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Literature summary for 1.14.19.69 extracted from

  • Zhao, B.; Lamb, D.C.; Lei, L.; Kelly, S.L.; Yuan, H.; Hachey, D.L.; Waterman, M.R.
    Different binding modes of two flaviolin substrate molecules in cytochrome P450 158A1 (CYP158A1) compared to CYP158A2 (2007), Biochemistry, 46, 8725-8733.
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
free isoform CYP158A1, in complex with imidazole and in complex with flaviolin. Comparison of structures with isoform CYP158A2. In isoform CYP158A1, only one flaviolin molecule is present close to the heme iron, and the second flaviolin molecule binds at the entrance of the putative substrate access channel on the protein distal surface 9 A away Streptomyces coelicolor

Organism

Organism UniProt Comment Textmining
Streptomyces coelicolor
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 comparison of isoforms CYP158A1 and CYP158A2
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4 flaviolin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
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 Streptomyces coelicolor 3,3'-biflaviolin + 3,8'-biflaviolin + 4 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O with isoform CYP158A1, product 3,8'-biflaviolin is about 40% of total product. Isoform CYP158A1 generates a further biflaviolin isomer and some triflaviolin ?