BRENDA - Enzyme Database

ArsH from the cyanobacterium Synechocystis sp. PCC 6803 is an efficient NADPH-dependent quinone reductase

Hervas, M.; Lopez-Maury, L.; Leon, P.; Sanchez-Riego, A.M.; Florencio, F.J.; Navarro, J.A.; Biochemistry 51, 1178-1187 (2012)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
1.6.5.5
gene arsH
Synechocystis sp.
1.6.5.10
gene arsh, expression as N-terminallyy His-tagged enzyme in Escherichia coli strain BL21(DE3)
Synechocystis sp.
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.6.5.5
menadione
-
Synechocystis sp.
1.6.5.5
NADP+
can act as a competitive inhibitor for NADPH binding at the active site of an enzyme
Synechocystis sp.
1.6.5.10
dicoumarol
-
Synechocystis sp.
1.6.5.10
NADP+
NADP+ acts as a competitive inhibitor for NADPH binding at the active site of an enzyme
Synechocystis sp.
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.6.5.5
additional information
-
additional information
stopped-flow and laser-flash photolysis kinetic analyses, steady-state kinetics
Synechocystis sp.
1.6.5.5
0.0012
-
dibromothymoquinone
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
0.0013
-
2,5-dimethyl-4-benzoquinone
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
0.0028
-
duroquinone
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
0.0057
-
menadione
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
0.0119
-
coenzyme Q10
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
0.0237
-
2-Hydroxy-1,4-naphthoquinone
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
0.0315
-
NADPH
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
0.0345
-
anthraquinone-2-sulfonate
pH 7.5, 10°C
Synechocystis sp.
1.6.5.10
additional information
-
additional information
stopped-flow and steady-state kinetics, overview
Synechocystis sp.
1.6.5.10
0.0012
-
dibromothymoquinone
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
0.0013
-
2,5-dimethyl-4-benzoquinone
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
0.0028
-
duroquinone
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
0.0057
-
menadione
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
0.0119
-
coenzyme Q10
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
0.0237
-
2-Hydroxy-1,4-naphthoquinone
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
0.0315
-
NADPH
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
0.0345
-
anthraquinone-2-sulfonate
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.6.5.5
25900
-
4 * 25900, SDS-PAGE
Synechocystis sp.
1.6.5.5
108000
-
gel filtration
Synechocystis sp.
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.6.5.5
NADPH + H+ + 2 quinone
Synechocystis sp.
-
NADP+ + 2 semiquinone
-
-
?
1.6.5.10
NADPH + H+ + a quinone
Synechocystis sp.
the catalytic cycle of ArsH consists of the acceptance of two electrons from NADPH to reduce the flavin cofactor (reductive half-reaction) and the transfer of these electrons to an acceptor (oxidative half-reaction)
NADP+ + a quinol
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.6.5.5
Synechocystis sp.
-
gene arsh, encoded in the arsenic resistance operon
-
1.6.5.10
Synechocystis sp.
-
gene arsH
-
Reaction
EC Number
Reaction
Commentary
Organism
1.6.5.5
NADPH + H+ + 2 quinone = NADP+ + 2 semiquinone
ping pong reaction mechanism
Synechocystis sp.
1.6.5.10
NADPH + H+ + a quinone = NADP+ + a quinol
ping pong reaction mechanism
Synechocystis sp.
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.6.5.5
additional information
although the enzyme is able to stabilize the anionic semiquinone form of the FMN, reduction of quinones involves the hydroquinone form of the flavin cofactor, and the enzymatic reaction occurs through a ping pong-type mechanism. ArsH is able to catalyze one-electron reactions (oxygen and cytocrome c reduction), involving the FMN semiquinone form, but with lower efficiency
724333
Synechocystis sp.
?
-
-
-
-
1.6.5.5
NADPH + H+ + 2 2,5-dimethyl-4-benzoquinone
-
724333
Synechocystis sp.
NADP+ + 2 2,5-dimethyl-4-benzosemiquinone
-
-
-
?
1.6.5.5
NADPH + H+ + 2 2-hydroxy-1,4-naphthoquinone
-
724333
Synechocystis sp.
NADP+ + 2 2-hydroxy-1,4-naphthosemiquinone
-
-
-
?
1.6.5.5
NADPH + H+ + 2 anthraquinone-2-sulfonate
-
724333
Synechocystis sp.
NADP+ + ?
-
-
-
?
1.6.5.5
NADPH + H+ + 2 coenzyme Q10
-
724333
Synechocystis sp.
NADP+ + ?
-
-
-
?
1.6.5.5
NADPH + H+ + 2 dibromothymoquinone
-
724333
Synechocystis sp.
NADP+ + 2 dibromothymosemiquinone
-
-
-
?
1.6.5.5
NADPH + H+ + 2 duroquinone
-
724333
Synechocystis sp.
NADP+ + 2 durosemiquinone
-
-
-
?
1.6.5.5
NADPH + H+ + 2 menadione
-
724333
Synechocystis sp.
NADP+ + ?
-
-
-
?
1.6.5.5
NADPH + H+ + 2 quinone
-
724333
Synechocystis sp.
NADP+ + 2 semiquinone
-
-
-
?
1.6.5.5
NADPH + H+ + 2 quinone
the catalytic cycle of ArsH consists of the acceptance of two electrons from NADPH to reduce the flavin cofactor (reductive half-reaction) and the transfer of these electrons to an acceptor (oxidative half-reaction)
724333
Synechocystis sp.
NADP+ + 2 semiquinone
-
-
-
?
1.6.5.10
additional information
NADH, deazariboflavin, and methylviologen can also act as electron donors
724333
Synechocystis sp.
?
-
-
-
-
1.6.5.10
NADPH + H+ + 2,5-dimethyl-4-benzoquinone
-
724333
Synechocystis sp.
NADP+ + 2,5-dimethyl-4-benzoquinonl
-
-
-
?
1.6.5.10
NADPH + H+ + 2-hydroxy-1,4-naphthoquinone
-
724333
Synechocystis sp.
NADP+ + 2-hydroxy-1,4-naphthoquinol
-
-
-
?
1.6.5.10
NADPH + H+ + a quinone
the catalytic cycle of ArsH consists of the acceptance of two electrons from NADPH to reduce the flavin cofactor (reductive half-reaction) and the transfer of these electrons to an acceptor (oxidative half-reaction)
724333
Synechocystis sp.
NADP+ + a quinol
-
-
-
?
1.6.5.10
NADPH + H+ + anthraquinone-2-sulfonate
-
724333
Synechocystis sp.
NADP+ + ?
-
-
-
?
1.6.5.10
NADPH + H+ + coenzyme Q10
-
724333
Synechocystis sp.
NADP+ + reduced coenzyme Q10
-
-
-
?
1.6.5.10
NADPH + H+ + dibromothymoquinone
-
724333
Synechocystis sp.
NADP+ + dibromothymoquinol
-
-
-
?
1.6.5.10
NADPH + H+ + dichlorophenolindophenol
-
724333
Synechocystis sp.
NADP+ + reduced dichlorophenolindophenol
-
-
-
?
1.6.5.10
NADPH + H+ + duroquinone
-
724333
Synechocystis sp.
NADP+ + duroquinol
-
-
-
?
1.6.5.10
NADPH + H+ + menadione
-
724333
Synechocystis sp.
NADP+ + menadiol
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
1.6.5.5
tetramer
4 * 25900, SDS-PAGE
Synechocystis sp.
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.6.5.5
10
25
assay at
Synechocystis sp.
1.6.5.10
25
-
assay at
Synechocystis sp.
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.6.5.5
5
-
coenzyme Q10
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
9.4
-
anthraquinone-2-sulfonate
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
11
-
2-Hydroxy-1,4-naphthoquinone
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
25
-
duroquinone
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
26
-
menadione
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
35
-
dibromothymoquinone
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
36.7
-
2,5-dimethyl-4-benzoquinone
pH 7.5, 10°C
Synechocystis sp.
1.6.5.10
5
-
coenzyme Q10
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
9.4
-
anthraquinone-2-sulfonate
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
11
-
2-Hydroxy-1,4-naphthoquinone
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
25
-
duroquinone
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
26
-
menadione
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
35
-
dibromothymoquinone
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
36.7
-
2,5-dimethyl-4-benzoquinone
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.6.5.5
7.5
8
assay at
Synechocystis sp.
1.6.5.10
8
-
assay at
Synechocystis sp.
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.6.5.5
FMN
in silico structural model of ArsH reconstituted with FMN, overview
Synechocystis sp.
1.6.5.10
FMN
-
Synechocystis sp.
IC50 Value
EC Number
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
1.6.5.10
0.008
0.01
with dichlorophenolindophenol, pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
dicoumarol
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.6.5.5
gene arsH
Synechocystis sp.
1.6.5.10
gene arsh, expression as N-terminallyy His-tagged enzyme in Escherichia coli strain BL21(DE3)
Synechocystis sp.
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.6.5.5
FMN
in silico structural model of ArsH reconstituted with FMN, overview
Synechocystis sp.
1.6.5.10
FMN
-
Synechocystis sp.
IC50 Value (protein specific)
EC Number
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
1.6.5.10
0.008
0.01
with dichlorophenolindophenol, pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
dicoumarol
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.6.5.5
menadione
-
Synechocystis sp.
1.6.5.5
NADP+
can act as a competitive inhibitor for NADPH binding at the active site of an enzyme
Synechocystis sp.
1.6.5.10
dicoumarol
-
Synechocystis sp.
1.6.5.10
NADP+
NADP+ acts as a competitive inhibitor for NADPH binding at the active site of an enzyme
Synechocystis sp.
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.6.5.5
additional information
-
additional information
stopped-flow and laser-flash photolysis kinetic analyses, steady-state kinetics
Synechocystis sp.
1.6.5.5
0.0012
-
dibromothymoquinone
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
0.0013
-
2,5-dimethyl-4-benzoquinone
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
0.0028
-
duroquinone
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
0.0057
-
menadione
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
0.0119
-
coenzyme Q10
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
0.0237
-
2-Hydroxy-1,4-naphthoquinone
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
0.0315
-
NADPH
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
0.0345
-
anthraquinone-2-sulfonate
pH 7.5, 10°C
Synechocystis sp.
1.6.5.10
additional information
-
additional information
stopped-flow and steady-state kinetics, overview
Synechocystis sp.
1.6.5.10
0.0012
-
dibromothymoquinone
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
0.0013
-
2,5-dimethyl-4-benzoquinone
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
0.0028
-
duroquinone
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
0.0057
-
menadione
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
0.0119
-
coenzyme Q10
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
0.0237
-
2-Hydroxy-1,4-naphthoquinone
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
0.0315
-
NADPH
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
0.0345
-
anthraquinone-2-sulfonate
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.6.5.5
25900
-
4 * 25900, SDS-PAGE
Synechocystis sp.
1.6.5.5
108000
-
gel filtration
Synechocystis sp.
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.6.5.5
NADPH + H+ + 2 quinone
Synechocystis sp.
-
NADP+ + 2 semiquinone
-
-
?
1.6.5.10
NADPH + H+ + a quinone
Synechocystis sp.
the catalytic cycle of ArsH consists of the acceptance of two electrons from NADPH to reduce the flavin cofactor (reductive half-reaction) and the transfer of these electrons to an acceptor (oxidative half-reaction)
NADP+ + a quinol
-
-
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.6.5.5
additional information
although the enzyme is able to stabilize the anionic semiquinone form of the FMN, reduction of quinones involves the hydroquinone form of the flavin cofactor, and the enzymatic reaction occurs through a ping pong-type mechanism. ArsH is able to catalyze one-electron reactions (oxygen and cytocrome c reduction), involving the FMN semiquinone form, but with lower efficiency
724333
Synechocystis sp.
?
-
-
-
-
1.6.5.5
NADPH + H+ + 2 2,5-dimethyl-4-benzoquinone
-
724333
Synechocystis sp.
NADP+ + 2 2,5-dimethyl-4-benzosemiquinone
-
-
-
?
1.6.5.5
NADPH + H+ + 2 2-hydroxy-1,4-naphthoquinone
-
724333
Synechocystis sp.
NADP+ + 2 2-hydroxy-1,4-naphthosemiquinone
-
-
-
?
1.6.5.5
NADPH + H+ + 2 anthraquinone-2-sulfonate
-
724333
Synechocystis sp.
NADP+ + ?
-
-
-
?
1.6.5.5
NADPH + H+ + 2 coenzyme Q10
-
724333
Synechocystis sp.
NADP+ + ?
-
-
-
?
1.6.5.5
NADPH + H+ + 2 dibromothymoquinone
-
724333
Synechocystis sp.
NADP+ + 2 dibromothymosemiquinone
-
-
-
?
1.6.5.5
NADPH + H+ + 2 duroquinone
-
724333
Synechocystis sp.
NADP+ + 2 durosemiquinone
-
-
-
?
1.6.5.5
NADPH + H+ + 2 menadione
-
724333
Synechocystis sp.
NADP+ + ?
-
-
-
?
1.6.5.5
NADPH + H+ + 2 quinone
-
724333
Synechocystis sp.
NADP+ + 2 semiquinone
-
-
-
?
1.6.5.5
NADPH + H+ + 2 quinone
the catalytic cycle of ArsH consists of the acceptance of two electrons from NADPH to reduce the flavin cofactor (reductive half-reaction) and the transfer of these electrons to an acceptor (oxidative half-reaction)
724333
Synechocystis sp.
NADP+ + 2 semiquinone
-
-
-
?
1.6.5.10
additional information
NADH, deazariboflavin, and methylviologen can also act as electron donors
724333
Synechocystis sp.
?
-
-
-
-
1.6.5.10
NADPH + H+ + 2,5-dimethyl-4-benzoquinone
-
724333
Synechocystis sp.
NADP+ + 2,5-dimethyl-4-benzoquinonl
-
-
-
?
1.6.5.10
NADPH + H+ + 2-hydroxy-1,4-naphthoquinone
-
724333
Synechocystis sp.
NADP+ + 2-hydroxy-1,4-naphthoquinol
-
-
-
?
1.6.5.10
NADPH + H+ + a quinone
the catalytic cycle of ArsH consists of the acceptance of two electrons from NADPH to reduce the flavin cofactor (reductive half-reaction) and the transfer of these electrons to an acceptor (oxidative half-reaction)
724333
Synechocystis sp.
NADP+ + a quinol
-
-
-
?
1.6.5.10
NADPH + H+ + anthraquinone-2-sulfonate
-
724333
Synechocystis sp.
NADP+ + ?
-
-
-
?
1.6.5.10
NADPH + H+ + coenzyme Q10
-
724333
Synechocystis sp.
NADP+ + reduced coenzyme Q10
-
-
-
?
1.6.5.10
NADPH + H+ + dibromothymoquinone
-
724333
Synechocystis sp.
NADP+ + dibromothymoquinol
-
-
-
?
1.6.5.10
NADPH + H+ + dichlorophenolindophenol
-
724333
Synechocystis sp.
NADP+ + reduced dichlorophenolindophenol
-
-
-
?
1.6.5.10
NADPH + H+ + duroquinone
-
724333
Synechocystis sp.
NADP+ + duroquinol
-
-
-
?
1.6.5.10
NADPH + H+ + menadione
-
724333
Synechocystis sp.
NADP+ + menadiol
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.6.5.5
tetramer
4 * 25900, SDS-PAGE
Synechocystis sp.
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.6.5.5
10
25
assay at
Synechocystis sp.
1.6.5.10
25
-
assay at
Synechocystis sp.
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.6.5.5
5
-
coenzyme Q10
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
9.4
-
anthraquinone-2-sulfonate
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
11
-
2-Hydroxy-1,4-naphthoquinone
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
25
-
duroquinone
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
26
-
menadione
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
35
-
dibromothymoquinone
pH 7.5, 10°C
Synechocystis sp.
1.6.5.5
36.7
-
2,5-dimethyl-4-benzoquinone
pH 7.5, 10°C
Synechocystis sp.
1.6.5.10
5
-
coenzyme Q10
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
9.4
-
anthraquinone-2-sulfonate
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
11
-
2-Hydroxy-1,4-naphthoquinone
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
25
-
duroquinone
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
26
-
menadione
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
35
-
dibromothymoquinone
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
1.6.5.10
36.7
-
2,5-dimethyl-4-benzoquinone
pH 8.0, 25°C, recombinant His-tagged enzyme
Synechocystis sp.
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.6.5.5
7.5
8
assay at
Synechocystis sp.
1.6.5.10
8
-
assay at
Synechocystis sp.
General Information
EC Number
General Information
Commentary
Organism
1.6.5.5
additional information
in silico structural model of ArsH reconstituted with FMN, overview
Synechocystis sp.
1.6.5.5
physiological function
ArsH plays a role in the response to oxidative stress caused by arsenite
Synechocystis sp.
1.6.5.10
evolution
the enzyme is a member of the family of NADPH-dependent FMN reductases
Synechocystis sp.
1.6.5.10
malfunction
arsH mutants are sensitive to the oxidizing agent menadione
Synechocystis sp.
1.6.5.10
additional information
although the enzyme is able to stabilize the anionic semiquinone form of the FMN, reduction of quinones involves the hydroquinone form of the flavin cofactor, and the enzymatic reaction occurs through a ping pong-type mechanism. ArsH is able to catalyze one-electron reactions (oxygen and cytocrome c reduction), involving the FMN semiquinone form, but with lower efficiency
Synechocystis sp.
1.6.5.10
physiological function
ArsH plays a role in the response to oxidative stress caused by arsenite
Synechocystis sp.
General Information (protein specific)
EC Number
General Information
Commentary
Organism
1.6.5.5
additional information
in silico structural model of ArsH reconstituted with FMN, overview
Synechocystis sp.
1.6.5.5
physiological function
ArsH plays a role in the response to oxidative stress caused by arsenite
Synechocystis sp.
1.6.5.10
evolution
the enzyme is a member of the family of NADPH-dependent FMN reductases
Synechocystis sp.
1.6.5.10
malfunction
arsH mutants are sensitive to the oxidizing agent menadione
Synechocystis sp.
1.6.5.10
additional information
although the enzyme is able to stabilize the anionic semiquinone form of the FMN, reduction of quinones involves the hydroquinone form of the flavin cofactor, and the enzymatic reaction occurs through a ping pong-type mechanism. ArsH is able to catalyze one-electron reactions (oxygen and cytocrome c reduction), involving the FMN semiquinone form, but with lower efficiency
Synechocystis sp.
1.6.5.10
physiological function
ArsH plays a role in the response to oxidative stress caused by arsenite
Synechocystis sp.