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Enzyme Nomenclature
Information on EC 1.14.13.111 - methanesulfonate monooxygenase (NADH)
Word Map on EC 1.14.13.111
- 1.14.13.111
- methylovora
- methanol
- sulfur
- methylobacterium
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ferredoxins
- flavin
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metagenome
-
multicomponent
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ecological
- hyphomicrobium
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rieske-type
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atmosphere
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nadh-specific
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methylotrophy
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portuguese
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antarctica
-
portugal
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ocean
- afipia
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signy
-
rieske
- dimethylsulfide
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biogeochemical
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estuary
- felis
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The expected taxonomic range for this enzyme is: Alphaproteobacteria
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EC NUMBER 
COMMENTARY 
1.14.13.111
-
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RECOMMENDED NAME
GeneOntology No.
methanesulfonate monooxygenase (NADH)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
methanesulfonate + NADH + H+ + O2 = formaldehyde + NAD+ + sulfite + H2O
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
methanesulfonate,NADH:oxygen oxidoreductase
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. cf. EC 1.14.14.34, methanesulfonate monooxygenase (FMNH2).
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
all strains isolated grow with methanesulfonate as sole carbon substrate
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
methanesulfonate + NADH + H+ + O2
formaldehyde + NAD+ + sulfite + H2O
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-
-
?
CH3SO3- + O2 + NADH + H+
?
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no significant methanesulfonate monooxygenase activity can be detected when NADPH replaces NADH
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-
?
CH3SO3- + O2 + NADH + H+
formaldehyde + HSO3- + NAD+ + H2O
-
-
-
-
?
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
-
-
?
CH3SO3- + O2 + NADH + H+
formaldehyde + HSO3- + NAD+ + H2O
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-
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CH3SO3- + O2 + NADH + H+
formaldehyde + HSO3- + NAD+ + H2O
-
MSAMO is specifically induced during growth on methanesulfonate
-
-
?
CH3SO3- + O2 + NADH + H+
formaldehyde + HSO3- + NAD+ + H2O
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MSAMO is specifically induced during growth on methanesulfonate
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
within the sequence of MsmD an oxidoreductase FAD/NAD binding domain located toward the C-terminal end of the polypeptide is found
additional information
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flavin is absent in the two-component hydroxylase of methanesulfonic acid monooxygenase
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
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
Iron
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the ferredoxin component of the methanesulfonate monooxygenase and the hydroxylase component of methanesulfonate monooxygenase contain a Rieske [2Fe-2S] centre
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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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
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presence on an intact Rieske-iron sulfur centre in the hydroxylase component of methanesulfonate monooxygenase
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ACTIVATING COMPOUND
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
3.9
4.9
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two-component hydroxylase of methanesulfonic acid monooxygenase, chromatofocusing
5.6
5.8
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MsmA, large subunit of hydroxylase component, calculated from sequence
6
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MsmB, small subunit of hydroxylase component, calculated from sequence
6.5
6.7
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
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
6.7
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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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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
13748
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2 * 13748, electron transfer protein (MsmC) of methanesulfonic acid monooxygenase, calculated from sequence
13752
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
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ferredoxin component of the methanesulfonate monooxygenase
20422
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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
23000
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3 * 43700 (MsmA) + 3 * 23000 (MsmB), two-component hydroxylase of methanesulfonic acid monooxygenase, SDS-PAGE
32000
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electron transfer protein (MsmC) of methanesulfonic acid monooxygenase, gel filtration
38000
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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
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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
43700
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3 * 43700 (MsmA) + 3 * 23000 (MsmB), two-component hydroxylase of methanesulfonic acid monooxygenase, SDS-PAGE
48000
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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
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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
200000
-
hydroxylase component of methanesulfonate monooxygenase, gel filtration
209000
-
two-component hydroxylase of methanesulfonic acid monooxygenase, gel filtration
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
13752
-
2 * 13752, electron transfer protein (MsmC) of methanesulfonic acid monooxygenase, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
?
-
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
-
?
-
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
?
-
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
?
-
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
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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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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, two-component hydroxylase (large subunit (MsmA) and small subunit (MsmB))
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
electron transfer protein (MsmC) of methanesulfonic acid monooxygenase
-
hydroxylase component of methanesulfonate monooxygenase, ferredoxin component of the methanesulfonate monooxygenase and reductase component of the methanesulfonate monooxygenase
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purification of two-component hydroxylase of methanesulfonic acid monooxygenase. Purification of the reductase component (MsmD) using a range of chromatographic techniques fails
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two-component hydroxylase (large subunit (MsmA) and small subunit (MsmB))
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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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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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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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.111)
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