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.
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 |
- |
? |
|
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.5.3.10 |
FAD |
- |
Arthrobacter globiformis |
|