CATH Classification
Level | CATH Code | Description |
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2 | Mainly Beta |
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2.40 | Beta Barrel |
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2.40.40 | Barwin-like endoglucanases |
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2.40.40.20 |
Domain Context
CATH Clusters
Superfamily | 2.40.40.20 |
Functional Family | Biotin sulfoxide reductase 2 |
Enzyme Information
1.7.2.3 |
Trimethylamine-N-oxide reductase.
based on mapping to UniProt Q52675
Trimethylamine + 2 (ferricytochrome c)-subunit + H(2)O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H(+).
-!- Contains bis(molybdopterin guanine dinucleotide)molybdenum cofactor. -!- The reductant is a membrane-bound multiheme cytochrome c. -!- Also reduces dimethyl sulfoxide to dimethyl sulfide.
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1.8.5.3 |
Respiratory dimethylsulfoxide reductase.
based on mapping to UniProt Q52675
Dimethylsulfide + menaquinone + H(2)O = dimethylsulfoxide + menaquinol.
-!- The enzyme participates in bacterial electron transfer pathways in which dimethylsulfoxide (DMSO) is the terminal electron acceptor. -!- It is composed of three subunits - DmsA contains a bis(guanylyl molybdopterin) cofactor and a [4Fe-4S] cluster, DmsB is an iron- sulfur protein, and DmsC is a transmembrane protein that anchors the enzyme and accepts electrons from the quinol pool. -!- The electrons are passed through DmsB to DmsA and on to DMSO. -!- The enzyme can also reduce pyridine-N-oxide and trimethylamine N-oxide to the corresponding amines with lower activity.
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UniProtKB Entries (1)
Q52675 |
DSTOR_RHOCA
Rhodobacter capsulatus
Dimethyl sulfoxide/trimethylamine N-oxide reductase
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PDB Structure
PDB | 1E60 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Reversible Dissociation of Thiolate Ligands from Molybdenum in an Enzyme of the Dimethyl Sulfoxide Reductase Family
Biochemistry
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