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Literature summary extracted from

  • Billett, E.E.; Smith, H.
    Cinnamic acid 4-hydroxylase from Gherkin tissue (1978), Phytochemistry, 17, 1511-1516.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.14.91 2-mercaptoethanol 0.1 mM, stimulates Cucumis sativus
1.14.14.91 ascorbic acid 0.1 mM, stimulates Cucumis sativus
1.14.14.91 dithiothreitol 0.1 mM, stimulates Cucumis sativus
1.14.14.91 glutathione 0.1 mM, stimulates Cucumis sativus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.14.91 2,4-dinitrophenol 0.1 mM, 83% loss of activity Cucumis sativus
1.14.14.91 2-mercaptoethanol 2.0 mM Cucumis sativus
1.14.14.91 antimycin A 0.005 mM, 16% loss of activity Cucumis sativus
1.14.14.91 ascorbic acid 2.0 mM Cucumis sativus
1.14.14.91 chlorogenic acid 0.1 mM, 9% loss of activity Cucumis sativus
1.14.14.91 CO
-
 Cucumis sativus
1.14.14.91 CuSO4 1 mM, complete loss of activity Cucumis sativus
1.14.14.91 dithiothreitol 2.0 mM Cucumis sativus
1.14.14.91 EDTA 1 mM, 18% loss of activity Cucumis sativus
1.14.14.91 FAD 1 mM, 73% loss of activity Cucumis sativus
1.14.14.91 FMN 1 mM, 75% loss of activity Cucumis sativus
1.14.14.91 gallic acid 0.1 mM, 20% loss of activity Cucumis sativus
1.14.14.91 KCl 200 mM, 39% loss of activity. 500 mM, 69% loss of activity Cucumis sativus
1.14.14.91 KCN 10 mM, 21% loss of activity Cucumis sativus
1.14.14.91 menadione 0.1 mM, 92% loss of activity Cucumis sativus
1.14.14.91 MnCl2 1 mM, 27% loss of activity Cucumis sativus
1.14.14.91 additional information no inhibition by p-coumaric acid Cucumis sativus
1.14.14.91 Sodium azide 10 mM, 64% loss of activity Cucumis sativus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.14.91 0.0025
-
 trans-cinnamate
-
 Cucumis sativus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.14.91 endoplasmic reticulum
-
 Cucumis sativus 5783
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.14.91 KCN 1 mM, increase to 125% of the activity Cucumis sativus

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.91 Cucumis sativus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.14.91 cotyledon
-
 Cucumis sativus
-
1.14.14.91 hypocotyl
-
 Cucumis sativus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.91 trans-cinnamate + [reduced NADPH-hemoprotein reductase] + O2
-
 Cucumis sativus 4-hydroxycinnamate + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.14.91 7.5
-
-
 Cucumis sativus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.14.14.91 5.5 8.8 about 50% of maximal activity at pH 5.5 and at pH 8.8 Cucumis sativus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.91 cytochrome P450 involved in hydroxylation Cucumis sativus
1.14.14.91 NADH NADH has a synergistic effect on NADPH-supported hydroxylation, at both nonsaturating, 0.1 mM, and near-saturating, 1 mM, concentrations of NADPH Cucumis sativus