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Literature summary 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(Commentary)

EC Number Cloned (Comment) Organism
1.5.3.10 expression in Escherichia coli Arthrobacter globiformis

Crystallization (Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
1.5.3.10 D552A mutation leads to increased formaldehyde release Arthrobacter globiformis
1.5.3.10 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

EC Number Organism UniProt Comment Textmining
1.5.3.10 Arthrobacter globiformis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.3.10 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
-
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Cofactor

EC Number Cofactor Comment Organism Structure
1.5.3.10 FAD
-
Arthrobacter globiformis