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Literature summary 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

General Stability

EC Number General Stability Organism
1.14.14.36 fairly stable Sorghum bicolor
1.14.14.37 CYP71E1 is labile and prone to rapid denaturation at room temperature. CYP71E1 is isolated in the low spin form. Sorghum bicolor

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.14.36 0.013
-
 NADPH
-
 Sorghum bicolor
1.14.14.36 0.3
-
 NADH
-
 Sorghum bicolor

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.14.36 microsome
-
 Sorghum bicolor
-
-
1.14.14.37 microsome
-
 Sorghum bicolor
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.36 L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase] Sorghum bicolor enzyme in biosynthesis of cyanogenic glucosides N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.36 Sorghum bicolor
-
-
-
1.14.14.36 Sorghum bicolor Q43135
-
-
1.14.14.37 Sorghum bicolor O48958
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.14.36 seedling
-
 Sorghum bicolor
-
1.14.14.37 seedling
-
 Sorghum bicolor
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.36 L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
-
 Sorghum bicolor (E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O overall reaction. NADPH is a much better cofactor for NADPH-hemoprotein reductase than NADH although NADH does support the entire catalytic cycle ?
1.14.14.36 L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase] intermediate products: N-hydroxytyrosine, N,N-dihydroxytyrosine, (E)-p-hydroxyphenylacetaldoxime Sorghum bicolor (E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
 ?
1.14.14.36 L-tyrosine + O2 + NADH + H+
-
 Sorghum bicolor N-hydroxy-L-tyrosine + NAD+ + H2O
-
 r
1.14.14.36 L-tyrosine + O2 + NADPH + H+
-
 Sorghum bicolor N-hydroxy-L-tyrosine + NADP+ + H2O
-
 r
1.14.14.36 L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase] enzyme in biosynthesis of cyanogenic glucosides Sorghum bicolor N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
1.14.14.36 additional information CYP79A1 has a very high substrate specificity, tyrosine being the only substrate found. Analogs 1-nitro-2-p-(hydroxyphenyl)ethane, N-hydroxytyrosine and phenylalanine are able to bind to the enzyme, without being metabolized Sorghum bicolor ?
-
 ?
1.14.14.37 (E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
-
 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 ?
1.14.14.37 (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
-
 ?
1.14.14.37 additional information CYP71E1 metabolizes aromatic oximes efficiently, whereas aliphatic oximes are slowly metabolized Sorghum bicolor ?
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.36 NADPH better cofactor than NADH Sorghum bicolor