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Literature summary extracted from

  • Legaz, M.E.; Fontaniella, B.; Millanes, A.M.; Carlos, V.
    Secreted arginases from phylogenetically farrelated lichen species act as cross-recognition factors for two different algal cells (2004), Eur. J. Cell Biol., 83, 435-446.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.3.1 Ca2+ inhibitory to enzymic activity in presence of Mn2+, enhances lectin function of enzyme Evernia prunastri
3.5.3.1 Ca2+ inhibitory to enzymic activity in presence of Mn2+, enhances lectin function of enzyme Xanthoria parietina
3.5.3.1 additional information binding to lectins is inhibitory to enzymic activity, which is recovered after desorption of the lectin with alpha-D-galactose Evernia prunastri
3.5.3.1 additional information binding to lectins is inhibitory to enzymic activity, which is recovered after desorption of the lectin with alpha-D-galactose Xanthoria parietina

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.5.3.1 extracellular
-
 Evernia prunastri
-
-
3.5.3.1 extracellular
-
 Xanthoria parietina
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.3.1 Mn2+ required for catalysis, enhances lectin function of enzyme Evernia prunastri
3.5.3.1 Mn2+ required for catalysis, enhances lectin function of enzyme Xanthoria parietina

Organism

EC Number Organism UniProt Comment Textmining
3.5.3.1 Evernia prunastri
-
 enzyme additionally shows lectin function, binding to the cell wall of both homologous and heterologous algae
-
3.5.3.1 Xanthoria parietina
-
 enzyme additionally shows lectin function, binding to the cell wall of both homologous and heterologous algae
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.3.1 L-arginine + H2O
-
 Evernia prunastri L-ornithine + urea
-
 ?
3.5.3.1 L-arginine + H2O
-
 Xanthoria parietina L-ornithine + urea
-
 ?