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Literature summary for 1.14.14.37 extracted from

  • Shimada, M.; Conn, E.E.
    The enzymatic conversion of p-hydroxyphenylacetaldoxime to p-hydroxymandelonitrile (1977), Arch. Biochem. Biophys., 180, 199-207.
    View publication on PubMed
Search for more literature for 1.14.14.37

Inhibitors

Inhibitors Comment Organism Structure
2-hydroxy(p-hydroxyphenyl)acetaldoxime in higher concentrations Sorghum bicolor

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.2
-
 p-hydroxyphenylacetaldoxime
-
 Sorghum bicolor
0.35
-
 p-hydroxyphenylacetonitrile
-
 Sorghum bicolor

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
 Sorghum bicolor
-
-

Organism

Organism UniProt Comment Textmining
Sorghum bicolor
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
seedling
-
 Sorghum bicolor
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
-
 Sorghum bicolor (S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
 ?
2-hydroxy(p-hydroxyphenyl)acetaldoxime poor substrate Sorghum bicolor 4-hydroxymandelonitrile + H2O
-
 ?
4-hydroxyphenylacetonitrile + [reduced NADPH-hemoprotein reductase] + O2
-
 Sorghum bicolor (S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
-
 Sorghum bicolor (E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
 ?

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Sorghum bicolor
O2
-
 Sorghum bicolor

General Information

General Information Comment Organism
physiological function during biosynthesis of dhurrin, 4-hydroxyphenylacetonitrile functions as an intermediate, and not 2-hydroxy(4-hydroxyphenyl)-acetaldoxime Sorghum bicolor