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IUBMB CommentsA flavoprotein. Methanesulfonate is the simplest of the sulfonates and is a substrate for the growth of certain methylotrophic microorganisms. Compared with EC 1.14.14.5, alkanesulfonate monooxygenase, this enzyme has a restricted substrate range that includes only the short-chain aliphatic sulfonates (methanesulfonate to butanesulfonate) and excludes all larger molecules, such as arylsulfonates . The enzyme from the bacterium Methylosulfonomonas methylovora is a multicomponent system comprising a hydroxylase, a reductase (MsmD) and a ferredoxin (MsmC). The hydroxylase has both large (MsmA) and small (MsmB) subunits, with each large subunit containing a Rieske-type [2Fe-2S] cluster. cf. EC 1.14.14.34, methanesulfonate monooxygenase (FMNH2).
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CH3SO3- + O2 + NADH + H+
?
CH3SO3- + O2 + NADH + H+
formaldehyde + HSO3- + NAD+ + H2O
methanesulfonate + NADH + H+ + O2
formaldehyde + NAD+ + sulfite + H2O
CH3SO3- + O2 + NADH + H+
?
-
no significant methanesulfonate monooxygenase activity can be detected when NADPH replaces NADH
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-
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CH3SO3- + O2 + NADH + H+
?
-
-
-
-
?
CH3SO3- + O2 + NADH + H+
?
-
-
-
-
?
CH3SO3- + O2 + NADH + H+
formaldehyde + HSO3- + NAD+ + H2O
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-
-
-
?
CH3SO3- + O2 + NADH + H+
formaldehyde + HSO3- + NAD+ + H2O
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MSAMO is specifically induced during growth on methanesulfonate
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-
?
CH3SO3- + O2 + NADH + H+
formaldehyde + HSO3- + NAD+ + H2O
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-
-
-
?
CH3SO3- + O2 + NADH + H+
formaldehyde + HSO3- + NAD+ + H2O
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MSAMO is specifically induced during growth on methanesulfonate
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-
?
CH3SO3- + O2 + NADH + H+
formaldehyde + HSO3- + NAD+ + H2O
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-
-
-
?
methanesulfonate + NADH + H+ + O2
formaldehyde + NAD+ + sulfite + H2O
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-
-
?
methanesulfonate + NADH + H+ + O2
formaldehyde + NAD+ + sulfite + H2O
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-
-
?
methanesulfonate + NADH + H+ + O2
formaldehyde + NAD+ + sulfite + H2O
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-
-
?
methanesulfonate + NADH + H+ + O2
formaldehyde + NAD+ + sulfite + H2O
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-
-
?
methanesulfonate + NADH + H+ + O2
formaldehyde + NAD+ + sulfite + H2O
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-
-
?
methanesulfonate + NADH + H+ + O2
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
methanesulfonate + NADH + H+ + O2
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
methanesulfonate + NADH + H+ + O2
formaldehyde + NAD+ + sulfite + H2O
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-
-
?
methanesulfonate + NADH + H+ + O2
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
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CH3SO3- + O2 + NADH + H+
formaldehyde + HSO3- + NAD+ + H2O
methanesulfonate + NADH + H+ + O2
formaldehyde + NAD+ + sulfite + H2O
CH3SO3- + O2 + NADH + H+
formaldehyde + HSO3- + NAD+ + H2O
-
MSAMO is specifically induced during growth on methanesulfonate
-
-
?
CH3SO3- + O2 + NADH + H+
formaldehyde + HSO3- + NAD+ + H2O
-
MSAMO is specifically induced during growth on methanesulfonate
-
-
?
methanesulfonate + NADH + H+ + O2
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
methanesulfonate + NADH + H+ + O2
formaldehyde + NAD+ + sulfite + H2O
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-
-
?
methanesulfonate + NADH + H+ + O2
formaldehyde + NAD+ + sulfite + H2O
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-
-
?
methanesulfonate + NADH + H+ + O2
formaldehyde + NAD+ + sulfite + H2O
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-
-
?
methanesulfonate + NADH + H+ + O2
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
methanesulfonate + NADH + H+ + O2
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
methanesulfonate + NADH + H+ + O2
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
methanesulfonate + NADH + H+ + O2
formaldehyde + NAD+ + sulfite + H2O
-
-
-
?
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[2Fe-2S] cluster
the predicted gene product of gene msmA reveals a unique sequence in the region associated to the Rieske-type [2Fe-2S] cluster, with a longer-than-usual 26-amino acid spacer between the two highly conserved cysteine-histidine groups in the CXH-Xn-CXXH conserved motif
additional information
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chromium, cobalt, copper, lead, nickel, molybdenum, tungsten and vanadium are not detected in two-component hydroxylase of methanesulfonic acid monooxygenase
Fe2+
-
0.1 mM, stimulates
Fe2+
two iron ions per enzyme molecule
Fe2+
two iron ions per enzyme molecule
Fe2+
two iron ions per enzyme molecule
Fe2+
two iron ions per enzyme molecule
Fe2+
two iron ions per enzyme molecule
Iron
-
presence of iron-sulfur centres. The two-component hydroxylase of methanesulfonic acid monooxygenase preparations containes 1 mol sulfide and 3 mol iron per mol alphabeta-monomer
Iron
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presence on an intact Rieske-iron sulfur centre in the hydroxylase component of methanesulfonate monooxygenase
Iron
-
the electron transfer protein (MsmC) of methanesulfonic acid monooxygenase contains an iron-sulfur center with spectral characteristics similar to those of other proteins containing Rieske [2Fe-2S] centers
Iron
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the enzyme contains a two-component hydroxylase of the mononuclear-iron-center type. The large subunit of the hydroxylase (MsmA) contains a typical Rieske-type [2Fe2S] center with an unusual iron-binding motif. The reductase component (MsmD) possesses a typical chloroplast-like [2Fe2S] center
Iron
-
the ferredoxin component of the methanesulfonate monooxygenase and the hydroxylase component of methanesulfonate monooxygenase contain a Rieske [2Fe-2S] centre
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4.9
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two-component hydroxylase of methanesulfonic acid monooxygenase, chromatofocusing
5.1
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MsmD, reductase component, calculated from sequence
5.8
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MsmA, large subunit of hydroxylase component, calculated from sequence
6
-
MsmB, small subunit of hydroxylase component, calculated from sequence
3.9
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ferredoxin component of the methanesulfonate monooxygenase
3.9
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isoelectric focusing, electron transfer protein (MsmC) of methanesulfonic acid monooxygenase
3.9
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MsmC, ferredoxin component, calculated from sequence
4
-
MsmC, ferredoxin component, calculated from sequence
4
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pI calculated from sequence is 3.97, electron transfer protein (MsmC) of methanesulfonic acid monooxygenase
5.6
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beta-subunit of hydroxylase component of methanesulfonate monooxygenase
5.6
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MsmB, small subunit of hydroxylase component, calculated from sequence
6.5
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MsmD, ferredoxin component, calculated from sequence
6.5
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reductase component of methanesulfonate monooxygenase
6.7
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alpha-subunit of hydroxylase component of methanesulfonate monooxygenase
6.7
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MsmA, small subunit of hydroxylase component, calculated from sequence
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evolution
the two msm operons in Filomicrobium sp. strains Y and W are divergently transcribed, like in Methylosulfonomonas methylovora str. M2
evolution
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the two msm operons in Filomicrobium sp. strains Y and W are divergently transcribed, like in Methylosulfonomonas methylovora str. M2
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evolution
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the two msm operons in Filomicrobium sp. strains Y and W are divergently transcribed, like in Methylosulfonomonas methylovora str. M2
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physiological function
all strains isolated grow with methanesulfonate as sole carbon substrate
physiological function
the enzyme is responsible for splitting the C-S bond, catalyzing the first oxidative step of MSA to the central methylotrophic intermediate formaldehyde with the release of sulfite, which is subsequently oxidized to sulfate. Formaldehyde is assimilated through the serine cycle or fully oxidized to CO2 and H2O, in order to yield reducing power and energy
physiological function
the enzyme is responsible for splitting the C-S bond, catalyzing the first oxidative step of MSA to the central methylotrophic intermediate formaldehyde with the release of sulfite, which is subsequently oxidized to sulfate. Formaldehyde is assimilated through the serine cycle or fully oxidized to CO2 and H2O, in order to yield reducing power and energy
physiological function
the enzyme is responsible for splitting the C-S bond, catalyzing the first oxidative step of MSA to the central methylotrophic intermediate formaldehyde with the release of sulfite, which is subsequently oxidized to sulfate. Formaldehyde is assimilated through the serine cycle or fully oxidized to CO2 and H2O, in order to yield reducing power and energy
physiological function
the enzyme is responsible for splitting the C-S bond, catalyzing the first oxidative step of MSA to the central methylotrophic intermediate formaldehyde with the release of sulfite, which is subsequently oxidized to sulfate. Formaldehyde is assimilated through the serine cycle or fully oxidized to CO2 and H2O, in order to yield reducing power and energy
physiological function
the enzyme is responsible for splitting the C-S bond, catalyzing the first oxidative step of MSA to the central methylotrophic intermediate formaldehyde with the release of sulfite, which is subsequently oxidized to sulfate. Formaldehyde is assimilated through the serine cycle or fully oxidized to CO2 and H2O, in order to yield reducing power and energy
physiological function
-
the enzyme is responsible for splitting the C-S bond, catalyzing the first oxidative step of MSA to the central methylotrophic intermediate formaldehyde with the release of sulfite, which is subsequently oxidized to sulfate. Formaldehyde is assimilated through the serine cycle or fully oxidized to CO2 and H2O, in order to yield reducing power and energy
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physiological function
-
the enzyme is responsible for splitting the C-S bond, catalyzing the first oxidative step of MSA to the central methylotrophic intermediate formaldehyde with the release of sulfite, which is subsequently oxidized to sulfate. Formaldehyde is assimilated through the serine cycle or fully oxidized to CO2 and H2O, in order to yield reducing power and energy
-
physiological function
-
the enzyme is responsible for splitting the C-S bond, catalyzing the first oxidative step of MSA to the central methylotrophic intermediate formaldehyde with the release of sulfite, which is subsequently oxidized to sulfate. Formaldehyde is assimilated through the serine cycle or fully oxidized to CO2 and H2O, in order to yield reducing power and energy
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13748
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2 * 13748, electron transfer protein (MsmC) of methanesulfonic acid monooxygenase, calculated from sequence
14126
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x * 48373, large subunit of hydroxylase component (MsmA), + x * 20422, small subunit of hydroxylase component (MsmB), + x * 14126, ferredoxin component (MsmC), + x * 40106, reductase component (MsmD), calculated from sequence
20000
-
ferredoxin component of the methanesulfonate monooxygenase
200000
-
hydroxylase component of methanesulfonate monooxygenase, gel filtration
20422
-
x * 48373, large subunit of hydroxylase component (MsmA), + x * 20422, small subunit of hydroxylase component (MsmB), + x * 14126, ferredoxin component (MsmC), + x * 40106, reductase component (MsmD), calculated from sequence
209000
-
two-component hydroxylase of methanesulfonic acid monooxygenase, gel filtration
23000
-
3 * 43700 (MsmA) + 3 * 23000 (MsmB), two-component hydroxylase of methanesulfonic acid monooxygenase, SDS-PAGE
32000
-
electron transfer protein (MsmC) of methanesulfonic acid monooxygenase, gel filtration
38000
-
3 * 48000 + 3 * 20000, hydroxylase component of methanesulfonate monooxygenase consist of large (alpha) and small (beta) subunits, MALDI mass spectrometry. 2 * 13752, the ferredoxin component of methanesulfonate monooxygenase consists of 2 subunits, electron spray mass spectrometry. 1 * 38000, The reductase component of methanesulfonate monooxygenase is a single polypeptide of 38000 Da
40106
-
x * 48373, large subunit of hydroxylase component (MsmA), + x * 20422, small subunit of hydroxylase component (MsmB), + x * 14126, ferredoxin component (MsmC), + x * 40106, reductase component (MsmD), calculated from sequence
43700
-
3 * 43700 (MsmA) + 3 * 23000 (MsmB), two-component hydroxylase of methanesulfonic acid monooxygenase, SDS-PAGE
48000
-
3 * 48000 + 3 * 20000, hydroxylase component of methanesulfonate monooxygenase consist of large (alpha) and small (beta) subunits, MALDI mass spectrometry. 2 * 13752, the ferredoxin component of methanesulfonate monooxygenase consists of 2 subunits, electron spray mass spectrometry. 1 * 38000, The reductase component of methanesulfonate monooxygenase is a single polypeptide of 38000 Da
48373
-
x * 48373, large subunit of hydroxylase component (MsmA), + x * 20422, small subunit of hydroxylase component (MsmB), + x * 14126, ferredoxin component (MsmC), + x * 40106, reductase component (MsmD), calculated from sequence
13752
-
2 * 13752, electron transfer protein (MsmC) of methanesulfonic acid monooxygenase, SDS-PAGE
13752
-
3 * 48000 + 3 * 20000, hydroxylase component of methanesulfonate monooxygenase consist of large (alpha) and small (beta) subunits, MALDI mass spectrometry. 2 * 13752, the ferredoxin component of methanesulfonate monooxygenase consists of 2 subunits, electron spray mass spectrometry. 1 * 38000, The reductase component of methanesulfonate monooxygenase is a single polypeptide of 38000 Da
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?
-
x * 48373, large subunit of hydroxylase component (MsmA), + x * 20422, small subunit of hydroxylase component (MsmB), + x * 14126, ferredoxin component (MsmC), + x * 40106, reductase component (MsmD), calculated from sequence
?
-
x * 48373, large subunit of hydroxylase component (MsmA), + x * 20422, small subunit of hydroxylase component (MsmB), + x * 14126, ferredoxin component (MsmC), + x * 40106, reductase component (MsmD), calculated from sequence
-
?
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2 * 13748, electron transfer protein (MsmC) of methanesulfonic acid monooxygenase, calculated from sequence
?
-
2 * 13752, electron transfer protein (MsmC) of methanesulfonic acid monooxygenase, SDS-PAGE
?
-
3 * 48000 + 3 * 20000, hydroxylase component of methanesulfonate monooxygenase consist of large (alpha) and small (beta) subunits, MALDI mass spectrometry. 2 * 13752, the ferredoxin component of methanesulfonate monooxygenase consists of 2 subunits, electron spray mass spectrometry. 1 * 38000, The reductase component of methanesulfonate monooxygenase is a single polypeptide of 38000 Da
?
-
multicomponent enzyme contains a two-component hydroxylase of the mononuclear-iron-center type. The large subunit of the hydroxylase, MsmA (48473 Da calculated from sequence), contains a typical Rieske-type [2Fe2S] center with an unusual iron-binding motif. The small subunit of the hydroxylase, MsmB (20478 Da calculated from sequence). MsmC (13748 Da calculated from sequence) is the ferredoxin component, and MsmD (388520 Da calculated from sequence) is the reductase component
?
-
2 * 13748, electron transfer protein (MsmC) of methanesulfonic acid monooxygenase, calculated from sequence
-
?
-
2 * 13752, electron transfer protein (MsmC) of methanesulfonic acid monooxygenase, SDS-PAGE
-
?
-
multicomponent enzyme contains a two-component hydroxylase of the mononuclear-iron-center type. The large subunit of the hydroxylase, MsmA (48473 Da calculated from sequence), contains a typical Rieske-type [2Fe2S] center with an unusual iron-binding motif. The small subunit of the hydroxylase, MsmB (20478 Da calculated from sequence). MsmC (13748 Da calculated from sequence) is the ferredoxin component, and MsmD (388520 Da calculated from sequence) is the reductase component
-
hexamer
-
3 * 43700 (MsmA) + 3 * 23000 (MsmB), two-component hydroxylase of methanesulfonic acid monooxygenase, SDS-PAGE
hexamer
-
3 * 43700 (MsmA) + 3 * 23000 (MsmB), two-component hydroxylase of methanesulfonic acid monooxygenase, SDS-PAGE
-
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cloning of the reductase encoded by the msmD gene. Cloning and overexpression of the msmD gene, encoding the reductase component, as a GST fusion protein results in the expression of a 65000 Da polypeptide matching the size of the GST protein plus the reductase protein when induced with isopropyl thio-beta-D-galactoside. The fusion between the two proteins is unstable, and purification by affinity chromatography is not possible
-
expression in Escherichia coli. The four polypeptides comprising MSAMO are the products of the coordinated expression of an operon (msmABCD)
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gene encoding the electron transfer protein (MsmC) of methanesulfonic acid monooxygenase
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gene msmA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli strain DH5alpha
msm gene cluster. Development of functional gene probes centered around the unique Rieske center encoding region of msmA which can be used to detect the presence of methanesulfonate-utilizing bacteria in the environment
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gene msmA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli strain DH5alpha
gene msmA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli strain DH5alpha
gene msmA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli strain DH5alpha
gene msmA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli strain DH5alpha
gene msmA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli strain DH5alpha
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Baxter, N.J.; Scanlan, J.; de Marco, P.; Wood, A.P.; Murrell, J.C.
Duplicate copies of genes encoding methanesulfonate monooxygenase in Marinosulfonomonas methylotropha strain TR3 and detection of methanesulfonate utilizers in the environment
Appl. Environ. Microbiol.
68
289-296
2002
Marinosulfonomonas methylotropha, Marinosulfonomonas methylotropha TR3
brenda
Kelly, D.P.; Murrell, J.C.
Microbial metabolism of methanesulfonic acid
Arch. Microbiol.
172
341-348
1999
Methylosulfonomonas methylovora
brenda
Moosvi, S.A.; Pacheco, C.C.; McDonald, I.R.; De Marco, P.; Pearce, D.A.; Kelly, D.P.; Wood, A.P.
Isolation and properties of methanesulfonate-degrading Afipia felis from Antarctica and comparison with other strains of A. felis
Environ. Microbiol.
7
22-23
2005
Afipia felis
brenda
Reichenbecher, W.; Murrell, J.C.
Purification and partial characterization of the hydroxylase component of the methanesulfonic acid mono-oxygenase from Methylosulfonomonas methylovora strain M2
Eur. J. Biochem.
267
4763-4769
2000
Methylosulfonomonas methylovora, Methylosulfonomonas methylovora M2
brenda
Higgins, T.P.; de Marco, P.; Murrell, J.C.
Purification and molecular characterization of the electron transfer protein of methanesulfonic acid monooxygenase
J. Bacteriol.
179
1974-1979
1979
Methylosulfonomonas methylovora, Methylosulfonomonas methylovora M2
brenda
de Marco, P.; Moradas-Ferreira, P.; Higgins, T.P.; McDonald, I.; Kenna, E.M.; Murrell, J.C.
Molecular analysis of a novel methanesulfonic acid monooxygenase from the methylotroph Methylosulfonomonas methylovora
J. Bacteriol.
181
2244-2251
1999
Methylosulfonomonas methylovora, Methylosulfonomonas methylovora M2
brenda
Jamshad, M.; Murrell, J.C.; Fueloep, V.
Purification and crystallization of the hydroxylase component of the methanesulfonate monooxygenase from Methylosulfonomonas methylovora strain M2
Protein Expr. Purif.
52
472-477
2007
Methylosulfonomonas methylovora, Methylosulfonomonas methylovora M2
brenda
Moosvi, S.A.; Pacheco, C.C.; McDonald, I.R.; De Marco, P.; Pearce, D.A.; Kelly, D.P.; Wood, A.P.
Isolation and properties of methanesulfonate-degrading Afipia felis from Antarctica and comparison with other strains of A. felis
Environ. Microbiol.
7
22-33
2005
Afipia felis (A4L9N9), Afipia felis
brenda
Henriques, A.C.; De Marco, P.
Methanesulfonate (MSA) catabolic genes from marine and estuarine bacteria
PLoS ONE
10
e0125735
2015
Candidatus Filomicrobium marinum (A0A0D6JGB8), Candidatus Filomicrobium marinum (A0A0G2RHR1), Methylobacterium sp. P1 (A0A0G2RG68), Hyphomicrobium sp. P2 (A0A0G2RHB5), Methylobacterium sp. RD4.1 (A0A0G2RI26), Methylosulfonomonas methylovora (Q9X404), Candidatus Filomicrobium marinum W (A0A0G2RHR1), Methylosulfonomonas methylovora M2 (Q9X404), Candidatus Filomicrobium marinum Y (A0A0D6JGB8)
brenda