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Literature summary for 1.5.8.2 extracted from

  • Steenkamp, D.J.; Gallup, M.
    The natural flavoprotein electron acceptor of trimethylamine dehydrogenase (1978), J. Biol. Chem., 253, 4086-4089.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Methylophilus methylotrophus
-
-
-
Methylophilus methylotrophus W3A1
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
cell culture
-
Methylophilus methylotrophus
-

Substrates and Products (Substrate)

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

Cofactor

Cofactor Comment Organism Structure
electron transferring flavoprotein 77 kDa dimer of two dissimilar subunits, containing 1 FAD per mol of protein, reduced by trimethylamine dehydrogenase to a stable semiquinone form Methylophilus methylotrophus
FMN
-
Methylophilus methylotrophus