Literature summary for 3.5.3.1 extracted from

Garcia, D.; Uribe, E.; Lobos, M.; Orellana, M.S.; Carvajal, N.
Studies on the functional significance of a C-terminal S-shaped motif in human arginase type I: essentiality for cooperative effects (2009), Arch. Biochem. Biophys., 481, 16-20.

Search for more literature for 3.5.3.1

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli strain JM109	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
E256Q	In contrast with R308A, the monomeric E256Q variant of the human enzyme is totally inactivated by dialysis in the presence of EDTA, leading to the suggestion that the quaternary structure could play a role in the affinity of metal binding to arginase	Homo sapiens
R308A	site-directed mutagenesis, single mutant R308A changed to a trimeric and kinetically cooperative form, with or without truncation	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
EDTA	in contrast with R308A, the monomeric E256Q variant of the human enzyme is totally inactivated by dialysis in the presence of EDTA, leading to the suggestion that the quaternary structure could play a role in the affinity of metal binding to arginase	Homo sapiens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1.5	-	L-arginine	wild-type, pH 9.5	Homo sapiens
3.7	-	L-arginine	monomeric E256Q variant, pH 9.5	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Guanidinium chloride	the single mutant R308A changes to a trimeric and kinetically cooperative form, whereas the other enzyme variants are not altered	Homo sapiens
Mn2+	increase in enzyme activity by incubation with 5 mM Mn2+ for 10 min at 60°C	Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
32000	-	gel filtration, replacement of Arg-308 with alanine, with or without truncation, yielded monomeric species	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P05089	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Homo sapiens

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
monomer	replacement of Arg-308 with alanine, with or without truncation, yielded monomeric species	Homo sapiens
More	functional significance of a C-terminal S-shaped motif (residues 304-322) is explored by examining the kinetic properties of the R308A mutant and truncated species terminating in either Arg-308 or Ala-308	Homo sapiens

Synonyms

Synonyms	Comment	Organism
arginase I	-	Homo sapiens
human arginase type I	-	Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
180	-	L-arginine	monomeric E256Q variant, pH 9.5	Homo sapiens
190	-	L-arginine	wild-type, pH 9.5	Homo sapiens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
9.5	-	all mutants are kinetically indistinguishable from the wild-type enzyme at the optimum pH of 9.5. At the more physiological, pH 7.5, hyperbolic kinetics is observed for all the mutants, in contrast with the cooperative behavior exhibited by the wild-type species	Homo sapiens

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Release 2023.1 (January 2023)