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Literature summary for 2.1.1.106 extracted from
- Understanding the role of electron donors in the reaction catalyzed by Tsrm, a cobalamin-dependent radical S-adenosylmethionine methylase (2019), J. Biol. Inorg. Chem., 24, 831-839 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Streptomyces laurentii |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptomyces laurentii | C0JRZ9 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant protein | Streptomyces laurentii |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | TsrM can catalyze multiple turnovers in the absence of any reducing agent, but only when it is pre-loaded with methylcobalamin. When hydroxocobalamin or cob(II)alamin is bound to TsrM, a reductant is required to convert it to cob(I)alamin, which can acquire a methyl group directly from S-adenosylmethionine. TrsM is most active when flavodoxin/flavodoxin reductase/NADPH is included in the reaction | Streptomyces laurentii |
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Release 2023.1 (January 2023)
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