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EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.8.5.3evolution dimethyl sulfoxide reductase (DMSOR) represents the canonical member of the DMSOR family of prokaryotic pyranopterin molybdenum enzymes. DMSOR family enzymes have been classified by type, with type II/III enzymes being characterized by [(PDT)2MoVIO(OSer/Asp)]- oxidized active sites that possess N- and S-oxide reductase activity. Type III Rhodobacter capsulatus DMSOR catalyzes the reduction of dimethyl sulfoxide to dimethyl sulfide (DMS) as part of the global sulfur cycle 764842
Display the word mapDisplay the reaction diagram Show all sequences 1.8.5.3evolution dimethyl sulfoxide reductase (DMSOR) represents the canonical member of the DMSOR family of prokaryotic pyranopterin molybdenum enzymes. DMSOR family enzymes have been classified by type, with type II/III enzymes being characterized by [(PDT)2MoVIO(OSer/Asp)]- oxidized active sites that possess N- and S-oxide reductase activity. Type III Rhodobacter sphaeroides DMSOR catalyzes the reduction of dimethyl sulfoxide to dimethyl sulfide (DMS) as part of the global sulfur cycle 764842
Display the word mapDisplay the reaction diagram Show all sequences 1.8.5.3evolution respiratory enzyme members of the DMSOR family such as nitrate reductase (NR, EC 1.9.6.1), dimethyl sulfoxide reductase (DMSOR, EC 1.8.5.3), trimethylamine N-oxide reductase (TMAOR, EC 1.7.2.3), and formate dehydrogenase (FDH) contribute to this broad diversity. The DMSOR family of enzymes has diverse active sites that vary in the first coordination sphere of the molybdenum center. Many enzymes in the DMSOR family use oxygen atom transfer (OAT) reactions for substrate transformation, e.g. periplasmic nitrate reductase (Nap) and respiratory nitrate reductase (Nar) reduce nitrate to nitrite, TMAOR reduces TMAO to TMA, and DMSOR reduces DMSO to dimethyl sulfide (DMS). Enzymes that catalyze the same reaction, such as Nap and Nar, have different molybdenum coordination spheres. In NapA, molybdenum is coordinated by a cysteine residue in the 5th position and an oxo or a sulfido group in the 6th 765095
Display the word mapDisplay the reaction diagram Show all sequences 1.8.5.3evolution 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) -, 764899
Display the word mapDisplay the reaction diagram Show all sequences 1.8.5.3evolution the enzyme belongs to the dimethyl sulfoxide (DMSO) reductase family. The DMSO reductase family enzymes are the most structurally and catalytically diverse of the three pyranopterin Mo enzyme families. The DMSO reductase family enzymes are divided into three classes (Types I, II, and III) that are distinguished from each other by their active site structure and the nature of the donor ligand that is provided by the polypeptide. DMSO reductase family enzymes are quite diverse and not all of the enzymes in this family adhere to this general classification scheme. DMSO reductases are type III enzymes and a combination of EXAFS and high resolution X-ray crystallography shows that the oxidized active site possesses a distorted six-coordinate trigonal prismatic [(MPT)2MoO(OSer)]1- coordination geometry 765321
Display the word mapDisplay the reaction diagram Show all sequences 1.8.5.3evolution type VI and type I DMSO reductases are closely evolutionarily related. But both DMSO reductase isozymes, type I and type VI, in WP3 are functionally independent despite their close evolutionary relationship. Classification and phylogenetic analysis of DMSO respiratory subsystems in Shewanella species, overview -, 763950
Display the word mapDisplay the reaction diagram Show all sequences 1.8.5.3evolution ubiquitous in Archaea and Bacteria, mononuclear molybdoenzymes of the dimethyl sulfoxide reductase (DMSOR) family are believed to have been core components of the first anaerobic respiratory chains, and thus present at life's origins. The family, which has been defined by the presence of a mononuclear molybdopterin or tungstopterin bis(pyranopterin guanine dinucleotide) (Mo/W-bisPGD) cofactor, is named after DMSO reductases, the first members of the family to be well-characterized. Phylogenetic analysis of DMSOR family clades and members, detailed overview. The enzyme belongs to a clade of DMSOR members that include the respiratory dimethyl sulfoxide reductase (DmsA), respiratory nitrate reductase (NarG), PsrA/PhsA/SrrA, ArxA/ArrA, and TtrA/SrdA/archaeal arsenate reductase lineages that interact with the membrane quinone pool during anaerobic respiration using the canonical subunits. The association of DMSOR members with characteristic electron transfer and membrane anchor subunits arose once early in the evolution of DSMORs and co-evolved with these representatives through multiple diversification events 765770
Display the word mapDisplay the reaction diagram Show all sequences 1.8.5.3malfunction loss of DmsABC reduces Haemophilus influenzae fitness in interactions with human bronchial epithelial cells and neutrophils. Mutant Hi2019DELTAdmsA shows an increase in biofilm formation and increased resistance to HOCl -, 764743
Display the word mapDisplay the reaction diagram Show all sequences 1.8.5.3malfunction loss of DMSO-dependent growth of the DELTAdmsA1/DELTAdmsB6 and DELTAdmsA6/DELTAdmsB1 mutants, which can be rescued by introduction of dmsA1 and dmsA6, respectively. The deficiencies of DMSO-dependent growth in DELTAdmsA1/DELTAdmsB6 and DELTAdmsA6/DELTAdmsB1 mutants are attributable to the inability to form functional DMSO reductases rather than to the silencing of the expression of both dms gene clusters. In other words, functional compensation did not occur between DmsA1 and DmsA6 or between DmsB1 and DmsB6 -, 763950
Display the word mapDisplay the reaction diagram Show all sequences 1.8.5.3metabolism two functional DMSO respiratory subsystems are essential for maximum growth of strain WP3 under in situ conditions (4C/20 MPa). A core electron transport model of DMSO reduction in the deep-sea bacterium Shewanella piezotolerans strain WP3 is proposed based on genetic and physiological data, overview. The results collectively suggest that the possession of two sets of DMSO reductases with distinct subcellular localizations may be an adaptive strategy for WP3 to achieve maximum DMSO utilization in deep-sea environments. CymA serves as a preferential electron transport protein for the type I and type VI DMSO reductases, in which type VI accepts electrons from CymA in a DmsE- and DmsF-independent manner. DmsE passes electrons to DmsA1 for DMSO reduction. Type VI DMSO reductase accepts electrons from CymA in a DmsE-independent manner, while type I DMSO reductase is strongly dependent on DmsE for electron transfer. DmsF, an integral outer membrane beta-barrel protein, facilitates electron transfer by forming a pore-like structure through the outer membrane to mediate direct interaction between the extracellular DMSO reductase and DmsE -, 763950
Results 1 - 10 of 22 > >>