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Information on EC 2.1.1.269 - dimethylsulfoniopropionate demethylase
for references in articles please use BRENDA:EC2.1.1.269
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.269 dimethylsulfoniopropionate demethylase
IUBMB Comments
The enzyme from the marine bacteria Pelagibacter ubique and Ruegeria pomeroyi are specific towards S,S-dimethyl-β-propiothetin. They do not demethylate glycine-betaine [1,2].
The enzyme appears in viruses and cellular organisms
- 2.1.1.269
- sulfur
-
demethylation
-
ocean
-
phytoplankton
- roseobacter
- clade
- dimethylsulfide
-
bacterioplankton
- sulfide
-
climatically
- seawater
-
algal
-
metagenomic
-
pacific
- atmosphere
-
coastal
- pomeroyi
-
subclade
-
pelagibacter
- ubique
- lyases
-
free-living
Reaction Schemes
showSynonyms
dmsp demethylase, dimethylsulfoniopropionate demethylase, dmsp methyltransferase, dimethylsufoniopropionate-dependent demethylase a, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimethylsulfoniopropionate demethylase
dimethylsulfoniopropionate methyltransferase
dimethylsulfoniopropionate-dependent demethylase
dimethylsulfoniumpropionate:tetrahydrofolate S-methyltransferase
DmdA
DMSP demethylase
DMSP methyltransferase
DMSP:THF demethylase
dimethylsulfoniumpropionate:tetrahydrofolate S-methyltransferase
-
-
dimethylsulfoniumpropionate:tetrahydrofolate S-methyltransferase
Candidatus Pelagibacter communis HTCC1062
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S,S-dimethyl-beta-propiothetin + tetrahydrofolate = 3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
S,S-dimethyl-beta-propiothetin + tetrahydrofolate = 3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
-
-
-
S,S-dimethyl-beta-propiothetin + tetrahydrofolate = 3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
DmdA catalyzes a redox-neutral methyl transfer reaction to produce 5-methyltetrahydrofolate, mechanism, overview
S,S-dimethyl-beta-propiothetin + tetrahydrofolate = 3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
concerted mechanism in which methyl transfer is coupled to proton transfer
S,S-dimethyl-beta-propiothetin + tetrahydrofolate = 3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
concerted mechanism in which methyl transfer is coupled to proton transfer
Candidatus Pelagibacter communis HTCC1062
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
demethylation
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
dimethylsulfoniopropanoate degradation III (demethylation)
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SYSTEMATIC NAME
IUBMB Comments
S,S-dimethyl-beta-propiothetin:tetrahydrofolate S-methyltransferase
The enzyme from the marine bacteria Pelagibacter ubique and Ruegeria pomeroyi are specific towards S,S-dimethyl-beta-propiothetin. They do not demethylate glycine-betaine [1,2].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-(dimethylsulfonio)propanoate + tetrahydrofolate
2-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
2-(dimethylsulfonio)propanoate + tetrahydrofolate
2-(methylthio)propanoate + 5-methyltetrahydrofolate
3-(S,S-dimethylsulfonio)propanoate + tetrahydrofolate
3-(methylthio)propanoate + 5-methyltetrahydrofolate
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
2-(dimethylsulfonio)propanoate + tetrahydrofolate
2-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
Substrates: -
Products: -
Products: -
?
2-(dimethylsulfonio)propanoate + tetrahydrofolate
2-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
Substrates: enzyme exhibits strict substrate specificity for 2-(dimethylsulfonio)propanoate
Products: -
Products: -
?
2-(dimethylsulfonio)propanoate + tetrahydrofolate
2-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
Substrates: -
Products: -
Products: -
?
2-(dimethylsulfonio)propanoate + tetrahydrofolate
2-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
Substrates: DmdA catalyzes a redox-neutral methyl transfer reaction to produce 5-methyltetrahydrofolate
Products: -
Products: -
?
2-(dimethylsulfonio)propanoate + tetrahydrofolate
2-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
Candidatus Pelagibacter communis HTCC1062
Substrates: enzyme exhibits strict substrate specificity for 2-(dimethylsulfonio)propanoate
Products: -
Products: -
?
2-(dimethylsulfonio)propanoate + tetrahydrofolate
2-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
Substrates: enzyme exhibits strict substrate specificity for 2-(dimethylsulfonio)propanoate
Products: -
Products: -
?
2-(dimethylsulfonio)propanoate + tetrahydrofolate
2-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
Substrates: -
Products: -
Products: -
?
2-(dimethylsulfonio)propanoate + tetrahydrofolate
2-(methylthio)propanoate + 5-methyltetrahydrofolate
Substrates: -
Products: -
Products: -
r
2-(dimethylsulfonio)propanoate + tetrahydrofolate
2-(methylthio)propanoate + 5-methyltetrahydrofolate
Candidatus Pelagibacter communis HTCC1062
Substrates: -
Products: -
Products: -
r
3-(S,S-dimethylsulfonio)propanoate + tetrahydrofolate
3-(methylthio)propanoate + 5-methyltetrahydrofolate
Substrates: -
Products: -
Products: -
?
3-(S,S-dimethylsulfonio)propanoate + tetrahydrofolate
3-(methylthio)propanoate + 5-methyltetrahydrofolate
Candidatus Pelagibacter communis HTCC1062
Substrates: -
Products: -
Products: -
?
3-(S,S-dimethylsulfonio)propanoate + tetrahydrofolate
3-(methylthio)propanoate + 5-methyltetrahydrofolate
Substrates: -
Products: -
Products: -
?
3-(S,S-dimethylsulfonio)propanoate + tetrahydrofolate
3-(methylthio)propanoate + 5-methyltetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
3-(S,S-dimethylsulfonio)propanoate + tetrahydrofolate
3-(methylthio)propanoate + 5-methyltetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
Substrates: -
Products: -
Products: -
?
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
Candidatus Pelagibacter communis HTCC1062
Substrates: -
Products: -
Products: -
?
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
Substrates: -
Products: -
Products: -
?
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
Substrates: -
Products: -
Products: -
?
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
Substrates: -
Products: -
Products: -
?
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: marine bacterioplankton regulate sulfur flux by converting the precursor dimethylsulfoniopropionate either to dimethylsulfide or to sulfur compounds that are not climatically active
Products: -
Products: -
?
additional information
?
-
-
Substrates: no detectable demethylase activity with glycine betaine, dimethyl glycine, methylmercaptopropionate, methionine, or dimethylsulfonioacetate. Less than 1% activity is found with dimethylsulfoniobutanoate and dimethylsulfoniopentanoate
Products: -
Products: -
?
additional information
?
-
Substrates: no detectable demethylase activity with glycine betaine, dimethyl glycine, methylmercaptopropionate, methionine, or dimethylsulfonioacetate. Less than 1% activity is found with dimethylsulfoniobutanoate and dimethylsulfoniopentanoate
Products: -
Products: -
?
additional information
?
-
-
Substrates: strict substrate specificity for dimethylsulfoniopropionate. No detectable demethylase activity with glycine betaine,dimethyl glycine, methylmercaptopropionate, methionine, or dimethylsulfonioacetate and less than 1% activity with dimethylsulfoniobutanoate and dimethylsulfoniopentanoate
Products: -
Products: -
?
additional information
?
-
Substrates: strict substrate specificity for dimethylsulfoniopropionate. No detectable demethylase activity with glycine betaine,dimethyl glycine, methylmercaptopropionate, methionine, or dimethylsulfonioacetate and less than 1% activity with dimethylsulfoniobutanoate and dimethylsulfoniopentanoate
Products: -
Products: -
?
additional information
?
-
Substrates: assay metod, overview. The substrate THF and product 5-methyl-THF are labile under aerobic conditions, oxidation of THF is irreversible and results in the release of 4-aminobenzoyl glutamate, essentially breaking the molecule in half. Half-life of THF in solution at pH 7.0 is about 40 min. DTT can stabilize THF in solution
Products: -
Products: -
?
additional information
?
-
Candidatus Pelagibacter communis HTCC1062
-
Substrates: no detectable demethylase activity with glycine betaine, dimethyl glycine, methylmercaptopropionate, methionine, or dimethylsulfonioacetate. Less than 1% activity is found with dimethylsulfoniobutanoate and dimethylsulfoniopentanoate
Products: -
Products: -
?
additional information
?
-
Candidatus Pelagibacter communis HTCC1062
Substrates: no detectable demethylase activity with glycine betaine, dimethyl glycine, methylmercaptopropionate, methionine, or dimethylsulfonioacetate. Less than 1% activity is found with dimethylsulfoniobutanoate and dimethylsulfoniopentanoate
Products: -
Products: -
?
additional information
?
-
Candidatus Pelagibacter communis HTCC1062
-
Substrates: strict substrate specificity for dimethylsulfoniopropionate. No detectable demethylase activity with glycine betaine,dimethyl glycine, methylmercaptopropionate, methionine, or dimethylsulfonioacetate and less than 1% activity with dimethylsulfoniobutanoate and dimethylsulfoniopentanoate
Products: -
Products: -
?
additional information
?
-
Candidatus Pelagibacter communis HTCC1062
Substrates: strict substrate specificity for dimethylsulfoniopropionate. No detectable demethylase activity with glycine betaine,dimethyl glycine, methylmercaptopropionate, methionine, or dimethylsulfonioacetate and less than 1% activity with dimethylsulfoniobutanoate and dimethylsulfoniopentanoate
Products: -
Products: -
?
additional information
?
-
Candidatus Pelagibacter communis HTCC1062
Substrates: assay metod, overview. The substrate THF and product 5-methyl-THF are labile under aerobic conditions, oxidation of THF is irreversible and results in the release of 4-aminobenzoyl glutamate, essentially breaking the molecule in half. Half-life of THF in solution at pH 7.0 is about 40 min. DTT can stabilize THF in solution
Products: -
Products: -
?
additional information
?
-
Substrates: no detectable demethylase activity with glycine betaine, dimethyl glycine, methylmercaptopropionate, methionine, or dimethylsulfonioacetate. Less than 1% activity is found with dimethylsulfoniobutanoate and dimethylsulfoniopentanoate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no detectable demethylase activity with glycine betaine, dimethyl glycine, methylmercaptopropionate, methionine, or dimethylsulfonioacetate. Less than 1% activity is found with dimethylsulfoniobutanoate and dimethylsulfoniopentanoate
Products: -
Products: -
?
additional information
?
-
Substrates: strict substrate specificity for dimethylsulfoniopropionate. No detectable demethylase activity with glycine betaine, dimethyl glycine, methylmercaptopropionate, methionine, or dimethylsulfonioacetate and less than 1% activity with dimethylsulfoniobutanoate and dimethylsulfoniopentanoate
Products: -
Products: -
?
additional information
?
-
-
Substrates: strict substrate specificity for dimethylsulfoniopropionate. No detectable demethylase activity with glycine betaine, dimethyl glycine, methylmercaptopropionate, methionine, or dimethylsulfonioacetate and less than 1% activity with dimethylsulfoniobutanoate and dimethylsulfoniopentanoate
Products: -
Products: -
?
additional information
?
-
Substrates: assay metod, overview. The substrate THF and product 5-methyl-THF are labile under aerobic conditions, oxidation of THF is irreversible and results in the release of 4-aminobenzoyl glutamate, essentially breaking the molecule in half. Half-life of THF in solution at pH 7.0 is about 40 min. DTT can stabilize THF in solution
Products: -
Products: -
?
additional information
?
-
Substrates: assay metod, overview. The substrate THF and product 5-methyl-THF are labile under aerobic conditions, oxidation of THF is irreversible and results in the release of 4-aminobenzoyl glutamate, essentially breaking the molecule in half. Half-life of THF in solution at pH 7.0 is about 40 min. DTT can stabilize THF in solution
Products: -
Products: -
?
additional information
?
-
Substrates: assay metod, overview. The substrate THF and product 5-methyl-THF are labile under aerobic conditions, oxidation of THF is irreversible and results in the release of 4-aminobenzoyl glutamate, essentially breaking the molecule in half. Half-life of THF in solution at pH 7.0 is about 40 min. DTT can stabilize THF in solution
Products: -
Products: -
?
additional information
?
-
Substrates: marine bacterioplankton regulate sulfur flux by converting the precursor dimethylsulfoniopropionate either to dimethylsulfide or to sulfur compounds that are not climatically active
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: betaine. Reaction does not require ATP or reductive activation by titanium(III)-nitrilotriacetic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: betaine. Reaction does not require ATP or reductive activation by titanium(III)-nitrilotriacetic acid
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-(dimethylsulfonio)propanoate + tetrahydrofolate
2-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
Substrates: -
Products: -
Products: -
?
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
Substrates: -
Products: -
Products: -
?
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
Candidatus Pelagibacter communis HTCC1062
Substrates: -
Products: -
Products: -
?
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
Substrates: -
Products: -
Products: -
?
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
Substrates: -
Products: -
Products: -
?
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
Substrates: -
Products: -
Products: -
?
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
S,S-dimethyl-beta-propiothetin + tetrahydrofolate
3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: marine bacterioplankton regulate sulfur flux by converting the precursor dimethylsulfoniopropionate either to dimethylsulfide or to sulfur compounds that are not climatically active
Products: -
Products: -
?
additional information
?
-
Substrates: marine bacterioplankton regulate sulfur flux by converting the precursor dimethylsulfoniopropionate either to dimethylsulfide or to sulfur compounds that are not climatically active
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tetrahydrofolate
-
methyl acceptor in the anaerobic demethylation of dimethylsulfoniopropionate to methylthiopropionate
tetrahydrofolate
(DMSP) demethylase is a tetrahydrofolate-dependent enzyme
tetrahydrofolate
(DMSP) demethylase is a tetrahydrofolate-dependent enzyme
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
salt solutions do not significantly stimulate activity nor are they required for enzyme stability during storage
additional information
salt solutions do not significantly stimulate activity nor are they required for enzyme stability during storage
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dimethylsulfoniobutanoate
substrate analog, weak inhibitor
dimethylsulfoniopentanoate
substrate analog, weak inhibitor
O2
-
preincubation of the extract under air decreases the activity, 35% loss in 3 h
Propyl iodide
-
0.5 mM, complete inhibition. In the light, the inhibition is far less strong
additional information
-
not inhibitory: 400 mM of (NH4)2SO4, K2HPO4, MgSO4, Na-acetate, NaCl, and KCl
-
additional information
not inhibitory: 400 mM of (NH4)2SO4, K2HPO4, MgSO4, Na-acetate, NaCl, and KCl
-
additional information
not inhibitory: 400 mM of (NH4)2SO4, K2HPO4, MgSO4, Na-acetate, NaCl, and KCl
-
additional information
-
not inhibitory: 400 mM of (NH4)2SO4, K2HPO4, MgSO4, Na-acetate, NaCl, and KCl
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.4
3-(S,S-dimethylsulfonio)propanoate
pH 7.5, temperature not specified in the publication
13.2
3-(S,S-dimethylsulfonio)propanoate
pH 7.5, temperature not specified in the publication
8.6
dimethylsulfoniopropionate
in cell extracts, similar to that of purified recombinant DmdA
13.2
S,S-dimethyl-beta-propiothetin
pH 7.5, 30°C, cell extract
0.21
tetrahydrofolate
pH 7.5, temperature not specified in the publication
0.29
tetrahydrofolate
pH 7.5, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.4
3-(S,S-dimethylsulfonio)propanoate
pH 7.5, temperature not specified in the publication
8.1
3-(S,S-dimethylsulfonio)propanoate
pH 7.5, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.45
3-(S,S-dimethylsulfonio)propanoate
pH 7.5, temperature not specified in the publication
0.618
3-(S,S-dimethylsulfonio)propanoate
pH 7.5, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.1
3-(methylthio)propanoate
pH 7.5, temperature not specified in the publication
2.1
methylmercaptopropionate
noncompetitive inhibition, product inhibition
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8
7.5
7 - 8
enzyme is more active in HEPES buffer than in MOPS or Tris-HCl buffer at the same pH
7 - 8
enzyme is more active in HEPES than in MOPS buffer, but the activities in HEPES and Tris-HCl buffers are the same
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.8
6.5 - 8.3
6 - 8.8
maximum activity is observed at pH 7.0 to 8.0, about 50% activity at pH 6.0 and 8.8
6.5 - 8.3
maximum activity is observed at pH 7.0 to 8.0, about 50% activity at pH 6.5 and 8.3
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
in phytoplankton bloom in Gulf of Mexico seawater, gene dmdA, genetic cluster identification from 578 dmdA sequences
-
-
brenda
in phytoplankton bloom in Gulf of Mexico seawater, gene dmdA, OM60 group, genetic cluster OM60-like identification from 578 dmdA sequences
-
-
brenda
in phytoplankton bloom in Gulf of Mexico seawater, gene dmdA, clade A, genetic cluster identification from 578 dmdA sequences
-
-
brenda
in phytoplankton bloom in Gulf of Mexico seawater, gene dmdA, OM60 group, genetic cluster OM60-like identification from 578 dmdA sequences
-
-
brenda
pelagibacteraceae, strains HTCC1002 and HTCC1062, in phytoplankton bloom in Gulf of Mexico seawater, gene dmdA, OM60 group, clade E, genetic cluster identification from 578 dmdA sequences
-
-
brenda
pelagibacteraceae, strains HTCC1002 and HTCC1062, in phytoplankton bloom in Gulf of Mexico seawater, gene dmdA, OM60 group, clade E, genetic cluster identification from 578 dmdA sequences
-
-
brenda
pelagibacteraceae, in phytoplankton bloom in Gulf of Mexico seawater, gene dmdA, SAR11 group, clade C, genetic cluster identification from 578 dmdA sequences
-
-
brenda
pelagibacteraceae, strains HTCC1002 and HTCC1062, in phytoplankton bloom in Gulf of Mexico seawater, gene dmdA, SAR11 group, clade D, genetic cluster identification from 578 dmdA sequences
-
-
brenda
Candidatus Pelagibacter communis HTCC7211
pelagibacteraceae, in phytoplankton bloom in Gulf of Mexico seawater, gene dmdA, SAR11 group, clade C, genetic cluster identification from 578 dmdA sequences
-
-
brenda
pelagibacteraceae, in phytoplankton bloom in Gulf of Mexico seawater, gene dmdA, SAR11 group, clade B, genetic cluster identification from 578 dmdA sequences
-
-
brenda
in phytoplankton bloom in Gulf of Mexico seawater, gene dmdA, clade A, genetic cluster identification from 578 dmdA sequences
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
-
positive correlation of katG expression with gene dmdA but not gene dddP during the period when regulation expression is uncoupled
evolution
DmdA belongs to a diverse family of enzymes, the overall fold of the DmdA is not similar to other enzymes that typically utilize the reduced form of tetrahydrofolate and in fact is a triple domain structure similar to what has been observed for the glycine cleavage T protein or sarcosine oxidase. All other THF binding fold enzymes produce 5,10-methylene-tetrahydrofolate. The relative positioning of Y206 in DmdA is different in comparison to the other THF dependent enzymes
evolution
-
phylogenetic analysis, multidimensional analysis based on the abundances of dimethylsulfoniopropionate degradation genes and environmental factors reveal that the distribution pattern of these genes is influenced by chlorophyll a concentrations and temperatures. dddP genes, dmdA subclade C/2 genes, and dmdA subclade D genes exhibit significant correlations with the marine Roseobacter clade, SAR11 subgroup Ib, and SAR11 subgroup Ia, respectively. SAR11 subgroups Ia and Ib, which possess dmdA genes, are suggested to be the main potential dimethylsulfoniopropionate consumers
evolution
-
phylogenetic analysis, multidimensional analysis based on the abundances of dimethylsulfoniopropionate degradation genes and environmental factors reveal that the distribution pattern of these genes is influenced by chlorophyll a concentrations and temperatures. dddP genes, dmdA subclade C/2 genes, and dmdA subclade D genes exhibit significant correlations with the marine Roseobacter clade, SAR11 subgroup Ib, and SAR11 subgroup Ia, respectively. SAR11 subgroups Ia and Ib, which possess dmdA genes, are suggested to be the main potential dimethylsulfoniopropionate consumers
evolution
-
phylogenetic analysis, multidimensional analysis based on the abundances of dimethylsulfoniopropionate degradation genes and environmental factors reveal that the distribution pattern of these genes is influenced by chlorophyll a concentrations and temperatures. dddP genes, dmdA subclade C/2 genes, and dmdA subclade D genes exhibit significant correlations with the marine Roseobacter clade, SAR11 subgroup Ib, and SAR11 subgroup Ia, respectively. SAR11 subgroups Ia and Ib, which possess dmdA genes, are suggested to be the main potential dimethylsulfoniopropionate consumers
evolution
-
detection of taxon-specific gene expression in Roseobacter sp. HTCC2255 and in situ regulation of the first gene in each DMSP pathway, gene dddP and gene dmdA, that corresponds with shifts in the taxonomy of the phytoplankton community
evolution
-
analysis of diversity of genes encoding DMSP demethylase (dmdA) and DMSP lyases (dddD, dddL, and dddP) in bacteria in the surface seawater of Ardley Cove and Great Wall Cove in Antarctic Maxwell Bay using DMSP degradation gene clone library analysis, overview. Both bacterial dmdA and dddP genes found in the two coves are completely confined to the Roseobacter clade, which indicated that this clade plays a significant role in DMSP catabolism in the coastal seawaters of Maxwell Bay. Diversity and distribution of dmdA genes within the Roseobacter clade, including the genera Litoreibacter, Loktanella, Octadecabacter, Roseobacter, Ruegeria, and Sulfitobacter, phylogenetic tree, overview
evolution
-
analysis of diversity of genes encoding DMSP demethylase (dmdA) and DMSP lyases (dddD, dddL, and dddP) in bacteria in the surface seawater of Ardley Cove and Great Wall Cove in Antarctic Maxwell Bay using DMSP degradation gene clone library analysis, overview. Both bacterial dmdA and dddP genes found in the two coves are completely confined to the Roseobacter clade, which indicated that this clade plays a significant role in DMSP catabolism in the coastal seawaters of Maxwell Bay. Diversity and distribution of dmdA genes within the Roseobacter clade, including the genera Litoreibacter, Loktanella, Octadecabacter, Roseobacter, Ruegeria, and Sulfitobacter, phylogenetic tree, overview
evolution
-
analysis of diversity of genes encoding DMSP demethylase (dmdA) and DMSP lyases (dddD, dddL, and dddP) in bacteria in the surface seawater of Ardley Cove and Great Wall Cove in Antarctic Maxwell Bay using DMSP degradation gene clone library analysis, overview. Both bacterial dmdA and dddP genes found in the two coves are completely confined to the Roseobacter clade, which indicated that this clade plays a significant role in DMSP catabolism in the coastal seawaters of Maxwell Bay. Diversity and distribution of dmdA genes within theRoseobacter clade, including the genera Litoreibacter, Loktanella, Octadecabacter, Roseobacter, Ruegeria, and Sulfitobacter, phylogenetic tree, overview
evolution
-
analysis of diversity of genes encoding DMSP demethylase (dmdA) and DMSP lyases (dddD, dddL, and dddP) in bacteria in the surface seawater of Ardley Cove and Great Wall Cove in Antarctic Maxwell Bay using DMSP degradation gene clone library analysis, overview. Both bacterial dmdA and dddP genes found in the two coves are completely confined to the Roseobacter clade, which indicated that this clade plays a significant role in DMSP catabolism in the coastal seawaters of Maxwell Bay. Diversity and distribution of dmdA genes within theRoseobacter clade, including the genera Litoreibacter, Loktanella, Octadecabacter, Roseobacter, Ruegeria, and Sulfitobacter, phylogenetic tree, overview
evolution
-
analysis of diversity of genes encoding DMSP demethylase (dmdA) and DMSP lyases (dddD, dddL, and dddP) in bacteria in the surface seawater of Ardley Cove and Great Wall Cove in Antarctic Maxwell Bay using DMSP degradation gene clone library analysis, overview. Both bacterial dmdA and dddP genes found in the two coves are completely confined to the Roseobacter clade, which indicated that this clade plays a significant role in DMSP catabolism in the coastal seawaters of Maxwell Bay. Diversity and distribution of dmdA genes within theRoseobacter clade, including the genera Litoreibacter, Loktanella, Octadecabacter, Roseobacter, Ruegeria, and Sulfitobacter, phylogenetic tree, overview
evolution
-
analysis of diversity of genes encoding DMSP demethylase (dmdA) and DMSP lyases (dddD, dddL, and dddP) in bacteria in the surface seawater of Ardley Cove and Great Wall Cove in Antarctic Maxwell Bay using DMSP degradation gene clone library analysis, overview. Both bacterial dmdA and dddP genes found in the two coves are completely confined to the Roseobacter clade, which indicated that this clade plays a significant role in DMSP catabolism in the coastal seawaters of Maxwell Bay. Diversity and distribution of dmdA genes within theRoseobacter clade, including the genera Litoreibacter, Loktanella, Octadecabacter, Roseobacter, Ruegeria, and Sulfitobacter, phylogenetic tree, overview
evolution
though DmdA is homologous to the glycine cleavage T-protein and shares structural similarity, the mechanism of carbon transfer is more similar to S-adenosyl-methionine (SAM)-dependent methyl-transfer enzymes. DmdA catalyzes the transfer of a methyl group to form 5-methyl-THF, which is analogous to SAM-dependent reactions. The gene dmdA is abundant in marine waters
evolution
though DmdA is homologous to the glycine cleavage T-protein and shares structural similarity, the mechanism of carbon transfer is more similar to S-adenosyl-methionine (SAM)-dependent methyl-transfer enzymes. DmdA catalyzes the transfer of a methyl group to form 5-methyl-THF, which is analogous to SAM-dependent reactions. The gene dmdA is abundant in marine waters
evolution
Candidatus Pelagibacter communis HTCC1062
-
though DmdA is homologous to the glycine cleavage T-protein and shares structural similarity, the mechanism of carbon transfer is more similar to S-adenosyl-methionine (SAM)-dependent methyl-transfer enzymes. DmdA catalyzes the transfer of a methyl group to form 5-methyl-THF, which is analogous to SAM-dependent reactions. The gene dmdA is abundant in marine waters
-
evolution
-
though DmdA is homologous to the glycine cleavage T-protein and shares structural similarity, the mechanism of carbon transfer is more similar to S-adenosyl-methionine (SAM)-dependent methyl-transfer enzymes. DmdA catalyzes the transfer of a methyl group to form 5-methyl-THF, which is analogous to SAM-dependent reactions. The gene dmdA is abundant in marine waters
-
evolution
-
phylogenetic analysis, multidimensional analysis based on the abundances of dimethylsulfoniopropionate degradation genes and environmental factors reveal that the distribution pattern of these genes is influenced by chlorophyll a concentrations and temperatures. dddP genes, dmdA subclade C/2 genes, and dmdA subclade D genes exhibit significant correlations with the marine Roseobacter clade, SAR11 subgroup Ib, and SAR11 subgroup Ia, respectively. SAR11 subgroups Ia and Ib, which possess dmdA genes, are suggested to be the main potential dimethylsulfoniopropionate consumers
-
evolution
-
detection of taxon-specific gene expression in Roseobacter sp. HTCC2255 and in situ regulation of the first gene in each DMSP pathway, gene dddP and gene dmdA, that corresponds with shifts in the taxonomy of the phytoplankton community
-
evolution
-
though DmdA is homologous to the glycine cleavage T-protein and shares structural similarity, the mechanism of carbon transfer is more similar to S-adenosyl-methionine (SAM)-dependent methyl-transfer enzymes. DmdA catalyzes the transfer of a methyl group to form 5-methyl-THF, which is analogous to SAM-dependent reactions. The gene dmdA is abundant in marine waters
-
metabolism
-
the enzyme catalyzes the first step of the dimethylsulfoniopropionate, DMSP, cleavage pathway. DMSP is a ubiquitous phytoplankton metabolite that is degraded by marine microorganisms by at least two major pathways
metabolism
-
the enzyme catalyzes the first step of the dimethylsulfoniopropionate, DMSP, cleavage pathway. DMSP is a ubiquitous phytoplankton metabolite that is degraded by marine microorganisms by at least two major pathways
metabolism
-
the enzyme catalyzes the first step of the dimethylsulfoniopropionate, DMSP, cleavage pathway. DMSP is a ubiquitous phytoplankton metabolite that is degraded by marine microorganisms by at least two major pathways
metabolism
-
the enzyme catalyzes the first step of the dimethylsulfoniopropionate, DMSP, cleavage pathway. DMSP is a ubiquitous phytoplankton metabolite that is degraded by marine microorganisms by at least two major pathways
metabolism
-
the enzyme catalyzes the first step of the dimethylsulfoniopropionate, DMSP, cleavage pathway. DMSP is a ubiquitous phytoplankton metabolite that is degraded by marine microorganisms by at least two major pathways
metabolism
-
the enzyme catalyzes the first step of the dimethylsulfoniopropionate, DMSP, cleavage pathway. DMSP is a ubiquitous phytoplankton metabolite that is degraded by marine microorganisms by at least two major pathways
metabolism
-
the enzyme catalyzes the first step of the dimethylsulfoniopropionate, DMSP, cleavage pathway. DMSP is a ubiquitous phytoplankton metabolite that is degraded by marine microorganisms by at least two major pathways
metabolism
-
the enzyme catalyzes the first step of the dimethylsulfoniopropionate, DMSP, cleavage pathway. DMSP is a ubiquitous phytoplankton metabolite that is degraded by marine microorganisms by at least two major pathways
metabolism
-
the bacterial switch is a proposed regulatory point in the global sulfur cycle that routes dimethylsulfoniopropionate to two fundamentally different fates in seawater through genes encoding either the cleavage or demethylation pathway, and affects the flux of volatile sulfur from ocean surface waters to the atmosphere
metabolism
-
the bacterial switch is a proposed regulatory point in the global sulfur cycle that routes dimethylsulfoniopropionate to two fundamentally different fates in seawater through genes encoding either the cleavage or demethylation pathway, and affects the flux of volatile sulfur from ocean surface waters to the atmosphere
metabolism
-
both bipolar and endemic bacterial DMSP degradation genes exist in polar marine environments
metabolism
-
both bipolar and endemic bacterial DMSP degradation genes exist in polar marine environments
metabolism
-
both bipolar and endemic bacterial DMSP degradation genes exist in polar marine environments
metabolism
-
both bipolar and endemic bacterial DMSP degradation genes exist in polar marine environments
metabolism
-
both bipolar and endemic bacterial DMSP degradation genes exist in polar marine environments
metabolism
-
both bipolar and endemic bacterial DMSP degradation genes exist in polar marine environments
metabolism
Candidatus Pelagibacter communis HTCC7211
-
the enzyme catalyzes the first step of the dimethylsulfoniopropionate, DMSP, cleavage pathway. DMSP is a ubiquitous phytoplankton metabolite that is degraded by marine microorganisms by at least two major pathways
-
metabolism
-
the enzyme catalyzes the first step of the dimethylsulfoniopropionate, DMSP, cleavage pathway. DMSP is a ubiquitous phytoplankton metabolite that is degraded by marine microorganisms by at least two major pathways
-
metabolism
-
the bacterial switch is a proposed regulatory point in the global sulfur cycle that routes dimethylsulfoniopropionate to two fundamentally different fates in seawater through genes encoding either the cleavage or demethylation pathway, and affects the flux of volatile sulfur from ocean surface waters to the atmosphere
-
physiological function
-
DMSP demethylase is responsible for the dimethylsulfoniopropionate assimilation
physiological function
-
DMSP demethylase is responsible for the dimethylsulfoniopropionate assimilation
physiological function
-
DMSP demethylase is responsible for the dimethylsulfoniopropionate assimilation
physiological function
-
Roseobacter plays a significant role in DMSP catabolism in the coastal seawaters of Maxwell Bay
physiological function
-
Roseobacter plays a significant role in DMSP catabolism in the coastal seawaters of Maxwell Bay
physiological function
-
Roseobacter plays a significant role in DMSP catabolism in the coastal seawaters of Maxwell Bay
physiological function
-
Roseobacter plays a significant role in DMSP catabolism in the coastal seawaters of Maxwell Bay
physiological function
-
Roseobacter plays a significant role in DMSP catabolism in the coastal seawaters of Maxwell Bay
physiological function
-
Roseobacter plays a significant role in DMSP catabolism in the coastal seawaters of Maxwell Bay
physiological function
dimethylsulfoniopropionate (DMSP) demethylase is a tetrahydrofolate-dependent enzyme that initiates the DMSP demethylation pathway in marine bacteria. This enzyme is important for understanding of organic sulfur flux from the oceans because it directs the sulfur from DMSP away from dimethylsulfide
physiological function
dimethylsulfoniopropionate (DMSP) demethylase is a tetrahydrofolate-dependent enzyme that initiates the DMSP demethylation pathway in marine bacteria. This enzyme is important for understanding of organic sulfur flux from the oceans because it directs the sulfur from DMSP away from dimethylsulfide
physiological function
Candidatus Pelagibacter communis HTCC1062
-
dimethylsulfoniopropionate (DMSP) demethylase is a tetrahydrofolate-dependent enzyme that initiates the DMSP demethylation pathway in marine bacteria. This enzyme is important for understanding of organic sulfur flux from the oceans because it directs the sulfur from DMSP away from dimethylsulfide
-
physiological function
-
dimethylsulfoniopropionate (DMSP) demethylase is a tetrahydrofolate-dependent enzyme that initiates the DMSP demethylation pathway in marine bacteria. This enzyme is important for understanding of organic sulfur flux from the oceans because it directs the sulfur from DMSP away from dimethylsulfide
-
physiological function
-
DMSP demethylase is responsible for the dimethylsulfoniopropionate assimilation
-
physiological function
-
dimethylsulfoniopropionate (DMSP) demethylase is a tetrahydrofolate-dependent enzyme that initiates the DMSP demethylation pathway in marine bacteria. This enzyme is important for understanding of organic sulfur flux from the oceans because it directs the sulfur from DMSP away from dimethylsulfide
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DMDA_PELUB
Pelagibacter ubique (strain HTCC1062)
369
0
41832
Swiss-Prot
other Location (Reliability: 3)
DMDA_RUEPO
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
364
0
39895
Swiss-Prot
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38500
68000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
dimer
under nondenaturing conditions, MW is 68000 Da, suggesting that the enzyme is likely to be a dimer
dimer
Candidatus Pelagibacter communis HTCC1062
-
under nondenaturing conditions, MW is 68000 Da, suggesting that the enzyme is likely to be a dimer
-
additional information
-
structure of apoenzyme DmdA and domain architecture, overview
additional information
structure of apoenzyme DmdA and domain architecture, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant DmdA alone or in complex with substrate 2-(dimethylsulfonio)propanoate or cofactor tetrahydrofolate, mother liquor consists of 325 mM NaCl, 30% PEG 2000, 25 mM HEPES, pH 6.8. method optimization, soaking in solution containing 2 mM DMSP or 2 mM tetrahydrofolate, X-ray diffraction structure determination and analysis at 2.1 A and 1.6 A resolution, respectively, modeling
structure of the apoenzyme DmdA to 2.1 A, as well as for co-crystals soaked with substrate dimethylsulfoniopropionate to 1.6 A or the cofactor tetrahydrofolate to 1.6 A. The overall fold is a triple domain structure similar to what has been observed for the glycine cleavage T protein or sarcosine oxidase. The tetrahydrofolate binding fold appears conserved
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
salt solutions do not significantly stimulate activity nor are they required for enzyme stability during storage
salt solutions do not significantly stimulate activity nor are they required for enzyme stability during storage
salt solutions do not significantly stimulate activity nor are they required for enzyme stability during storage
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, enzyme in cell-free extract, in presence of EDTA and 20% glycerol, several weeks without significant loss of activity
4C, enzyme in cell-free extract, in presence of EDTA, several weeks without significant loss of activity. Without addition of EDTA, the enzyme loses all activity over the course of several days
-20C, enzyme in cell-free extract, in presence of EDTA and 20% glycerol, several weeks without significant loss of activity
-20C, enzyme in cell-free extract, in presence of EDTA and 20% glycerol, several weeks without significant loss of activity
4C, enzyme in cell-free extract, in presence of EDTA, several weeks without significant loss of activity. Without addition of EDTA, the enzyme loses all activity over the course of several days
4C, enzyme in cell-free extract, in presence of EDTA, several weeks without significant loss of activity. Without addition of EDTA, the enzyme loses all activity over the course of several days
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
anion-exchange, hydrophobic interaction, and hydroxyapatite chromatographies
recombinant protein
anion-exchange, hydrophobic interaction, and hydroxyapatite chromatographies
anion-exchange, hydrophobic interaction, and hydroxyapatite chromatographies
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene dmdA, functional recombinant expression in Escherichia coli
gene dmdA, genetic cluster identification from 578 dmdA sequences from seawater plankton probes, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene dmdA, genotyping and expression analysis in relation to the phytoplankton dynamics in Monterey Bay
-
gene dmdA, genotyping in marine bacteria, overview
gene dmdA, genotyping in samples collected from the surface seawater of Ardley Cove and Great Wall Cove in Antarctic Maxwell Bay, clone library construction and sequencing, determination of GenBank IDs KF153913-KF153928 and KF486968-KF487000 for dmdA genes from uncultured bacteria, phylogenetic tree, overview
synthesized and introduced in trans into Escherichia coli
gene dmdA, functional recombinant expression in Escherichia coli
gene dmdA, genetic cluster identification from 578 dmdA sequences from seawater plankton probes, DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
gene dmdA, genetic cluster identification from 578 dmdA sequences from seawater plankton probes, DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
gene dmdA, genetic cluster identification from 578 dmdA sequences from seawater plankton probes, DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
gene dmdA, genetic cluster identification from 578 dmdA sequences from seawater plankton probes, DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
gene dmdA, genotyping in samples collected from the surface seawater of Ardley Cove and Great Wall Cove in Antarctic Maxwell Bay, clone library construction and sequencing, determination of GenBank IDs KF153913-KF153928 and KF486968-KF487000 for dmdA genes from uncultured bacteria, phylogenetic tree, overview
-
gene dmdA, genotyping in samples collected from the surface seawater of Ardley Cove and Great Wall Cove in Antarctic Maxwell Bay, clone library construction and sequencing, determination of GenBank IDs KF153913-KF153928 and KF486968-KF487000 for dmdA genes from uncultured bacteria, phylogenetic tree, overview
-
gene dmdA, genotyping in samples collected from the surface seawater of Ardley Cove and Great Wall Cove in Antarctic Maxwell Bay, clone library construction and sequencing, determination of GenBank IDs KF153913-KF153928 and KF486968-KF487000 for dmdA genes from uncultured bacteria, phylogenetic tree, overview
-
gene dmdA, genotyping in samples collected from the surface seawater of Ardley Cove and Great Wall Cove in Antarctic Maxwell Bay, clone library construction and sequencing, determination of GenBank IDs KF153913-KF153928 and KF486968-KF487000 for dmdA genes from uncultured bacteria, phylogenetic tree, overview
-
gene dmdA, genotyping in samples collected from the surface seawater of Ardley Cove and Great Wall Cove in Antarctic Maxwell Bay, clone library construction and sequencing, determination of GenBank IDs KF153913-KF153928 and KF486968-KF487000 for dmdA genes from uncultured bacteria, phylogenetic tree, overview
-
gene dmdA, genotyping in samples collected from the surface seawater of Ardley Cove and Great Wall Cove in Antarctic Maxwell Bay, clone library construction and sequencing, determination of GenBank IDs KF153913-KF153928 and KF486968-KF487000 for dmdA genes from uncultured bacteria, phylogenetic tree, overview
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
dimethylsulfoniopropionate (DMSP) induces gene dmdA transcription
dimethylsulfoniopropionate (DMSP) induces gene dmdA transcription
dimethylsulfoniopropionate (DMSP) induces gene dmdA transcription
Candidatus Pelagibacter communis HTCC1062
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Reisch, C.R.; Moran, M.A.; Whitman, W.B.
Dimethylsulfoniopropionate-dependent demethylase (DmdA) from Pelagibacter ubique and Silicibacter pomeroyi
J. Bacteriol.
190
8018-8024
2008
Candidatus Pelagibacter communis, Candidatus Pelagibacter communis (Q4FP21), Candidatus Pelagibacter communis HTCC1062, Candidatus Pelagibacter communis HTCC1062 (Q4FP21), Ruegeria pomeroyi (Q5LS57), Ruegeria pomeroyi
brenda
Howard, E.C.; Henriksen, J.R.; Buchan, A.; Reisch, C.R.; Brgmann, H.; Welsh, R.; Ye, W.; Gonzlez, J.M.; Mace, K.; Joye, S.B.; Kiene, R.P.; Whitman, W.B.; Moran, M.A.
Bacterial taxa that limit sulfur flux from the ocean
Science
314
649-652
2006
Candidatus Pelagibacter communis (Q4FP21), Ruegeria pomeroyi DSS-3 (Q5LS57)
brenda
Howard, E.C.; Sun, S.; Reisch, C.R.; del Valle, D.A.; Buergmann, H.; Kiene, R.P.; Moran, M.A.
Changes in dimethylsulfoniopropionate demethylase gene assemblages in response to an induced phytoplankton bloom
Appl. Environ. Microbiol.
77
524-531
2011
Candidatus Pelagibacter communis, Candidatus Pelagibacter communis HTCC7211, Candidatus Puniceispirillum marinum, Flavobacteriaceae, Rhodobacterales, Rhodospirillales, Roseobacter sp., Sphingomonadales, unidentified marine bacterioplankton, unidentified marine bacterioplankton HTCC2080
brenda
Schuller, D.J.; Reisch, C.R.; Moran, M.A.; Whitman, W.B.; Lanzilotta, W.N.
Structures of dimethylsulfoniopropionate-dependent demethylase from the marine organism Pelagabacter ubique
Protein Sci.
21
289-298
2012
Candidatus Pelagibacter communis, Candidatus Pelagibacter communis (Q4FP21), Candidatus Pelagibacter communis HTCC1062 (Q4FP21)
brenda
Jansen, M.; Hansen, T.A.
Tetrahydrofolate serves as a methyl acceptor in the demethylation of dimethylsulfoniopropionate in cell extracts of sulfate-reducing bacteria
Arch. Microbiol.
169
84-87
1998
uncultured bacterium, uncultured bacterium WN
brenda
Cui, Y.; Suzuki, S.; Omori, Y.; Wong, S.K.; Ijichi, M.; Kaneko, R.; Kameyama, S.; Tanimoto, H.; Hamasaki, K.
Abundance and distribution of dimethylsulfoniopropionate degradation genes and the corresponding bacterial community structure at dimethyl sulfide hot spots in the tropical and subtropical pacific ocean
Appl. Environ. Microbiol.
81
4184-4194
2015
Candidatus Pelagibacter communis, Candidatus Pelagibacter communis HTCC7211, Candidatus Puniceispirillum marinum, Candidatus Puniceispirillum marinum IMCC1322, Roseobacter sp.
brenda
Varaljay, V.A.; Robidart, J.; Preston, C.M.; Gifford, S.M.; Durham, B.P.; Burns, A.S.; Ryan, J.P.; Marin, R.; Kiene, R.P.; Zehr, J.P.; Scholin, C.A.; Moran, M.A.
Single-taxon field measurements of bacterial gene regulation controlling DMSP fate
ISME J.
9
1677-1686
2015
Roseobacter sp., Roseobacter sp. HTCC 2255, Ruegeria pomeroyi
brenda
Zeng, Y.X.; Qiao, Z.Y.
Diversity of dimethylsulfoniopropionate degradation genes reveals the significance of marine Roseobacter clade in sulfur metabolism in coastal areas of antarctic Maxwell Bay
Curr. Microbiol.
76
967-974
2019
Litoreibacter sp., Loktanella sp., Octadecabacter sp., Roseobacter sp., Ruegeria sp., Sulfitobacter sp.
brenda
Reisch, C.R.
Assay and analysis of dimethylsulfoniopropionate demethylase
Methods Enzymol.
605
325-333
2018
Candidatus Pelagibacter communis (Q4FP21), Candidatus Pelagibacter communis HTCC1062 (Q4FP21), Ruegeria pomeroyi (Q5LS57), Ruegeria pomeroyi ATCC 700808 (Q5LS57), Ruegeria pomeroyi DSM 15171 (Q5LS57)
brenda
EXTERNAL LINKS (specific for EC-Number 2.1.1.269)
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