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Literature summary extracted from

  • Szczepaniak, K.; Worch, R.; Grzyb, J.
    Ferredoxin NADP+ oxidoreductase in junction with CdSe/ZnS quantum dots Characteristics of an enzymatically active nanohybrid (2013), J. Phys. Condens. Matter, 25, 194162 .
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.18.1.2 0.0074
-
reduced ferricyanide at pH 8.7 and 22°C Synechocystis sp.
1.18.1.2 0.46
-
reduced 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone at pH 7.5 and 22°C Synechocystis sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.18.1.2 reduced ferredoxin + NADP+ + H+ Synechocystis sp.
-
oxidized ferredoxin + NADPH
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.2 Synechocystis sp.
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.18.1.2 HisTrap column chromatography Synechocystis sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.2 reduced 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone + NADP+ + H+
-
Synechocystis sp. oxidized 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone + NADPH
-
?
1.18.1.2 reduced ferredoxin + NADP+ + H+
-
Synechocystis sp. oxidized ferredoxin + NADPH
-
?
1.18.1.2 reduced ferricyanide + NADP+ + H+
-
Synechocystis sp. ferrocyanide + NADPH
-
?

Synonyms

EC Number Synonyms Comment Organism
1.18.1.2 ferredoxin:NADP+ oxidoreductase
-
Synechocystis sp.
1.18.1.2 FNR
-
Synechocystis sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.18.1.2 0.43
-
reduced 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone at pH 7.5 and 22°C Synechocystis sp.
1.18.1.2 0.43
-
reduced ferricyanide at pH 8.7 and 22°C Synechocystis sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.2 FAD one FAD molecule per enzyme molecule Synechocystis sp.