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Literature summary extracted from

  • Zhang, L.; Nelson, K.J.; Rajagopalan, K.V.; George, G.N.
    Structure of the molybdenum site of Escherichia coli trimethylamine N-oxide reductase (2008), Inorg. Chem., 47, 1074-1078.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.7.2.3
-
Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.7.2.3 Molybdenum involved in the catalytic mechanism, experimental data suggest that the active site of TMAO reductase with bound molybdenum can exist in three different forms Escherichia coli
1.7.2.3 molybdopterin in the molybdopterin molybdenum cofactor, Mo-S and Mo-O interactions, molecular structure modelling, overview Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.7.2.3 trimethylamine-N-oxide + enzyme-MoIV Escherichia coli anaerobic respiration trimethylamine + enzyme-MoVI + H2O
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.3 Escherichia coli
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.7.2.3 trimethylamine + 2 (ferricytochrome c)-subunit + H2O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+ molybdenum serves as electron donor within the enzyme, enzyme-MoIV + (CH3)3NdO + 2H+ = enzyme-MoVI + (CH3)3N + H2O Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.2.3 additional information the TMAO reductase active site can exist in multiple forms, molecular modelling, overview Escherichia coli ?
-
?
1.7.2.3 trimethylamine-N-oxide + enzyme-MoIV anaerobic respiration Escherichia coli trimethylamine + enzyme-MoVI + H2O
-
?

Subunits

EC Number Subunits Comment Organism
1.7.2.3 More structure comparison and analysis, the TMAO reductase active site can exist in multiple forms, molecular modelling, overview Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.7.2.3 TMAO reductase
-
Escherichia coli
1.7.2.3 TMAO reductase belongs to the DMSO reductase family of molybdenum enzymes Escherichia coli
1.7.2.3 trimethylamine N-oxide reductase
-
Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.2.3 molybdopterin
-
Escherichia coli