2.1.1.373: 2-hydroxy-4-(methylsulfanyl)butanoate S-methyltransferase
This is an abbreviated version!
For detailed information about 2-hydroxy-4-(methylsulfanyl)butanoate S-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.373
-
2.1.1.373
-
sulfur
-
dimethylsulfoniopropionate
-
o-acetyl
-
kjellm
-
sulfhydrylase
-
pertusa
-
earth
- 2.1.1.373
- sulfur
- dimethylsulfoniopropionate
-
o-acetyl
-
kjellm
-
sulfhydrylase
- pertusa
-
earth
Reaction
Synonyms
dsyB, methylthiohydroxybutryate methyltransferase, methylthiohydroxybutyrate methyltransferase, methylthiohydroxybutyrate S-methyltransferase, MMT, MTHB methyltransferase, MTHB S-methyltransferase, MTHB-methyltransferase, SIAM614_21095, Tp23128, TpMT2, XP_002291473
ECTree
Advanced search results
General Information
General Information on EC 2.1.1.373 - 2-hydroxy-4-(methylsulfanyl)butanoate S-methyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
malfunction
-
metagenome data show that bacterial dsyB mutants are less tolerant of deep ocean pressures than wild-type strains
metabolism
physiological function
-
evolutionary analysis suggests that eukaryotic enzyme (DSYB) originates in bacteria and is passed to eukaryotes early in their evolution
evolution
-
evolutionary analysis suggests that eukaryotic enzyme (DSYB) originates in bacteria and is passed to eukaryotes early in their evolution
evolution
-
evolutionary analysis suggests that eukaryotic enzyme (DSYB) originates in bacteria and is passed to eukaryotes early in their evolution
evolution
-
evolutionary analysis suggests that eukaryotic enzyme (DSYB) originates in bacteria and is passed to eukaryotes early in their evolution
evolution
-
evolutionary analysis suggests that eukaryotic enzyme (DSYB) originates in bacteria and is passed to eukaryotes early in their evolution
evolution
-
evolutionary analysis suggests that eukaryotic enzyme (DSYB) originates in bacteria and is passed to eukaryotes early in their evolution
evolution
-
evolutionary analysis suggests that eukaryotic enzyme (DSYB) originates in bacteria and is passed to eukaryotes early in their evolution
evolution
-
the bacterial DsyB enzyme is homologous to the algal DSYB enzyme and likely originates in bacteria
evolution
Chrysochromulina tobinii CCMP291
-
evolutionary analysis suggests that eukaryotic enzyme (DSYB) originates in bacteria and is passed to eukaryotes early in their evolution
-
evolution
Prymnesium parvum CCAP946/1B
-
evolutionary analysis suggests that eukaryotic enzyme (DSYB) originates in bacteria and is passed to eukaryotes early in their evolution
-
evolution
Lingulodinium polyedra CCMP1936
-
evolutionary analysis suggests that eukaryotic enzyme (DSYB) originates in bacteria and is passed to eukaryotes early in their evolution
-
evolution
Alexandrium tamarense CCMP1771
-
evolutionary analysis suggests that eukaryotic enzyme (DSYB) originates in bacteria and is passed to eukaryotes early in their evolution
-
evolution
Prymnesium parvum CCAP941
-
evolutionary analysis suggests that eukaryotic enzyme (DSYB) originates in bacteria and is passed to eukaryotes early in their evolution
-
evolution
-
evolutionary analysis suggests that eukaryotic enzyme (DSYB) originates in bacteria and is passed to eukaryotes early in their evolution
-
evolution
Acropora cervicornis CCMP1771
-
evolutionary analysis suggests that eukaryotic enzyme (DSYB) originates in bacteria and is passed to eukaryotes early in their evolution
-
evolution
Symbiodinium microadriaticum CCMP2467
-
evolutionary analysis suggests that eukaryotic enzyme (DSYB) originates in bacteria and is passed to eukaryotes early in their evolution
-
-
the enzyme catalyses the key step of dimethylsulfoniopropionate biosynthesis in phytoplankton
metabolism
-
the enzyme catalyses the key step of dimethylsulfoniopropionate biosynthesis in phytoplankton
metabolism
-
the enzyme catalyses the key step of dimethylsulfoniopropionate biosynthesis in phytoplankton
metabolism
-
the enzyme catalyses the key step of dimethylsulfoniopropionate biosynthesis in phytoplankton
metabolism
-
the enzyme catalyses the key step of dimethylsulfoniopropionate biosynthesis in phytoplankton
metabolism
-
the enzyme catalyses the key step of dimethylsulfoniopropionate biosynthesis in phytoplankton
metabolism
-
the enzyme catalyses the key step of dimethylsulfoniopropionate biosynthesis in phytoplankton
metabolism
the enzyme catalyses the key step of dimethylsulfoniopropionate biosynthesis. Dimethylsulfoniopropionate plays a pivotal role in the marine sulfur cycle
metabolism
Chrysochromulina tobinii CCMP291
-
the enzyme catalyses the key step of dimethylsulfoniopropionate biosynthesis in phytoplankton
-
metabolism
-
the enzyme catalyses the key step of dimethylsulfoniopropionate biosynthesis. Dimethylsulfoniopropionate plays a pivotal role in the marine sulfur cycle
-
metabolism
Prymnesium parvum CCAP946/1B
-
the enzyme catalyses the key step of dimethylsulfoniopropionate biosynthesis in phytoplankton
-
metabolism
Lingulodinium polyedra CCMP1936
-
the enzyme catalyses the key step of dimethylsulfoniopropionate biosynthesis in phytoplankton
-
metabolism
Alexandrium tamarense CCMP1771
-
the enzyme catalyses the key step of dimethylsulfoniopropionate biosynthesis in phytoplankton
-
metabolism
Prymnesium parvum CCAP941
-
the enzyme catalyses the key step of dimethylsulfoniopropionate biosynthesis in phytoplankton
-
metabolism
-
the enzyme catalyses the key step of dimethylsulfoniopropionate biosynthesis in phytoplankton
-
metabolism
Acropora cervicornis CCMP1771
-
the enzyme catalyses the key step of dimethylsulfoniopropionate biosynthesis in phytoplankton
-
metabolism
Symbiodinium microadriaticum CCMP2467
-
the enzyme catalyses the key step of dimethylsulfoniopropionate biosynthesis in phytoplankton
-
-
the enzyme is involved in biosynthesis of dimethylsulfoniopropionate from methionine. Sulfur deficiency increases the activity of the sulfur assimilation enzyme O-acetyl serine sulfhydrylase but decreases the 2-hydroxy-4-(methylsulfanyl)butanoate S-methyltransferase activity
physiological function
-
the enzyme is involved in biosynthesis of the marine osmolyte dimethylsulfoniopropionate (DMSP). The physiological function for DMSP in hydrostatic pressure protection. Bacteria are key DMSP producers in deep seawater and sediment. The genetic potential for bacterial DMSP synthesis via the dsyB gene and its transcription is greater in the deep ocean, and is highest in the sediment.s DMSP catabolic potential is present throughout the trench waters, but is less prominent below 8000 m, perhaps indicating a preference to store DMSP in the deep for stress protection. Deep ocean bacterial isolates show enhanced DMSP production under increased hydrostatic pressure. No eukaryotic DMSP synthesis genes are detected in any metagenomes, even from the surface waters
physiological function
Roseibium aggregatum
enzyme is involved in synthesis of dimethylsulfoniopropionate. A DsyB disruption mutant no longer produces dimethylsulfoniopropionate but accumulates approximately threefold more 4-methylthio-2-hydroxybutyrate than the wild-type
physiological function
-
recombinant expression in Rhizobium leguminosarum confers dimethylsulfoniopropionate production from 4-methylthio-2-hydroxybutanoate
physiological function
-
recombinant expression in Rhizobium leguminosarum confers dimethylsulfoniopropionate production from 4-methylthio-2-hydroxybutanoate
physiological function
-
recombinant expression in Rhizobium leguminosarum confers dimethylsulfoniopropionate production from 4-methylthio-2-hydroxybutanoate
physiological function
-
the enzyme is involved in the 3-dimethylsulfoniopropionate synthesis pathway. The enzyme may be involved to confer osmotolerance. The product (2R)-4-(dimethylsulfaniumyl)-2-hydroxybutanoate is an osmoprotectant
physiological function
-
recombinant expression in Rhizobium leguminosarum confers dimethylsulfoniopropionate production from 4-methylthio-2-hydroxybutanoate
-
physiological function
Roseibium aggregatum LZB033
-
enzyme is involved in synthesis of dimethylsulfoniopropionate. A DsyB disruption mutant no longer produces dimethylsulfoniopropionate but accumulates approximately threefold more 4-methylthio-2-hydroxybutyrate than the wild-type
-
physiological function
-
recombinant expression in Rhizobium leguminosarum confers dimethylsulfoniopropionate production from 4-methylthio-2-hydroxybutanoate
-