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EC Tree
IUBMB Comments The enzyme, characterized from Pseudomonas strains, allows the organisms to utilize methanesulfonate as their sulfur source. It acts in combination with a dedicated NADH-dependent FMN reductase (EC 1.5.1.42), which provides it with reduced FMN. cf. EC 1.14.13.111, methanesulfonate monooxygenase (NADH).
The enzyme appears in viruses and cellular organisms
Synonyms
msuD ,
snfG , SsuD,
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msuD
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SsuD
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methanesulfonate + FMNH2 + O2 = formaldehyde + FMN + sulfite + H2O
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methanesulfonate,FMNH2:oxygen oxidoreductase
The enzyme, characterized from Pseudomonas strains, allows the organisms to utilize methanesulfonate as their sulfur source. It acts in combination with a dedicated NADH-dependent FMN reductase (EC 1.5.1.42), which provides it with reduced FMN. cf. EC 1.14.13.111, methanesulfonate monooxygenase (NADH).
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ethanesulfonate + FMNH2 + O2
acetaldehyde + FMN + sulfite + H2O
isethionate + FMNH2 + O2
hydroxyacetaldehyde + FMN + sulfite + H2O
methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
morpholinepropanesulfonic acid + FMNH2 + O2
3-(morpholin-4-yl)propanal + FMN + sulfite + H2O
pentanesulfonate + FMNH2 + O2
pentanal + FMN + sulfite + H2O
piperazine-N,N'-bis(2-ethanesulfonic acid) + 2 FMNH2 + 2 O2
2,2'-piperazine-1,4-diyldiacetaldehyde + 2 FMN + 2 sulfite + 2 H2O
31% of the activity with methanesulfonate
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additional information
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ethanesulfonate + FMNH2 + O2
acetaldehyde + FMN + sulfite + H2O
27% of the activity with methanesulfonate
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ethanesulfonate + FMNH2 + O2
acetaldehyde + FMN + sulfite + H2O
27% of the activity with methanesulfonate
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isethionate + FMNH2 + O2
hydroxyacetaldehyde + FMN + sulfite + H2O
19% of the activity with methanesulfonate
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isethionate + FMNH2 + O2
hydroxyacetaldehyde + FMN + sulfite + H2O
19% of the activity with methanesulfonate
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methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
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methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
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methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
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methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
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methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
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methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
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morpholinepropanesulfonic acid + FMNH2 + O2
3-(morpholin-4-yl)propanal + FMN + sulfite + H2O
17% of the activity with methanesulfonate
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morpholinepropanesulfonic acid + FMNH2 + O2
3-(morpholin-4-yl)propanal + FMN + sulfite + H2O
17% of the activity with methanesulfonate
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pentanesulfonate + FMNH2 + O2
pentanal + FMN + sulfite + H2O
13% of the activity with methanesulfonate
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pentanesulfonate + FMNH2 + O2
pentanal + FMN + sulfite + H2O
13% of the activity with methanesulfonate
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pentanesulfonate + FMNH2 + O2
pentanal + FMN + sulfite + H2O
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pentanesulfonate + FMNH2 + O2
pentanal + FMN + sulfite + H2O
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additional information
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no substrates: DMSO, dimethyl sulfone
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additional information
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no substrates: DMSO, dimethyl sulfone
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methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
pentanesulfonate + FMNH2 + O2
pentanal + FMN + sulfite + H2O
additional information
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methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
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methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
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pentanesulfonate + FMNH2 + O2
pentanal + FMN + sulfite + H2O
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pentanesulfonate + FMNH2 + O2
pentanal + FMN + sulfite + H2O
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additional information
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no substrates: DMSO, dimethyl sulfone
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additional information
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no substrates: DMSO, dimethyl sulfone
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121000
substrate methanesulfonate, pH 8.0, 30°C
82900
substrate pentanesulfonate, pH 8.0, 30°C
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brenda
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UniProt
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UniProt
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UniProt
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UniProt
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physiological function
methanesulfonate is a metabolic intermediate of dimethyl sulfide and desulfonated by monooxygenase SsuD. SsuD is essential for desulfonation, but disruption of the SsuD gene does not affect utilization of pentanesulfonate or butanesulfonate
physiological function
the MsuD protein catalyzes the desulfonation of alkanesulfonates, requiring oxygen and FMNH2 for the reaction, and shows highest activity with methanesulfonate. NADH-dependent flavin mononucleotide reductase MsuE provides reduced FMN for the MsuD enzyme. Putative monooxygenase MsuC is involved but not essential in the desulfonation process
physiological function
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the MsuD protein catalyzes the desulfonation of alkanesulfonates, requiring oxygen and FMNH2 for the reaction, and shows highest activity with methanesulfonate. NADH-dependent flavin mononucleotide reductase MsuE provides reduced FMN for the MsuD enzyme. Putative monooxygenase MsuC is involved but not essential in the desulfonation process
physiological function
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methanesulfonate is a metabolic intermediate of dimethyl sulfide and desulfonated by monooxygenase SsuD. SsuD is essential for desulfonation, but disruption of the SsuD gene does not affect utilization of pentanesulfonate or butanesulfonate
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SSUD_PSEPU
382
0
41553
Swiss-Prot
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MSUD_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
381
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41596
Swiss-Prot
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x * 41600, calculated
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x * 41600, calculated
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expression in Escherichia coli
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expression of the msu operon is derepressed during growth with methionine or alkanesulfonates
expression of the msu operon is repressed in the presence of sulfate, sulfite, sulfide, or cysteine
growth with methanesulfonate requires an intact cysB gene, and the msu operon is part of the cys regulon
expression of the msu operon is derepressed during growth with methionine or alkanesulfonates
expression of the msu operon is derepressed during growth with methionine or alkanesulfonates
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expression of the msu operon is repressed in the presence of sulfate, sulfite, sulfide, or cysteine
expression of the msu operon is repressed in the presence of sulfate, sulfite, sulfide, or cysteine
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growth with methanesulfonate requires an intact cysB gene, and the msu operon is part of the cys regulon
growth with methanesulfonate requires an intact cysB gene, and the msu operon is part of the cys regulon
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Borodina, E.; Kelly, D.; Rainey, F.; Ward-Rainey, N.; Wood, A.
Dimethylsulfone as a growth substrate for novel methylotrophic species of Hyphomicrobium and Arthrobacter
Arch. Microbiol.
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425-437
2000
Hyphomicrobium sulfonivorans
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Endoh, T.; Kasuga, K.; Horinouchi, M.; Yoshida, T.; Habe, H.; Nojiri, H.; Omori, T.
Characterization and identification of genes essential for dimethyl sulfide utilization in Pseudomonas putida strain DS1
Appl. Microbiol. Biotechnol.
62
83-91
2003
Pseudomonas putida (O85764), Pseudomonas putida DS1 (O85764)
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Kertesz, M.A.; Schmidt-Larbig, K.; Wueest, T.
A novel reduced flavin mononucleotide-dependent methanesulfonate sulfonatase encoded by the sulfur-regulated msu operon of Pseudomonas aeruginosa
J. Bacteriol.
181
1464-1473
1999
Pseudomonas aeruginosa (Q9I1C2), Pseudomonas aeruginosa DSM 22644 (Q9I1C2)
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Enzyme Nomenclature
1.14.14.34 methanesulfonate monooxygenase (FMNH2)
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