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Information on EC 1.14.14.34 - methanesulfonate monooxygenase (FMNH2)
for references in articles please use BRENDA:EC1.14.14.34
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
1.14.14.34 methanesulfonate monooxygenase (FMNH2)
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
showSynonyms
msuD, snfG, SsuD, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
msuD
snfG
-
-
-
-
SsuD
msuD
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
methanesulfonate + FMNH2 + O2 = formaldehyde + FMN + sulfite + H2O
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-
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SYSTEMATIC NAME
IUBMB Comments
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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
morpholinepropanesulfonic acid + FMNH2 + O2
3-(morpholin-4-yl)propanal + 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
ethanesulfonate + FMNH2 + O2
acetaldehyde + FMN + sulfite + H2O
Substrates: 27% of the activity with methanesulfonate
Products: -
Products: -
?
ethanesulfonate + FMNH2 + O2
acetaldehyde + FMN + sulfite + H2O
Substrates: 27% of the activity with methanesulfonate
Products: -
Products: -
?
isethionate + FMNH2 + O2
hydroxyacetaldehyde + FMN + sulfite + H2O
Substrates: 19% of the activity with methanesulfonate
Products: -
Products: -
?
isethionate + FMNH2 + O2
hydroxyacetaldehyde + FMN + sulfite + H2O
Substrates: 19% of the activity with methanesulfonate
Products: -
Products: -
?
methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
-
Substrates: -
Products: -
Products: -
?
methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
-
Substrates: -
Products: -
Products: -
?
methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
morpholinepropanesulfonic acid + FMNH2 + O2
3-(morpholin-4-yl)propanal + FMN + sulfite + H2O
Substrates: 17% of the activity with methanesulfonate
Products: -
Products: -
?
morpholinepropanesulfonic acid + FMNH2 + O2
3-(morpholin-4-yl)propanal + FMN + sulfite + H2O
Substrates: 17% of the activity with methanesulfonate
Products: -
Products: -
?
pentanesulfonate + FMNH2 + O2
pentanal + FMN + sulfite + H2O
Substrates: 13% of the activity with methanesulfonate
Products: -
Products: -
?
pentanesulfonate + FMNH2 + O2
pentanal + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
pentanesulfonate + FMNH2 + O2
pentanal + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
piperazine-N,N'-bis(2-ethanesulfonic acid) + 2 FMNH2 + 2 O2
2,2'-piperazine-1,4-diyldiacetaldehyde + 2 FMN + 2 sulfite + 2 H2O
Substrates: 31% of the activity with methanesulfonate
Products: -
Products: -
?
piperazine-N,N'-bis(2-ethanesulfonic acid) + 2 FMNH2 + 2 O2
2,2'-piperazine-1,4-diyldiacetaldehyde + 2 FMN + 2 sulfite + 2 H2O
Substrates: 31% of the activity with methanesulfonate
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: DMSO, dimethyl sulfone
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: DMSO, dimethyl sulfone
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
methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
pentanesulfonate + FMNH2 + O2
pentanal + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
pentanesulfonate + FMNH2 + O2
pentanal + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: DMSO, dimethyl sulfone
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: DMSO, dimethyl sulfone
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
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
physiological function
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
-
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
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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). MSUD_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
381
0
41596
Swiss-Prot
Secretory Pathway (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
-
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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-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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.
173
425-437
2000
Hyphomicrobium sulfonivorans
brenda
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)
brenda
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)
brenda
EXTERNAL LINKS (specific for EC-Number 1.14.14.34)
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Release 2026.1 (March 2026)
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