays a (beta5/alpha4) motif. An auxiliary [4Fe-4S] cluster in BtrN, thought to bind substrate, is instead implicated in substrate-radical oxidation | Niallia circulans |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.1.99.38 | Niallia circulans | Q8G907 | - |
- |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.1.99.38 | BtrN | - |
Niallia circulans |
| 1.1.99.38 | DOIA dehydrogenase | - |
Niallia circulans |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.99.38 | [4Fe-4S]-center | cluster is implicated in substrate-radical oxidation | Niallia circulans |  |
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Release 2023.1 (January 2023)
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