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show all sequences of 1.8.2.1

Catalytic voltammetry of the molybdoenzyme sulfite dehydrogenase from Sinorhizobium meliloti

Kalimuthu, P.; Kappler, U.; Bernhardt, P.V.; J. Phys. Chem. B 118, 7091-7099 (2014)

Data extracted from this reference:

Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
periplasm
-
Sinorhizobium meliloti
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mo4+
molybdenum enzyme. Sulfite oxidizing enzymes (regardless of origin) share a common active site comprising a dioxido-MoVI moiety chelated by a molybdopterin dithiolene ligand in addition to a cysteinyl S-donor. The equatorial oxido ligand is the one transferred to sulfite during its 2-electron O-atom transfer reaction
Sinorhizobium meliloti
additional information
the enzyme bears no heme cofactor
Sinorhizobium meliloti
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
78000
-
-
Sinorhizobium meliloti
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
sulfite + 2 ferricytochrome c + H2O
Sinorhizobium meliloti
-
sulfate + 2 ferrocytochrome c + 2 H+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sinorhizobium meliloti
-
-
-
Reaction
Reaction
Commentary
Organism
sulfite + 2 ferricytochrome c + H2O = sulfate + 2 ferrocytochrome c + 2 H+
mechanism of electrochemically mediated, enzyme SorT-catalyzed sulfite oxidation
Sinorhizobium meliloti
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
7.4
-
pH 8.0, 22C, with horse heart cytochrome c
Sinorhizobium meliloti
33.4
-
pH 8.0, 22C, with SorU
Sinorhizobium meliloti
470
-
pH 8.0, 22C, with ferricyanide
Sinorhizobium meliloti
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
favorable protein-protein interactions between SorT and c-type cytochrome SorU, i.e. Smc04048, lead to productive electron transfer and catalytic activity. No activity with ferrous horse heart cytochrome c, and no activity with O2 as an sulfite oxidase
743146
Sinorhizobium meliloti
?
-
-
-
-
sulfite + 2 ferricytochrome c + H2O
-
743146
Sinorhizobium meliloti
sulfate + 2 ferrocytochrome c + 2 H+
-
-
-
?
sulfite + 2 ferrocene methanol + H2O
-
743146
Sinorhizobium meliloti
sulfate + 2 reduced ferrocene methanol + 2 H+
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
-
Sinorhizobium meliloti
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
22
-
assay at room temperature
Sinorhizobium meliloti
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
22
-
20 min, inactivation
Sinorhizobium meliloti
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
the lack of a plateau prevents the determination of a genuine pH optimum, an apparently linear decrease in activity as a function of pH is not interpretable by standard models of pH-dependent enzyme activity which predict sigmoidal or bell-shaped profiles
Sinorhizobium meliloti
8
-
assay at
Sinorhizobium meliloti
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6
11
the greatest loss in activity occurs while the enzyme is at pH 10, while in the range above pH 6 and below pH 9 there is no significant variation, inactivation at pH 11.0
Sinorhizobium meliloti
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
11
-
irreversible time-dependent loss of catalytic activity
Sinorhizobium meliloti
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome c
c-type cytochrome SorU, i.e. Smc04048
Sinorhizobium meliloti
additional information
ferrocene methanol (in its oxidized ferrocenium form) is utilized as an artificial electron acceptor for the catalytic SorT sulfite oxidation reaction
Sinorhizobium meliloti
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome c
c-type cytochrome SorU, i.e. Smc04048
Sinorhizobium meliloti
additional information
ferrocene methanol (in its oxidized ferrocenium form) is utilized as an artificial electron acceptor for the catalytic SorT sulfite oxidation reaction
Sinorhizobium meliloti
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
periplasm
-
Sinorhizobium meliloti
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mo4+
molybdenum enzyme. Sulfite oxidizing enzymes (regardless of origin) share a common active site comprising a dioxido-MoVI moiety chelated by a molybdopterin dithiolene ligand in addition to a cysteinyl S-donor. The equatorial oxido ligand is the one transferred to sulfite during its 2-electron O-atom transfer reaction
Sinorhizobium meliloti
additional information
the enzyme bears no heme cofactor
Sinorhizobium meliloti
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
78000
-
-
Sinorhizobium meliloti
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
sulfite + 2 ferricytochrome c + H2O
Sinorhizobium meliloti
-
sulfate + 2 ferrocytochrome c + 2 H+
-
-
?
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
7.4
-
pH 8.0, 22C, with horse heart cytochrome c
Sinorhizobium meliloti
33.4
-
pH 8.0, 22C, with SorU
Sinorhizobium meliloti
470
-
pH 8.0, 22C, with ferricyanide
Sinorhizobium meliloti
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
favorable protein-protein interactions between SorT and c-type cytochrome SorU, i.e. Smc04048, lead to productive electron transfer and catalytic activity. No activity with ferrous horse heart cytochrome c, and no activity with O2 as an sulfite oxidase
743146
Sinorhizobium meliloti
?
-
-
-
-
sulfite + 2 ferricytochrome c + H2O
-
743146
Sinorhizobium meliloti
sulfate + 2 ferrocytochrome c + 2 H+
-
-
-
?
sulfite + 2 ferrocene methanol + H2O
-
743146
Sinorhizobium meliloti
sulfate + 2 reduced ferrocene methanol + 2 H+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
-
Sinorhizobium meliloti
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
22
-
assay at room temperature
Sinorhizobium meliloti
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
22
-
20 min, inactivation
Sinorhizobium meliloti
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
the lack of a plateau prevents the determination of a genuine pH optimum, an apparently linear decrease in activity as a function of pH is not interpretable by standard models of pH-dependent enzyme activity which predict sigmoidal or bell-shaped profiles
Sinorhizobium meliloti
8
-
assay at
Sinorhizobium meliloti
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6
11
the greatest loss in activity occurs while the enzyme is at pH 10, while in the range above pH 6 and below pH 9 there is no significant variation, inactivation at pH 11.0
Sinorhizobium meliloti
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
11
-
irreversible time-dependent loss of catalytic activity
Sinorhizobium meliloti
Other publictions for EC 1.8.2.1
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)
743146
Kalimuthu
Catalytic voltammetry of the ...
Sinorhizobium meliloti
J. Phys. Chem. B
118
7091-7099
2014
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1
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7
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1
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1
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1
1
2
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2
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1
2
1
1
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3
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3
1
1
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1
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2
1
1
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724418
Rapson
Short circuiting a sulfite oxi ...
Starkeya novella
Biochim. Biophys. Acta
1807
108-118
2011
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1
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4
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3
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710857
Kalimuthu
Highly sensitive and stable el ...
Starkeya novella
Anal. Chem.
82
7374-7379
2010
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1
1
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1
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1
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711223
Johnson-Winters
Effects of interdomain tether ...
Homo sapiens
Biochemistry
49
1290-1296
2010
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3
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7
1
1
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1
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1
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7
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7
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6
6
711242
Qiu
The structures of the C185S an ...
Gallus gallus
Biochemistry
49
3989-4000
2010
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1
1
2
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1
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2
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711780
Spricigo
-
Sulfite biosensor based on osm ...
Homo sapiens
Colloids Surf. A Physicochem. Eng. Asp.
354
314-319
2010
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1
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724587
Ogawa
Biochemical studies of a soxF- ...
Chlorobaculum tepidum
Biosci. Biotechnol. Biochem.
74
771-780
2010
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1
1
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700633
Astashkin
Exchangeable oxygens in the vi ...
Starkeya novella
Phys. Chem. Chem. Phys.
11
6733-6742
2009
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712157
Hernandez-Marin
Theoretical study of the oxida ...
Gallus gallus
Inorg. Chem.
48
1323-1333
2009
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722663
Bailey
Molecular basis for enzymatic ...
Starkeya novella
J. Biol. Chem.
284
2053-2063
2009
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3
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32
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30
1
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32
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30
1
1
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32
32
691057
Rapson
Direct catalytic electrochemis ...
Starkeya novella
Biochim. Biophys. Acta
1777
1319-1325
2008
1
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6
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694023
Workun
Evolutionary persistence of th ...
Starkeya novella
Microbiol. Mol. Biol. Rev.
72
228-48
2008
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694036
Denger
Bacterial sulfite dehydrogenas ...
Cupriavidus necator H16, Delftia acidovorans SPH-1
Microbiology
154
256-263
2008
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667714
Wilson
The G473D mutation impairs dim ...
Homo sapiens
Biochemistry
45
2149-2160
2006
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667744
Kappler
Kinetic and structural evidenc ...
Starkeya novella
Biochemistry
45
9696-9705
2006
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6
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2
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668939
Doonan
Structure of the active site o ...
Starkeya novella
Inorg. Chem.
45
7488-7492
2006
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695918
Gorzynska
Inducible transcription of gen ...
Ruegeria pomeroyi
Arch. Microbiol.
185
402-406
2006
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667688
Sibille
Solution structure of the sulf ...
Escherichia coli
Biochemistry
44
9086-9095
2005
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Sulfite:cytochrome c oxidoredu ...
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Rhodotorula sp.
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Purification and some properti ...
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Partial purification and resol ...
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Purification of Thiobacillus n ...
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The sulfite oxidase of Thiobac ...
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Enzymes involved in the metabo ...
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394077
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Purification and properties of ...
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Mechanism of thiosulfate oxida ...
Starkeya novella, Thiobacillus denitrificans
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