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Literature summary for 1.14.14.36 extracted from

  • Nielsen, J.; Moller, B.
    Cloning and expression of cytochrome P450 enzymes catalyzing the conversion of tyrosine to p-hydroxyphenylacetaldoxime in the biosynthesis of cyanogenic glucosides in Triglochin maritima (2000), Plant Physiol., 122, 1311-1321.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Triglochin maritima

Organism

Organism UniProt Comment Textmining
Triglochin maritima Q9M7B9
-
-
Triglochin maritima Q9M7C0
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
-
 Triglochin maritima (E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
 ?
additional information no substrate: L-3,4-Dihydroxyphenyl-alanine, i.e. DOPA Triglochin maritima ?
-
 ?

Synonyms

Synonyms Comment Organism
cytochrome P450 CYP79E1
-
 Triglochin maritima
cytochrome P450 CYP79E2
-
 Triglochin maritima

General Information

General Information Comment Organism
physiological function multifunctional N-hydroxylase catalyzing the conversion of tyrosine to 4-hydroxyphenylacetaldoxime in the biosynthesis of the two cyanogenic glucosides taxiphyllin and triglochinin in Triglochin maritima Triglochin maritima
physiological function multifunctional N-hydroxylase catalyzing the conversion of tyrosine to 4-hydroxyphenylacetaldoxime in the biosynthesis of the two cyanogenic glucosides taxiphyllin and triglochinin in Triglochin maritima. When CYP79E1 is reconstituted with CYP71E1 and NADPH-cytochrome P450 oxidoreductase from Sorghum bicolor, efficient conversion of tyrosine to p-hydroxymandelonitrile is observed Triglochin maritima