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Literature summary for 1.5.8.2 extracted from

  • Steenkamp, D.J.; Singer, T.P.; Beinert, H.
    Participation of the iron-sulphur cluster and of the covalently bound coenzyme of trimethylamine dehydrogenase on catalysis (1978), Biochem. J., 169, 361-369.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
Fe 4Fe-4S-center Methylophilus methylotrophus

Natural Substrates/ Products (Substrates)

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

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 acceptor
-
Methylophilus methylotrophus dimethylamine + formaldehyde + reduced electron acceptor
-
?
trimethylamine + H2O + electron acceptor
-
Methylophilus methylotrophus W3A1 dimethylamine + formaldehyde + reduced electron acceptor
-
?

Cofactor

Cofactor Comment Organism Structure
FMN unusual type of covalently bound flavin Methylophilus methylotrophus