Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Ridge, J.P.; Aguey-Zinsou, K.F.; Bernhardt, P.V.; Hanson, G.R.; McEwan, A.G.
    The critical role of tryptophan-116 in the catalytic cycle of dimethylsulfoxide reductase from Rhodobacter capsulatus (2004), FEBS Lett., 563, 197-202.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.8.5.3 W116F residue W116 forms a hydrogen bond with a single oxo ligand bound to the molybdenum ion. Mutation of this residue to phenylalanine affects the UV/visible spectrum of the purified MoVI form of dimethylsulfoxide reductase resulting in the loss of the characteristic transition at 720 nm Rhodobacter capsulatus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.5.3 0.0097
-
 Dimethylsulfoxide wild-type, pH not specified in the publication, temperature not specified in the publication Rhodobacter capsulatus
1.8.5.3 0.0261
-
 Dimethylsulfoxide mutant W116F, pH not specified in the publication, temperature not specified in the publication Rhodobacter capsulatus
1.8.5.3 0.0959
-
 Trimethylamine-N-oxide mutant W116F, pH not specified in the publication, temperature not specified in the publication Rhodobacter capsulatus
1.8.5.3 0.193
-
 Trimethylamine-N-oxide wild-type, pH not specified in the publication, temperature not specified in the publication Rhodobacter capsulatus

Organism

EC Number Organism UniProt Comment Textmining
1.8.5.3 Rhodobacter capsulatus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.5.3 dimethylsulfoxide + reduced methyl viologen
-
 Rhodobacter capsulatus dimethylsulfide + H2O + oxidized methyl viologen
-
 r
1.8.5.3 trimethylamine-N-oxide + reduced methyl viologen
-
 Rhodobacter capsulatus trimethylamine + H2O + oxidized methyl viologen
-
 r

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8.5.3 7
-
 Dimethylsulfoxide mutant W116F, pH not specified in the publication, temperature not specified in the publication Rhodobacter capsulatus
1.8.5.3 11.3
-
 Trimethylamine-N-oxide mutant W116F, pH not specified in the publication, temperature not specified in the publication Rhodobacter capsulatus
1.8.5.3 42.9
-
 Dimethylsulfoxide wild-type, pH not specified in the publication, temperature not specified in the publication Rhodobacter capsulatus
1.8.5.3 134.5
-
 Trimethylamine-N-oxide wild-type, pH not specified in the publication, temperature not specified in the publication Rhodobacter capsulatus

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.5.3 molybdenum cofactor residue W116 forms a hydrogen bond with a single oxo ligand bound to the molybdenum ion. Mutation of this residue to phenylalanine affects the UV/visible spectrum of the purified MoVI form of dimethylsulfoxide reductase resulting in the loss of the characteristic transition at 720 nm. W116 plays a critical role in stabilizing the hexacoordinate monooxo MoVI form of the enzyme and prevents the formation of a dioxo pentacoordinate MoVI species Rhodobacter capsulatus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.8.5.3 100
-
 Trimethylamine-N-oxide mutant W116F, pH not specified in the publication, temperature not specified in the publication Rhodobacter capsulatus
1.8.5.3 300
-
 Dimethylsulfoxide mutant W116F, pH not specified in the publication, temperature not specified in the publication Rhodobacter capsulatus
1.8.5.3 700
-
 Trimethylamine-N-oxide wild-type, pH not specified in the publication, temperature not specified in the publication Rhodobacter capsulatus
1.8.5.3 4400
-
 Dimethylsulfoxide wild-type, pH not specified in the publication, temperature not specified in the publication Rhodobacter capsulatus