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Literature summary for 3.5.3.1 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
Search for more literature for 3.5.3.1

Inhibitors

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

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

Metals/Ions

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

Organism

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

Substrates and Products (Substrate)

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