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Literature summary for 1.14.14.91 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

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

Inhibitors

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

KM Value [mM]

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

Localization

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Cucumis sativus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
cotyledon
-
Cucumis sativus
-
hypocotyl
-
Cucumis sativus
-

Substrates and Products (Substrate)

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Cucumis sativus

pH Range

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

Cofactor

Cofactor Comment Organism Structure
cytochrome P450 involved in hydroxylation Cucumis sativus
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