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Literature summary extracted from

  • Hervas, M.; Lopez-Maury, L.; Leon, P.; Sanchez-Riego, A.M.; Florencio, F.J.; Navarro, J.A.
    ArsH from the cyanobacterium Synechocystis sp. PCC 6803 is an efficient NADPH-dependent quinone reductase (2012), Biochemistry, 51, 1178-1187.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) 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 Comment 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 Comment 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] Comment 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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 UniProt Comment 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 Comment Organism Reaction ID
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 Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 Synechocystis sp. ?
-
?
1.6.5.5 NADPH + H+ + 2 2,5-dimethyl-4-benzoquinone
-
Synechocystis sp. NADP+ + 2 2,5-dimethyl-4-benzosemiquinone
-
?
1.6.5.5 NADPH + H+ + 2 2-hydroxy-1,4-naphthoquinone
-
Synechocystis sp. NADP+ + 2 2-hydroxy-1,4-naphthosemiquinone
-
?
1.6.5.5 NADPH + H+ + 2 anthraquinone-2-sulfonate
-
Synechocystis sp. NADP+ + ?
-
?
1.6.5.5 NADPH + H+ + 2 coenzyme Q10
-
Synechocystis sp. NADP+ + ?
-
?
1.6.5.5 NADPH + H+ + 2 dibromothymoquinone
-
Synechocystis sp. NADP+ + 2 dibromothymosemiquinone
-
?
1.6.5.5 NADPH + H+ + 2 duroquinone
-
Synechocystis sp. NADP+ + 2 durosemiquinone
-
?
1.6.5.5 NADPH + H+ + 2 menadione
-
Synechocystis sp. NADP+ + ?
-
?
1.6.5.5 NADPH + H+ + 2 quinone
-
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) Synechocystis sp. NADP+ + 2 semiquinone
-
?
1.6.5.10 additional information NADH, deazariboflavin, and methylviologen can also act as electron donors Synechocystis sp. ?
-
?
1.6.5.10 NADPH + H+ + 2,5-dimethyl-4-benzoquinone
-
Synechocystis sp. NADP+ + 2,5-dimethyl-4-benzoquinonl
-
?
1.6.5.10 NADPH + H+ + 2-hydroxy-1,4-naphthoquinone
-
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) Synechocystis sp. NADP+ + a quinol
-
?
1.6.5.10 NADPH + H+ + anthraquinone-2-sulfonate
-
Synechocystis sp. NADP+ + ?
-
?
1.6.5.10 NADPH + H+ + coenzyme Q10
-
Synechocystis sp. NADP+ + reduced coenzyme Q10
-
?
1.6.5.10 NADPH + H+ + dibromothymoquinone
-
Synechocystis sp. NADP+ + dibromothymoquinol
-
?
1.6.5.10 NADPH + H+ + dichlorophenolindophenol
-
Synechocystis sp. NADP+ + reduced dichlorophenolindophenol
-
?
1.6.5.10 NADPH + H+ + duroquinone
-
Synechocystis sp. NADP+ + duroquinol
-
?
1.6.5.10 NADPH + H+ + menadione
-
Synechocystis sp. NADP+ + menadiol
-
?

Subunits

EC Number Subunits Comment Organism
1.6.5.5 tetramer 4 * 25900, SDS-PAGE Synechocystis sp.

Synonyms

EC Number Synonyms Comment Organism
1.6.5.5 ArsH
-
Synechocystis sp.
1.6.5.5 NADPH-dependent quinone reductase
-
Synechocystis sp.
1.6.5.10 ArsH
-
Synechocystis sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment 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 Comment 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 Comment 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 Comment 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 Comment 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

General Information

EC Number General Information Comment 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.