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Literature summary for 1.5.3.10 extracted from
- Crystal structure of DMGO provides a prototype for a new tetrahydrofolate-binding fold (2005), Biochem. Soc. Trans., 33, 776-779.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| in complex with folate compounds. N-terminal region covalently binds FAD and has dimethylglycine dehydrogenase activity | Arthrobacter globiformis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arthrobacter globiformis | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| N,N-dimethylglycine + 5,6,7,8-tetrahydrofolate + O2 = sarcosine + 5,10-methylenetetrahydrofolate + H2O2 | tetrahydrofolate-binding site of enzyme is highly specific for reduced folate compounds and enhances the nucleophilic character of the tetrahydrofolate N10 position | Arthrobacter globiformis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | - |
Arthrobacter globiformis |  |
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Release 2023.1 (January 2023)
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