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Literature summary for 1.5.8.2 extracted from

  • Steenkamp, D.J.; McIntire, W.; Kenney, W.C.
    Structure of the covalently bound coenzyme of trimethylamine dehydrogenase (1978), J. Biol. Chem., 253, 2818-2824.
    View publication on PubMed
Search for more literature for 1.5.8.2

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 6-S-cysteinyl-FMN coenzyme-peptide Methylophilus methylotrophus