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

BRENDA support

Literature summary for 2.4.2.8 extracted from

  • Monzani, P.S.; Alfonzo, J.D.; Simpson, L.; Oliva, G.; Thiemann, O.H.
    Cloning, characterization and preliminary crystallographic analysis of Leishmania hypoxanthine-guanine phosphoribosyltransferase (2002), Biochim. Biophys. Acta, 1598, 3-9.
    View publication on PubMed

Application

Application Comment Organism
medicine potential target for antiparasitic chemotherapy Leishmania tarentolae

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli BL21(DE3) Leishmania tarentolae

Crystallization (Commentary)

Crystallization (Comment) Organism
recombinant enzyme, 7 mg/ml, hanging-drop vapour-diffusion method, TMD buffer, pH 7.5, + equal volume of reservoir solution: 18°C or 4°C, pH 5.6 , 19% isopropanol, 19% polyethylene glycol 4000, 5% glycerol, or 17% polyethylene glycol 4000, 5% glycerol Leishmania tarentolae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0028
-
guanine recombinant enzyme, with 5-phospho-alpha-D-ribose 1-diphosphate Leishmania tarentolae
0.0044
-
hypoxanthine recombinant enzyme, with 5-phospho-alpha-D-ribose 1-diphosphate Leishmania tarentolae
0.127
-
5-phosphoribosyl 1-diphosphate recombinant enzyme, with guanine Leishmania tarentolae
0.138
-
5-phosphoribosyl 1-diphosphate recombinant enzyme, with hypoxanthine Leishmania tarentolae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
23000
-
2 * 23000, recombinant enzyme, SDS-PAGE Leishmania tarentolae
50000
-
recombinant enzyme, gel filtration Leishmania tarentolae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Leishmania tarentolae salvage incorporation of exogenous purine nucleotides, no de novo synthesis ?
-
?
additional information Leishmania tarentolae enzyme is essential for salvaging exogenous purine bases ?
-
?

Organism

Organism UniProt Comment Textmining
Leishmania tarentolae Q9NJI5 gene hgprt
-

Purification (Commentary)

Purification (Comment) Organism
recombinant from Escherichia coli Leishmania tarentolae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
Leishmania tarentolae GMP + diphosphate
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
Leishmania tarentolae IMP + diphosphate
-
?
additional information salvage incorporation of exogenous purine nucleotides, no de novo synthesis Leishmania tarentolae ?
-
?
additional information enzyme is essential for salvaging exogenous purine bases Leishmania tarentolae ?
-
?

Subunits

Subunits Comment Organism
dimer 2 * 23000, recombinant enzyme, SDS-PAGE Leishmania tarentolae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
recombinant enzyme, pI: 8.2 Leishmania tarentolae