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Literature summary extracted from

  • Orellana, M.S.; Lopez, V.; Uribe, E.; Fuentes, M.; Salas, M.; Carvajal, N.
    Insights into the interaction of human liver arginase with tightly and weakly bound manganese ions by chemical modification and site-directed mutagenesis studies (2002), Arch. Biochem. Biophys., 403, 155-159.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.5.3.1 H101N 60% of wild-type activity, unaltered Km for arginine and Ki for lysine compared to the wild-type enzyme Homo sapiens
3.5.3.1 H126N 82% of wild-type activity, unaltered Km for arginine and Ki for lysine compared to the wild-type enzyme Homo sapiens
3.5.3.1 H141F activation by Mn2+ Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.3.1 diethyl dicarbonate causes a loss in ability of Mn2+ to reactivate inactive subunits of wild-type and mutant enzyme H141F, effect is reversed by hydroxylamine Homo sapiens
3.5.3.1 EDTA
-
 Homo sapiens
3.5.3.1 lysine
-
 Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.3.1 Mn2+ activates, role of weakly and tightly bound metal ions in wild-type and mutant enzymes, metal content, overview Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.5.3.1 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.3.1 liver
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.3.1 L-arginine + H2O
-
 Homo sapiens L-ornithine + urea
-
 ?