BRENDA - Enzyme Database
show all sequences of 1.14.13.111

Molecular analysis of a novel methanesulfonic acid monooxygenase from the methylotroph Methylosulfonomonas methylovora

de Marco, P.; Moradas-Ferreira, P.; Higgins, T.P.; McDonald, I.; Kenna, E.M.; Murrell, J.C.; J. Bacteriol. 181, 2244-2251 (1999)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli. The four polypeptides comprising MSAMO are the products of the coordinated expression of an operon (msmABCD)
Methylosulfonomonas methylovora
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Iron
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) possesses a typical chloroplast-like [2Fe–2S] center
Methylosulfonomonas methylovora
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methylosulfonomonas methylovora
-
-
-
Methylosulfonomonas methylovora M2
-
-
-
Subunits
Subunits
Commentary
Organism
?
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 component
Methylosulfonomonas methylovora
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Methylosulfonomonas methylovora
MsmC, ferredoxin component, calculated from sequence
-
3.9
Methylosulfonomonas methylovora
MsmB, small subunit of hydroxylase component, calculated from sequence
-
5.6
Methylosulfonomonas methylovora
MsmD, ferredoxin component, calculated from sequence
-
6.5
Methylosulfonomonas methylovora
MsmA, small subunit of hydroxylase component, calculated from sequence
-
6.7
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli. The four polypeptides comprising MSAMO are the products of the coordinated expression of an operon (msmABCD)
Methylosulfonomonas methylovora
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Iron
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) possesses a typical chloroplast-like [2Fe–2S] center
Methylosulfonomonas methylovora
Subunits (protein specific)
Subunits
Commentary
Organism
?
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 component
Methylosulfonomonas methylovora
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Methylosulfonomonas methylovora
MsmC, ferredoxin component, calculated from sequence
-
3.9
Methylosulfonomonas methylovora
MsmB, small subunit of hydroxylase component, calculated from sequence
-
5.6
Methylosulfonomonas methylovora
MsmD, ferredoxin component, calculated from sequence
-
6.5
Methylosulfonomonas methylovora
MsmA, small subunit of hydroxylase component, calculated from sequence
-
6.7
Other publictions for EC 1.14.13.111
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
746182
Henriques
Methanesulfonate (MSA) catabo ...
Candidatus Filomicrobium marinum, Candidatus Filomicrobium marinum W, Candidatus Filomicrobium marinum Y, Hyphomicrobium sp. P2, Methylobacterium sp. P1, Methylobacterium sp. RD4.1, Methylosulfonomonas methylovora, Methylosulfonomonas methylovora M2
PLoS ONE
10
e0125735
2015
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5
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5
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6
8
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694958
Jamshad
Purification and crystallizati ...
Methylosulfonomonas methylovora, Methylosulfonomonas methylovora M2
Protein Expr. Purif.
52
472-477
2007
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1
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1
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7
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692108
Moosvi
Isolation and properties of me ...
Afipia felis
Environ. Microbiol.
7
22-23
2005
1
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1
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5
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738122
Moosvi
Isolation and properties of me ...
Afipia felis
Environ. Microbiol.
7
22-33
2005
1
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1
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1
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690515
Baxter
Duplicate copies of genes enco ...
Marinosulfonomonas methylotropha, Marinosulfonomonas methylotropha TR3
Appl. Environ. Microbiol.
68
289-296
2002
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1
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4
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11
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1
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4
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1
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1
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4
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692154
Reichenbecher
Purification and partial chara ...
Methylosulfonomonas methylovora, Methylosulfonomonas methylovora M2
Eur. J. Biochem.
267
4763-4769
2000
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2
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1
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1
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690638
Kelly
Microbial metabolism of methan ...
Methylosulfonomonas methylovora
Arch. Microbiol.
172
341-348
1999
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1
5
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5
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1
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5
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1
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4
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692819
de Marco
Molecular analysis of a novel ...
Methylosulfonomonas methylovora, Methylosulfonomonas methylovora M2
J. Bacteriol.
181
2244-2251
1999
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1
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1
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12
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692817
Higgins
Purification and molecular cha ...
Methylosulfonomonas methylovora, Methylosulfonomonas methylovora M2
J. Bacteriol.
179
1974-1979
1979
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3
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1
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1
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1
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3
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