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Literature summary for 1.6.2.4 extracted from

  • Higashimoto, Y.; Sato, H.; Sakamoto, H.; Takahashi, K.; Palmer, G.; Noguchi, M.
    The reactions of heme- and verdoheme-heme oxygenase-1 complexes with FMN-depleted NADPH-cytochrome P450 reductase. Electrons required for verdoheme oxidation can be transferred through a pathway not involving FMN (2006), J. Biol. Chem., 281, 31659-31667.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information FMN-depleted enzyme is prepared by dialyzing the mutant enzyme Y140A/Y178A, against 2 M KBr. FMN-depleted enzyme can support the conversion of verdoheme to the ferric biliverdin-iron chelate, indicating that electrons required for verdoheme oxidation can be transferred through a pathway not involving FMN Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
recombinant
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Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricytochrome c + NADPH
-
Rattus norvegicus 2 ferrocytochrome c + NADP+ + H+
-
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Cofactor

Cofactor Comment Organism Structure
NADPH
-
Rattus norvegicus