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Literature summary extracted from

  • Czichi, U.; Kindl, H.
    Phenylalanine ammonia lyase and cinnamic acid hydroxylases as assembled consecutive enzymes on microsomal membranes of cucumber cotyledons: cooperation and subcellular distribution (1977), Planta, 134, 133-143.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.13.14 additional information white light treatment for 200 min leads to 50% activation Cucumis sativus
1.14.13.14 sulfonic acid 700% activation at 0.003% Cucumis sativus
1.14.13.14 Triton X-100 700% activation at 0.025% Cucumis sativus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.13.14 KCN 70% inhibition at 10 mM Cucumis sativus
1.14.13.14 additional information UV-light treatment for 200 min leads to 30% inhibition Cucumis sativus
1.14.13.14 Triton X-100 concentration higher than 0.5% deactivates the enzyme Cucumis sativus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.13.14 chloroplast predominantly, chloroplast membrane Cucumis sativus 9507
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.14 trans-cinnamate + NADPH + O2 Cucumis sativus
-
 2-hydroxycinnamate + NADP+ + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.14 Cucumis sativus
-
 cucumber
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.13.14 cotyledon
-
 Cucumis sativus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.14 trans-cinnamate + NADPH + O2
-
 Cucumis sativus 2-hydroxycinnamate + NADP+ + H2O
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.14 NADPH
-
 Cucumis sativus