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Literature summary extracted from

  • Yanik, T.; Donaldson, R.P.
    A protective association between catalase and isocitrate lyase in peroxisomes (2005), Arch. Biochem. Biophys., 435, 243-252.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.3.1 H2O2 inhibits enzyme activity with increased concentrations, no activity above 1.3 mM Ricinus communis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.1.3.1 glyoxysome
-
Ricinus communis 9514
-

Organism

EC Number Organism UniProt Comment Textmining
4.1.3.1 Ricinus communis
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
4.1.3.1 H2O2 inactivates isocitrate lyase and degrades its product glyoxylate. Gel filtration, cross-linking and co-immunoprecipitation studies indicate association of isocitrate lyase with catalase, this would afford protection from H2O2. Ricinus communis

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.3.1
-
Ricinus communis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.3.1 isocitrate
-
Ricinus communis succinate + glyoxylate
-
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Synonyms

EC Number Synonyms Comment Organism
4.1.3.1 ICL
-
Ricinus communis