Literature summary for 3.5.3.1 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.

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Protein Variants

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

Inhibitors

Inhibitors	Comment	Organism	Structure
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
EDTA	-	Homo sapiens
lysine	-	Homo sapiens

Metals/Ions

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

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
liver	-	Homo sapiens	-

Substrates and Products (Substrate)

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

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Release 2023.1 (January 2023)