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Literature summary for 1.14.14.37 extracted from

  • Kahn, R.A.; Fahrendorf, T.; Halkier, B.A.; Moller, B.L.
    Substrate specificity of the cytochrome P450 enzymes CYP79A1 and CYP71E1 involved in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench (1999), Arch. Biochem. Biophys., 363, 9-18.
    View publication on PubMed
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General Stability

General Stability Organism
CYP71E1 is labile and prone to rapid denaturation at room temperature. CYP71E1 is isolated in the low spin form. Sorghum bicolor

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
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 Sorghum bicolor
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Organism

Organism UniProt Comment Textmining
Sorghum bicolor O48958
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Source Tissue

Source Tissue Comment Organism Textmining
seedling
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 Sorghum bicolor
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
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 Sorghum bicolor (S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O overall reaction. NADPH is a much better cofactor for NADPH-hemoprotein reductase than NADH although NADH does support the entire catalytic cycle ?
(E)-phenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2 oxime dervied from phenylalanine, 35% of the activity with (E)-4-hydroxyphenylacetaldehyde oxime Sorghum bicolor (S)-mandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
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 ?
additional information CYP71E1 metabolizes aromatic oximes efficiently, whereas aliphatic oximes are slowly metabolized Sorghum bicolor ?
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 ?