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Literature summary extracted from

  • Davidson, V.L.; Husain, M.; Neher, J.W.
    Electron transfer flavoprotein from Methylophilus methylotrophus: Properties, comparison with other electron transfer flavoproteins, and regulation of expression by carbon source (1986), J. Bacteriol., 166, 812-817.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.8.2 trimethylamine + H2O + electron transferring flavoprotein Methylophilus methylotrophus
-
 dimethylamine + formaldehyde + reduced electron transferring flavoprotein
-
 ?
1.5.8.2 trimethylamine + H2O + electron transferring flavoprotein Methylophilus methylotrophus W3A1
-
 dimethylamine + formaldehyde + reduced electron transferring flavoprotein
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.5.8.2 Methylophilus methylotrophus
-
-
-
1.5.8.2 Methylophilus methylotrophus W3A1
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.5.8.2 cell culture
-
 Methylophilus methylotrophus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.8.2 trimethylamine + H2O + electron transferring flavoprotein
-
 Methylophilus methylotrophus dimethylamine + formaldehyde + reduced electron transferring flavoprotein
-
 ?
1.5.8.2 trimethylamine + H2O + electron transferring flavoprotein
-
 Methylophilus methylotrophus W3A1 dimethylamine + formaldehyde + reduced electron transferring flavoprotein
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.8.2 electron transferring flavoprotein physiological cofactor, two subunits of 38 and 42 kDa, reduced by trimethylamine dehydrogenase to a stable anionic semiquinone form Methylophilus methylotrophus