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

BRENDA support

Literature summary for 3.5.3.1 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
Search for more literature for 3.5.3.1

Application

Application Comment Organism
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)

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

Protein Variants

Protein Variants Comment Organism
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]

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Leishmania donovani A0A0M4MCX5
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Leishmania donovani

Substrates and Products (Substrate)

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

Subunits

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

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Turnover Number [1/s]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
-
 Leishmania donovani

pH Range

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

General Information

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

kcat/KM [mM/s]

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