Information on EC 1.14.13.111 - methanesulfonate monooxygenase:
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EC NUMBERCOMMENTARY
1.14.13.111-

RECOMMENDED NAMEGeneOntology No.
methanesulfonate monooxygenaseGO:0018648

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
methanesulfonate + NADH + H+ + O2 = formaldehyde + NAD+ + sulfite + H2O
show the reaction diagram		----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

PATHWAYKEGG LinkMetaCyc Link
dimethyl sulfide degradation II (oxidation)-PWY-6059
methanesulfonate degradation-PWY-6044

SYSTEMATIC NAMEIUBMB Comments
methanesulfonate,NADH:oxygen oxidoreductase (bisulfite-forming)A 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 [1]. 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.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
methanesulfonic acid monooxygenaseMethylosulfonomonas methylovora--692154
MSA monooxygenaseMethylosulfonomonas methylovora--692819, 694958
MSAMOAfipia felis--692108
MSAMOMethylosulfonomonas methylovora--692154, 692817, 692819, 694958
MsmMarinosulfonomonas methylotropha--690515

CAS REGISTRY NUMBERCOMMENTARY
No entries in this field

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Afipia felisstrains 25E1 and RD1692108--Manually annotated by BRENDA team
Marinosulfonomonas methylotrophastrain TR3690515--Manually annotated by BRENDA team
Marinosulfonomonas methylotropha TR3strain TR3690515--Manually annotated by BRENDA team
Methylosulfonomonas methylovora-690638--Manually annotated by BRENDA team
Methylosulfonomonas methylovorastrain M2692154, 692817, 692819, 694958--Manually annotated by BRENDA team
Methylosulfonomonas methylovora M2strain M2692154--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
CH3SO3- + O2 + NADH + H+formaldehyde + HSO3- + NAD+ + H2O
show the reaction diagram		Methylosulfonomonas methylovora--692154, 694958--?
CH3SO3- + O2 + NADH + H+formaldehyde + HSO3- + NAD+ + H2O
show the reaction diagram		Methylosulfonomonas methylovora-MSAMO is specifically induced during growth on methanesulfonate692154--?
CH3SO3- + O2 + NADH + H+?
show the reaction diagram		Methylosulfonomonas methylovora--692817--?
CH3SO3- + O2 + NADH + H+?
show the reaction diagram		Afipia felis-no significant methanesulfonate monooxygenase activity can be detected when NADPH replaces NADH692108--?

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
CH3SO3- + O2 + NADH + H+formaldehyde + HSO3- + NAD+ + H2O
show the reaction diagram		Methylosulfonomonas methylovora-MSAMO is specifically induced during growth on methanesulfonate692154--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
NADHAfipia felis--692108 2D-image
NADHMethylosulfonomonas methylovora--692154, 692817, 694958 2D-image
FADMarinosulfonomonas methylotropha-within the sequence of MsmD an oxidoreductase FAD/NAD binding domain located toward the C-terminal end of the polypeptide is found690515 2D-image
additional informationMethylosulfonomonas methylovora-flavin is absent in the two-component hydroxylase of methanesulfonic acid monooxygenase692154-

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Fe2+Afipia felis-0.1 mM, stimulates692108
IronMethylosulfonomonas methylovora-the ferredoxin component of the methanesulfonate monooxygenase and the hydroxylase component of methanesulfonate monooxygenase contain a Rieske [2Fe-2S] centre690638
IronMethylosulfonomonas methylovora-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-monomer692154
IronMethylosulfonomonas methylovora-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] centers692817
IronMethylosulfonomonas methylovora-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 [2Fe–2S] center with an unusual iron-binding motif. The reductase component (MsmD) has got a typical chloroplast-like [2Fe–2S] center692819
IronMethylosulfonomonas methylovora-presence on an intact Rieske-iron sulfur centre in the hydroxylase component of methanesulfonate monooxygenase694958
additional informationMethylosulfonomonas methylovora-chromium, cobalt, copper, lead, nickel, molybdenum, tungsten and vanadium are not detected in two-component hydroxylase of methanesulfonic acid monooxygenase692154

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
FADAfipia felis-0.004 mM, stimulates692108 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.88-Methylosulfonomonas methylovora--692154

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
No entries in this field

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
3.9-Methylosulfonomonas methylovora-ferredoxin component of the methanesulfonate monooxygenase690638
3.9-Methylosulfonomonas methylovora-isoelectric focusing, electron transfer protein (MsmC) of methanesulfonic acid monooxygenase692817
3.9-Methylosulfonomonas methylovora-MsmC, ferredoxin component, calculated from sequence692819
4-Marinosulfonomonas methylotropha-MsmC, ferredoxin component, calculated from sequence690515
4-Methylosulfonomonas methylovora-pI calculated from sequence is 3.97, electron transfer protein (MsmC) of methanesulfonic acid monooxygenase692817
4.9-Methylosulfonomonas methylovora-two-component hydroxylase of methanesulfonic acid monooxygenase, chromatofocusing692154
5.1-Marinosulfonomonas methylotropha-MsmD, reductase component, calculated from sequence690515
5.6-Methylosulfonomonas methylovora-beta-subunit of hydroxylase component of methanesulfonate monooxygenase690638
5.6-Methylosulfonomonas methylovora-MsmB, small subunit of hydroxylase component, calculated from sequence692819
5.8-Marinosulfonomonas methylotropha-MsmA, large subunit of hydroxylase component, calculated from sequence690515
6-Marinosulfonomonas methylotropha-MsmB, small subunit of hydroxylase component, calculated from sequence690515
6.5-Methylosulfonomonas methylovora-reductase component of methanesulfonate monooxygenase690638
6.5-Methylosulfonomonas methylovora-MsmD, ferredoxin component, calculated from sequence692819
6.7-Methylosulfonomonas methylovora-alpha-subunit of hydroxylase component of methanesulfonate monooxygenase690638
6.7-Methylosulfonomonas methylovora-MsmA, small subunit of hydroxylase component, calculated from sequence692819

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
No entries in this field

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
cytoplasmMethylosulfonomonas methylovora--5737692154Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
No entries in this field

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
20000-Methylosulfonomonas methylovora-ferredoxin component of the methanesulfonate monooxygenase690638
32000-Methylosulfonomonas methylovora-electron transfer protein (MsmC) of methanesulfonic acid monooxygenase, gel filtration692817
200000-Methylosulfonomonas methylovora-hydroxylase component of methanesulfonate monooxygenase, gel filtration690638
209000-Methylosulfonomonas methylovora-two-component hydroxylase of methanesulfonic acid monooxygenase, gel filtration692154

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Marinosulfonomonas methylotropha-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 sequence690515
?Methylosulfonomonas methylovora-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 Da690638
?Methylosulfonomonas methylovora-2 * 13748, electron transfer protein (MsmC) of methanesulfonic acid monooxygenase, calculated from sequence; 2 * 13752, electron transfer protein (MsmC) of methanesulfonic acid monooxygenase, SDS-PAGE692817
?Methylosulfonomonas methylovora-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 [2Fe–2S] 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 component692819
hexamerMethylosulfonomonas methylovora-3 * 43700 (MsmA) + 3 * 23000 (MsmB), two-component hydroxylase of methanesulfonic acid monooxygenase, SDS-PAGE692154

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
hanging drop vapour diffusion method, two-component hydroxylase (large subunit (MsmA) and small subunit (MsmB))Methylosulfonomonas methylovora-694958

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
No entries in this field

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
electron transfer protein (MsmC) of methanesulfonic acid monooxygenaseMethylosulfonomonas methylovora-692817
hydroxylase component of methanesulfonate monooxygenase, ferredoxin component of the methanesulfonate monooxygenase and reductase component of the methanesulfonate monooxygenaseMethylosulfonomonas methylovora-690638
purification of two-component hydroxylase of methanesulfonic acid monooxygenase. Purification of the reductase component (MsmD) using a range of chromatographic techniques failsMethylosulfonomonas methylovora-692154
two-component hydroxylase (large subunit (MsmA) and small subunit (MsmB))Methylosulfonomonas methylovora-694958

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
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 environmentMarinosulfonomonas methylotropha-690515
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 possibleMethylosulfonomonas methylovora-692154
expression in Escherichia coli. The four polypeptides comprising MSAMO are the products of the coordinated expression of an operon (msmABCD)Methylosulfonomonas methylovora-692819
gene encoding the electron transfer protein (MsmC) of methanesulfonic acid monooxygenaseMethylosulfonomonas methylovora-692817

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
690515Baxter, 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 environmentAppl. Environ. Microbiol.68289-2962002Marinosulfonomonas methylotropha PubMed
690638Kelly, D.P.; Murrell, J.C.Microbial metabolism of methanesulfonic acidArch. Microbiol.172341-3481999Methylosulfonomonas methylovora PubMed
692108Moosvi, 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. felisEnviron. Microbiol.722-232005Afipia felis PubMed
692154Reichenbecher, W.; Murrell, J.C.Purification and partial characterization of the hydroxylase component of the methanesulfonic acid mono-oxygenase from Methylosulfonomonas methylovora strain M2Eur. J. Biochem.2674763-47692000Methylosulfonomonas methylovora PubMed
692817Higgins, T.P.; de Marco, P.; Murrell, J.C.Purification and molecular characterization of the electron transfer protein of methanesulfonic acid monooxygenaseJ. Bacteriol.1791974-19791979Methylosulfonomonas methylovora PubMed
692819de 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 methylovoraJ. Bacteriol.1812244-22511999Methylosulfonomonas methylovora PubMed
694958Jamshad, M.; Murrell, J.C.; Fueloep, V.Purification and crystallization of the hydroxylase component of the methanesulfonate monooxygenase from Methylosulfonomonas methylovora strain M2Protein Expr. Purif.52472-4772007Methylosulfonomonas methylovora PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.111)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)