ExplorEnz: EC 1.5.3.10

Your query returned 1 entry. Printable version

1.5.3.10

Accepted name:

dimethylglycine oxidase

Reaction:

N,N-dimethylglycine + 5,6,7,8-tetrahydrofolate + O₂ = sarcosine + 5,10-methylenetetrahydrofolate + H₂O₂

Other name(s):

dmg (gene name); N,N-dimethylglycine:oxygen oxidoreductase (demethylating)

Systematic name:

N,N-dimethylglycine,5,6,7,8-tetrahydrofolate:oxygen oxidoreductase (demethylating,5,10-methylenetetrahydrofolate-forming)

Comments:

A flavoprotein (FAD). The enzyme, characterized from the bacterium Arthrobacter globiformis, contains two active sites connected by a large "reaction chamber". An imine intermediate is transferred between the sites, eliminating the production of toxic formaldehyde. In the absence of folate the enzyme does form formaldehyde. Does not oxidize sarcosine. cf. EC 1.5.8.4, dimethylglycine dehydrogenase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-30-7

References:

1.	Mori, N., Kawakami, B., Tani, Y. and Yamada, H. Purification and properties of dimethylglycine oxidase from Cylindrocarpon didymum M-1. Agric. Biol. Chem. 44 (1980) 1383–1389.
2.	Meskys, R., Harris, R.J., Casaite, V., Basran, J. and Scrutton, N.S. Organization of the genes involved in dimethylglycine and sarcosine degradation in Arthrobacter spp.: implications for glycine betaine catabolism. Eur. J. Biochem. 268 (2001) 3390–3398. [DOI] [PMID: 11422368]
3.	Basran, J., Bhanji, N., Basran, A., Nietlispach, D., Mistry, S., Meskys, R. and Scrutton, N.S. Mechanistic aspects of the covalent flavoprotein dimethylglycine oxidase of Arthrobacter globiformis studied by stopped-flow spectrophotometry. Biochemistry 41 (2002) 4733–4743. [DOI] [PMID: 11926836]
4.	Leys, D., Basran, J. and Scrutton, N.S. Channelling and formation of ‘active’ formaldehyde in dimethylglycine oxidase. EMBO J. 22 (2003) 4038–4048. [DOI] [PMID: 12912903]
5.	Basran, J., Fullerton, S., Leys, D. and Scrutton, N.S. Mechanism of FAD reduction and role of active site residues His-225 and Tyr-259 in Arthrobacter globiformis dimethylglycine oxidase: analysis of mutant structure and catalytic function. Biochemistry 45 (2006) 11151–11161. [DOI] [PMID: 16964976]
6.	Tralau, T., Lafite, P., Levy, C., Combe, J.P., Scrutton, N.S. and Leys, D. An internal reaction chamber in dimethylglycine oxidase provides efficient protection from exposure to toxic formaldehyde. J. Biol. Chem. 284 (2009) 17826–17834. [DOI] [PMID: 19369258]
7.	Casaite, V., Poviloniene, S., Meskiene, R., Rutkiene, R. and Meskys, R. Studies of dimethylglycine oxidase isoenzymes in Arthrobacter globiformis cells. Curr. Microbiol. 62 (2011) 1267–1273. [DOI] [PMID: 21188587]

[EC 1.5.3.10 created 1992, modified 2022]