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Literature summary for 1.6.2.4 extracted from

  • Osman, A.M.; van Noort, P.C.M.
    Activation of paraquat in the earthworm Allolobophora chlorotica is mediated by NAD(P)H-cytochrome c reductase activities (2004), Pestic. Biochem. Physiol., 79, 101-110.
No PubMed abstract available

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 ferricytochrome P450 + NADPH Allolobophora chlorotica involved in drug metabolism 2 ferrocytochrome P450 + NADP+ + H+
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?
paraquat + NADPH Allolobophora chlorotica paraquat is a toxic herbicide ?
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?

Organism

Organism UniProt Comment Textmining
Allolobophora chlorotica
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricytochrome c + NADPH
-
Allolobophora chlorotica 2 ferrocytochrome c + NADP+ + H+
-
?
2 ferricytochrome P450 + NADPH involved in drug metabolism Allolobophora chlorotica 2 ferrocytochrome P450 + NADP+ + H+
-
?
paraquat + NADPH paraquat is a toxic herbicide Allolobophora chlorotica ?
-
?

Synonyms

Synonyms Comment Organism
NADPH-cytochrome P450 reductase
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Allolobophora chlorotica
NADPH-ferrihemoprotein reductase
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Allolobophora chlorotica
NADPH:ferrihemoprotein oxidoreductase
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Allolobophora chlorotica

Cofactor

Cofactor Comment Organism Structure
FAD together with FMN Allolobophora chlorotica
FMN together with FAD Allolobophora chlorotica
additional information NADH dependent activity on paraquat ist thought to be due to the presence of cytochrome b5 reductase Allolobophora chlorotica
NADPH
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Allolobophora chlorotica