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Literature summary for extracted from

  • Tralau, T.; Lafite, P.; Levy, C.; Combe, J.P.; Scrutton, N.S.; Leys, D.
    An internal reaction chamber in dimethylglycine oxidase provides efficient protection from exposure to toxic formaldehyde (2009), J. Biol. Chem., 284, 17826-17834.
    View publication on PubMedView publication on EuropePMC


Cloned (Comment) Organism
expression in Escherichia coli Arthrobacter globiformis

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant D552A in complex with tetrahydrofolate. Presence of one water molecule instead of the Asp552 side chain Arthrobacter globiformis

Protein Variants

Protein Variants Comment Organism
D552A mutation leads to increased formaldehyde release Arthrobacter globiformis
additional information complete removal of 5,10-CH2-THF synthase domain through expression of a truncated version generates a mutant enzyme unable to avoid hydrolysis of the imine species generated following amine oxidation Arthrobacter globiformis


Organism UniProt Comment Textmining
Arthrobacter globiformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N,N-dimethylglycine + H2O + O2 the oxidation of dimethylglycine is coupled to the synthesis of 5,10-methylenetetrahydrofolate through an unusual substrate channeling mechanism. Uncoupling of the active sites can be achieved by mutagenesis or deletion of the 5,10-methylenetetrahydrofolate synthase site and this leads to accumulation of intracellular formaldehyde. Channeling occurs by nonbiased diffusion of the labile intermediate through a large solvent cavity connecting both active sites Arthrobacter globiformis sarcosine + formaldehyde + H2O2


Cofactor Comment Organism Structure
Arthrobacter globiformis