Literature summary for 1.8.5.3 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.

Search for more literature for 1.8.5.3

Protein Variants

Protein Variants	Comment	Organism
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]

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

Organism

Organism	UniProt	Comment	Textmining
Rhodobacter capsulatus	-	-	-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

Cofactor

Cofactor	Comment	Organism	Structure
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]

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

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Release 2023.1 (January 2023)