Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.8.5.3 extracted from

  • Xiong, L.; Jian, H.; Xiao, X.
    Deep-sea bacterium Shewanella piezotolerans WP3 has two dimethyl sulfoxide reductases in distinct subcellular locations (2017), Appl. Environ. Microbiol., 83, e01262-17 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.8.5.3

Cloned(Commentary)

Cloned (Comment) Organism
gene dms, recombinant expression of wild-type dmsA1 and dmsB6 and mutant enzymes in wild-type and mutant lines of Shewanella piezotolerans Shewanella piezotolerans

Protein Variants

Protein Variants Comment Organism
additional information to investigate whether the subunits from these two DMSO reductases are interchangeable, two unmarked double in-frame DELTAdmsA1/DELTAdmsB6 and DELTAdmsA6/DELTAdmsB1 deletion mutants are constructed. Physiological assays demonstrate that the two double mutants lose the ability to utilize DMSO for anaerobic growth under different conditions. Moreover, transcriptional analyses reveal that deletion of the individual gene does not eliminate the expression of other genes within the same gene cluster. The loss of DMSO-dependent growth of the DELTAdmsA1/DELTAdmsB6 and DELTAdmsA6/DELTAdmsB1 mutants can be rescued by introduction of dmsA1 and dmsA6, respectively. Two complemented strains (the DELTAdmsA1/DELTAdmsB6-dmsA1-C and DELTAdmsA6/DELTAdmsB1-dmsA6-C strains [where -C refers to complementation]) are generated. The introduction of either dmsA1 into the DELTAdmsA1/DELTAdmsB6 mutant or dmsA6 into the DELTAdmsA6/DELTAdmsB1 mutant partially restores the ability of these double mutants to utilize DMSO for anaerobic growth. Growth curves of wild-type and mutant WP3 strains with DMSO as the sole electron acceptor, overview. Mutational analysis of subcellular localization of isozymes Shewanella piezotolerans

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information the type I DMSO reductase is localized on the outer leaflet of the outer membrane, whereas the type VI DMSO reductase is located within the periplasmic space, type I DMSO reductase tends to be localized extracellularly Shewanella piezotolerans
-
-
outer membrane type I DMSO reductase Shewanella piezotolerans 19867
-
periplasmic space type VI DMSO reductase Shewanella piezotolerans 42597
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dimethylsulfoxide + menaquinol Shewanella piezotolerans
-
 dimethylsulfide + menaquinone + H2O
-
 ?
dimethylsulfoxide + menaquinol Shewanella piezotolerans WP3
-
 dimethylsulfide + menaquinone + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Shewanella piezotolerans
-
 isolated from west Pacific deep-sea sediments at a water depth of 1914 m
-
Shewanella piezotolerans WP3
-
 isolated from west Pacific deep-sea sediments at a water depth of 1914 m
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information growth of wild-type and mutant WP3 strains with DMSO as the sole electron acceptor, overview Shewanella piezotolerans
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dimethylsulfoxide + menaquinol
-
 Shewanella piezotolerans dimethylsulfide + menaquinone + H2O
-
 ?
dimethylsulfoxide + menaquinol
-
 Shewanella piezotolerans WP3 dimethylsulfide + menaquinone + H2O
-
 ?
additional information CymA, a cytoplasmic membrane-bound tetraheme c-type cytochrome, 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 Shewanella piezotolerans ?
-
-
additional information CymA, a cytoplasmic membrane-bound tetraheme c-type cytochrome, 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 Shewanella piezotolerans WP3 ?
-
-

Synonyms

Synonyms Comment Organism
dms
-
 Shewanella piezotolerans
DMSO reductase
-
 Shewanella piezotolerans

Cofactor

Cofactor Comment Organism Structure
menaquinone
-
 Shewanella piezotolerans
additional information 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. In-frame deletion mutagenesis of dmsE (swp3461) and analysis Shewanella piezotolerans

General Information

General Information Comment Organism
evolution 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 Shewanella piezotolerans
malfunction 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 Shewanella piezotolerans
metabolism 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 Shewanella piezotolerans
physiological function dimethyl sulfoxide (DMSO) is an environmentally significant compound due to the potential role that it plays in the biogeochemical cycle of the climatically active gas dimethyl sulfide (DMS). DMSO can be produced through the transformation of DMS by both photooxidation and biooxidation routes or by direct production from marine phytoplankton. The formation of DMSO therefore leads to the removal of DMS from seawater, effectively controlling DMS flux into the atmosphere. In addition to its roles in protecting cells against photogenerated oxidants and cryogenic damage, DMSO can also be used as an alternative electron acceptor for energy conservation through microbial dissimilatory reduction, involving the enzyme DMSo redutase. DMSO acts as a substantial sink for DMS in deep oceanic waters. Both DMSO reductase isozymes, type I and type VI, in WP3 are functionally independent despite their close evolutionary relationship Shewanella piezotolerans