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Literature summary for extracted from

  • Scrutton, N.S.; Leys, D.
    Crystal structure of DMGO provides a prototype for a new tetrahydrofolate-binding fold (2005), Biochem. Soc. Trans., 33, 776-779.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with folate compounds. N-terminal region covalently binds FAD and has dimethylglycine dehydrogenase activity Arthrobacter globiformis


Organism UniProt Comment Textmining
Arthrobacter globiformis


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 Comment Organism Structure
Arthrobacter globiformis