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Literature summary for 3.5.3.1 extracted from

  • Lavulo, L.T.; Sossong, T.M., Jr.; Brigham-Burke, M.R.; Doyle, M.L.; Cox, J.D.; Christianson, D.W.; Ash, D.E.
    Subunit-subunit interactions in trimeric arginase. Generation of active monomers by mutation of a single amino acid (2001), J. Biol. Chem., 276, 14242-14248.
    View publication on PubMed
Search for more literature for 3.5.3.1

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of wild-type and mutant enzymes in Escherichia coli BL21(DE3) Rattus norvegicus

Crystallization (Commentary)

Crystallization (Comment) Organism
recombinant R308K mutant, X-ray diffraction structure determination and analysis at 3.0 A resolution Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
R308A site-directed mutagenesis, 17% activity compared to the wild-type enzyme, mutant forms monomers instead of trimers like the wild-type enzyme, reduced unfolding temperature compared to the wild-type enzyme Rattus norvegicus
R308E site-directed mutagenesis, 17% activity compared to the wild-type enzyme, mutant forms monomers instead of trimers like the wild-type enzyme, reduced unfolding temperature compared to the wild-type enzyme Rattus norvegicus
R308K site-directed mutagenesis, 13% activity compared to the wild-type enzyme, mutant forms monomers instead of trimers like the wild-type enzyme, reduced unfolding temperature compared to the wild-type enzyme Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.07
-
 L-arginine wild-type enzyme, pH 9.0 Rattus norvegicus
2.5
-
 L-arginine mutant R308A, pH 9.0 Rattus norvegicus
2.6
-
 L-arginine mutant R308E, pH 9.0 Rattus norvegicus
2.7
-
 L-arginine mutant R308K, pH 9.0 Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ dependent on, manganese-metalloenzyme, wild-type enzyme contains 1.97 mol Mn2+ per mol of subunit, mutants R308A and R308E contain 2.1 mol, and mutant R308K 1.25 mol per mol of subunit Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
30000
-
 mutants R308A and R308E, gel filtration Rattus norvegicus
34000
-
 mutant R308K, gel filtration Rattus norvegicus
35000
-
 3 * 35000, SDS-PAGE, wild-type enzyme Rattus norvegicus
94400
-
 wild-type enzyme, gel filtration Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-

Subunits

Subunits Comment Organism
monomer 1 * 30000-34000, mutant enzymes R308A, R308E, and R308K Rattus norvegicus
trimer 3 * 35000, SDS-PAGE, wild-type enzyme Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
72
-
 L-arginine mutant R308K, pH 9.0 Rattus norvegicus
84
-
 L-arginine mutant R308A, pH 9.0 Rattus norvegicus
89
-
 L-arginine mutant R308E, pH 9.0 Rattus norvegicus
220
-
 L-arginine wild-type enzyme, pH 9.0 Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
 assay at Rattus norvegicus