Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli strain JM109 | Homo sapiens |
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 | 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 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 | 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 Maximum [Da] | Comment | Organism |
---|---|---|---|
32000 | - |
gel filtration, replacement of Arg-308 with alanine, with or without truncation, yielded monomeric species | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P05089 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-arginine + H2O | - |
Homo sapiens | L-ornithine + urea | - |
? |
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 | Comment | Organism |
---|---|---|
arginase I | - |
Homo sapiens |
human arginase type I | - |
Homo sapiens |
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 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 |