Literature summary for 1.8.5.3 extracted from

Stewart, L.J.; Bailey, S.; Bennett, B.; Charnock, J.M.; Garner, C.D.; McAlpine, A.S.
Dimethylsulfoxide reductase: an enzyme capable of catalysis with either molybdenum or tungsten at the active site (2000), J. Mol. Biol., 299, 593-600.

Search for more literature for 1.8.5.3

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Rhodobacter capsulatus

Crystallization (Commentary)

Crystallization (Comment)	Organism
protein with tungsten in place of molybdenum, to 2.0 A resolution	Rhodobacter capsulatus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Tungsten	may replace molybdenum. Tungsten is ligated by the dithiolene group of the two pyranopterins, the oxygen atom of Ser147 plus another oxygen atom, and is located in a very similar site to that of molybdenum in Mo-DMSOR. W-DMSOR is significantly more active than Mo-DMSOR in catalysing the reduction of dimethylsulfoxide but shows no significant ability to catalyse the oxidation of dimethylsulfide	Rhodobacter capsulatus

Organism

Organism	UniProt	Comment	Textmining
Rhodobacter capsulatus	Q52675	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
dimethyl sulfoxide + reduced methyl viologen	-	Rhodobacter capsulatus	dimethyl sulfide + H2O + oxidized methyl viologen	-	r

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
21	-	dimethyl sulfoxide	enzyme Mo-DMSOR with molybdenum in the catalytic centre, pH not specified in the publication, temperature not specified in the publication	Rhodobacter capsulatus
470	-	dimethyl sulfoxide	enzyme W-DMSOR with tungsten in the catalytic centre, pH not specified in the publication, temperature not specified in the publication	Rhodobacter capsulatus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)