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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
3.5.3.1 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
3.5.3.1 R308A site-directed mutagenesis, single mutant R308A changed to a trimeric and kinetically cooperative form, with or without truncation Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.3.1 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.3.1 1.5
-
 L-arginine wild-type, pH 9.5 Homo sapiens
3.5.3.1 3.7
-
 L-arginine monomeric E256Q variant, pH 9.5 Homo sapiens

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.3.1 32000
-
 gel filtration, replacement of Arg-308 with alanine, with or without truncation, yielded monomeric species Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.5.3.1 Homo sapiens P05089
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.3.1
-
 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
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.3.1 monomer replacement of Arg-308 with alanine, with or without truncation, yielded monomeric species Homo sapiens
3.5.3.1 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

EC Number Synonyms Comment Organism
3.5.3.1 arginase I
-
 Homo sapiens
3.5.3.1 human arginase type I
-
 Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.3.1 180
-
 L-arginine monomeric E256Q variant, pH 9.5 Homo sapiens
3.5.3.1 190
-
 L-arginine wild-type, pH 9.5 Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.3.1 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