Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Gaur, N.; Kumar, K.; Gupta, C.L.; Saxena, J.K.
    Molecular characterization of recombinant arginase of Leishmania donovani (2019), Protein Expr. Purif., 159, 1-9 .
    View publication on PubMed

Application

EC Number Application Comment Organism
3.5.3.1 drug development arginase catalyzes the first committed step in the biosynthesis of polyamines that enable cell growth and hence potential drug target for the treatment of leishmaniasis Leishmania donovani

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.3.1 overexpression in Escherichia coli BL21 (DE3) Leishmania donovani

Protein Variants

EC Number Protein Variants Comment Organism
3.5.3.1 E288Q increase in KM value of the E288Q mutant enzyme as compared to wild-type enzyme suggests that substrate binding is significantly affected by the mutation Leishmania donovani

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.3.1 24.76
-
 L-arginine pH 9.0, 37°C, wild-type enzyme Leishmania donovani
3.5.3.1 107
-
 L-arginine pH 9.0, 37°C, mutant enzyme E288Q Leishmania donovani

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.3.1 36000
-
 SDS-PAGE Leishmania donovani
3.5.3.1 108000
-
 gel filtration Leishmania donovani

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.3.1 L-arginine + H2O Leishmania donovani arginase catalyzes the first committed step in the biosynthesis of polyamines L-ornithine + urea
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.3.1 Leishmania donovani A0A0M4MCX5
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.3.1
-
 Leishmania donovani

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.3.1 L-arginine + H2O
-
 Leishmania donovani L-ornithine + urea
-
 ?
3.5.3.1 L-arginine + H2O arginase catalyzes the first committed step in the biosynthesis of polyamines Leishmania donovani L-ornithine + urea
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.3.1 homotrimer 3 * 36000, SDs-PAGE Leishmania donovani

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.3.1 37
-
-
 Leishmania donovani

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.5.3.1 30 45 30°C: about 70% of maximal activity, 45°C: about 50% of maximal activity Leishmania donovani

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.3.1 179
-
 L-arginine pH 9.0, 37°C, wild-type enzyme Leishmania donovani
3.5.3.1 190
-
 L-arginine pH 9.0, 37°C, mutant enzyme E288Q Leishmania donovani

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.3.1 9
-
-
 Leishmania donovani

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.5.3.1 8 10 pH 8.0: about 60% of maximal activity, pH 10.5: about 55% of maximal activity Leishmania donovani

General Information

EC Number General Information Comment Organism
3.5.3.1 metabolism arginase catalyzes the first committed step in the biosynthesis of polyamines Leishmania donovani

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.5.3.1 1.7
-
 L-arginine pH 9.0, 37°C, mutant enzyme E288Q Leishmania donovani
3.5.3.1 7.2
-
 L-arginine pH 9.0, 37°C, wild-type enzyme Leishmania donovani