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Literature summary for 1.14.14.91 extracted from

  • Beneviste, I.; Salaun, J.P.; Durst, F.
    Wounding-induced cinnamic acid hydroxylase in Jerusalem artichoke tuber (1977), Phytochemistry, 16, 69-73.
No PubMed abstract available
Search for more literature for 1.14.14.91

Inhibitors

Inhibitors Comment Organism Structure
NADP+ competitive Helianthus tuberosus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.013
-
 NADPH
-
 Helianthus tuberosus

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
 Helianthus tuberosus 5783
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
trans-cinnamate + [reduced NADPH-hemoprotein reductase] + O2 Helianthus tuberosus the enzyme is regulated by the NADPH/NADP+ ratio 4-hydroxycinnamate + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Helianthus tuberosus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
tuber
-
 Helianthus tuberosus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
trans-cinnamate + [reduced NADPH-hemoprotein reductase] + O2
-
 Helianthus tuberosus 4-hydroxycinnamate + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
trans-cinnamate + [reduced NADPH-hemoprotein reductase] + O2 the enzyme is regulated by the NADPH/NADP+ ratio Helianthus tuberosus 4-hydroxycinnamate + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?

Cofactor

Cofactor Comment Organism Structure
cytochrome P450 electrons are transferred from NADPH, the preferential electron donor of the system, to cytochrome P-450 via NADPH-cytochrome P-450 reductase Helianthus tuberosus
NADH NADH alone can not supply the enzyme with electrons. NADH, 0.5 mM, results in 51% stimulation when NADPH is present at a saturating level, 0.5 mM Helianthus tuberosus