Information on EC 1.14.13.111 - methanesulfonate monooxygenase

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The expected taxonomic range for this enzyme is: Alphaproteobacteria

EC NUMBER
COMMENTARY hide
1.14.13.111
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RECOMMENDED NAME
GeneOntology No.
methanesulfonate monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
methanesulfonate + NADH + H+ + O2 = formaldehyde + NAD+ + sulfite + H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
methanesulfonate degradation
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Sulfur metabolism
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SYSTEMATIC NAME
IUBMB 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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strains 25E1 and RD1
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CH3SO3- + O2 + NADH + H+
?
show the reaction diagram
CH3SO3- + O2 + NADH + H+
formaldehyde + HSO3- + NAD+ + H2O
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CH3SO3- + O2 + NADH + H+
formaldehyde + HSO3- + NAD+ + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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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 hide
LITERATURE
Fe2+
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0.1 mM, stimulates
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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0.004 mM, stimulates
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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MsmB, small subunit of hydroxylase component, calculated from sequence
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20000
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ferredoxin component of the methanesulfonate monooxygenase
32000
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electron transfer protein (MsmC) of methanesulfonic acid monooxygenase, gel filtration
200000
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hydroxylase component of methanesulfonate monooxygenase, gel filtration
209000
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two-component hydroxylase of methanesulfonic acid monooxygenase, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
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
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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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