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Literature summary for 1.8.5.3 extracted from

  • Miralles-Robledillo, J.M.; Torregrosa-Crespo, J.; Martinez-Espinosa, R.M.; Pire, C.
    DMSO reductase family phylogenetics and applications of extremophiles (2019), Int. J. Mol. Sci., 20, 3349 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.8.5.3

Metals/Ions

Metals/Ions Comment Organism Structure
Molybdenum required Escherichia coli
Molybdenum reequired Halobacterium salinarum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dimethylsulfoxide + menaquinol Escherichia coli
-
 dimethylsulfide + menaquinone + H2O
-
 ?
dimethylsulfoxide + menaquinol Halobacterium salinarum
-
 dimethylsulfide + menaquinone + H2O
-
 ?
dimethylsulfoxide + menaquinol Escherichia coli K12
-
 dimethylsulfide + menaquinone + H2O
-
 ?
dimethylsulfoxide + menaquinol Halobacterium salinarum ATCC 700922
-
 dimethylsulfide + menaquinone + H2O
-
 ?
dimethylsulfoxide + menaquinol Halobacterium salinarum JCM 11081
-
 dimethylsulfide + menaquinone + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P18775
-
-
Escherichia coli K12 P18775
-
-
Halobacterium salinarum Q9HR74
-
-
Halobacterium salinarum ATCC 700922 Q9HR74
-
-
Halobacterium salinarum JCM 11081 Q9HR74
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dimethylsulfoxide + menaquinol
-
 Escherichia coli dimethylsulfide + menaquinone + H2O
-
 ?
dimethylsulfoxide + menaquinol
-
 Halobacterium salinarum dimethylsulfide + menaquinone + H2O
-
 ?
dimethylsulfoxide + menaquinol
-
 Escherichia coli K12 dimethylsulfide + menaquinone + H2O
-
 ?
dimethylsulfoxide + menaquinol
-
 Halobacterium salinarum ATCC 700922 dimethylsulfide + menaquinone + H2O
-
 ?
dimethylsulfoxide + menaquinol
-
 Halobacterium salinarum JCM 11081 dimethylsulfide + menaquinone + H2O
-
 ?

Synonyms

Synonyms Comment Organism
DmsA
-
 Escherichia coli
DmsA
-
 Halobacterium salinarum
DMSO reductase
-
 Escherichia coli
DMSO reductase
-
 Halobacterium salinarum

Cofactor

Cofactor Comment Organism Structure
molybdenum cofactor pterin-based cofactor MoCo, molybdenum is not active in cells until it forms the MoCo. The DMSO reductases family cofactor is the bis-molybdopterin-guanine dinucleotide (Bis-MGD) and it is composed by two pyranopterin molecules (instead of one pyranopterin as in sulfite oxidases and xanthine oxidases families), which are conjugated with nucleosides: cytosine or guanosine. In this family, the Mo atom in the MoCo is coordinated by four sulfur atoms of the pyranopterins rings and by an inorganic ion that could be selenium, oxygen, or sulfur atoms. In almost all cases, another ligand that has a role in coordination comes from an amino acid side chain that can be aspartate, serine, cysteine, and selenocysteine. Depending on this amino acid, the DMSO reductases can be classified in three types: cysteine or selenocysteine for type I, an aspartate for type II, and serine residue for type III. Enzyme DmsA is a type III enzyme Escherichia coli
molybdenum cofactor pterin-based cofactor MoCo, molybdenum is not active in cells until it forms the MoCo. The DMSO reductases family cofactor is the bis-molybdopterin-guanine dinucleotide (Bis-MGD) and it is composed by two pyranopterin molecules (instead of one pyranopterin as in sulfite oxidases and xanthine oxidases families), which are conjugated with nucleosides: cytosine or guanosine. In this family, the Mo atom in the MoCo is coordinated by four sulfur atoms of the pyranopterins rings and by an inorganic ion that could be selenium, oxygen, or sulfur atoms. In almost all cases, another ligand that has a role in coordination comes from an amino acid side chain that can be aspartate, serine, cysteine, and selenocysteine. Depending on this amino acid, the DMSO reductases can be classified in three types: cysteine or selenocysteine for type I, an aspartate for type II, and serine residue for type III. Enzyme DmsA is a type III enzyme. The Mo amino acid ligand in the MoCo of Halobacterium salinarum DmsA is an aspartate residue in all halophilic archaea instead of a serine residue Halobacterium salinarum
additional information tungsten is present as cofactor in tungsten enzymes, sharing a lot of resemblances with the MoCo of DMSO reductases Escherichia coli
additional information tungsten is present as cofactor in tungsten enzymes, sharing a lot of resemblances with the MoCo of DMSO reductases Halobacterium salinarum

General Information

General Information Comment Organism
evolution the DMSO reductases family cofactor is the bis-molybdopterin-guanine dinucleotide (Bis-MGD) and it is composed by two pyranopterin molecules (instead of one pyranopterin as in sulfite oxidases and xanthine oxidases families), which are conjugated with nucleosides: cytosine or guanosine. In this family, the Mo atom in the MoCo is coordinated by four sulfur atoms of the pyranopterins rings and by an inorganic ion that could be selenium, oxygen, or sulfur atoms. In almost all cases, another ligand that has a role in coordination comes from an amino acid side chain that can be aspartate, serine, cysteine, and selenocysteine. Depending on this amino acid, the DMSO reductases can be classified in three types: cysteine or selenocysteine for type I, an aspartate for type II, and serine residue for type III. Enzymes belonging to this family catalyze different types of reactions: oxidation/reduction, hydroxylation/hydration, and oxygen transfer reactions. Some DMSO reductases are able to recognize more than one substrate under anaerobic conditions. Phylogenetic analysis and tree of DMSO reductases, overview. Type III enzymes are grouped in two clades constituted by DMSO reductases and TMAO reductases from bacteria and archaea. Dual activity has been described in DMSO reductases, as in the case of the Escherichia coli DMSO reductase that can reduce TMAO and other. In contrast, no DMSO reductase activity has been found in biochemically characterized TMAO reductases (EC 1.7.2.3) Escherichia coli
evolution the DMSO reductases family cofactor is the bis-molybdopterin-guanine dinucleotide (Bis-MGD) and it is composed by two pyranopterin molecules (instead of one pyranopterin as in sulfite oxidases and xanthine oxidases families), which are conjugated with nucleosides: cytosine or guanosine. In this family, the Mo atom in the MoCo is coordinated by four sulfur atoms of the pyranopterins rings and by an inorganic ion that could be selenium, oxygen, or sulfur atoms. In almost all cases, another ligand that has a role in coordination comes from an amino acid side chain that can be aspartate, serine, cysteine, and selenocysteine. Depending on this amino acid, the DMSO reductases can be classified in three types: cysteine or selenocysteine for type I, an aspartate for type II, and serine residue for type III. Enzymes belonging to this family catalyze different types of reactions: oxidation/reduction, hydroxylation/hydration, and oxygen transfer reactions. Some DMSO reductases are able to recognize more than one substrate under anaerobic conditions. Phylogenetic analysis and tree of DMSO reductases, overview. Type III enzymes are grouped in two clades constituted by DMSO reductases and TMAO reductases from bacteria and archaea Halobacterium salinarum