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Literature summary 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

EC Number Application Comment Organism
2.4.2.8 medicine potential target for antiparasitic chemotherapy Leishmania tarentolae

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.2.8 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.2.8 0.0028
-
guanine recombinant enzyme, with 5-phospho-alpha-D-ribose 1-diphosphate Leishmania tarentolae
2.4.2.8 0.0044
-
hypoxanthine recombinant enzyme, with 5-phospho-alpha-D-ribose 1-diphosphate Leishmania tarentolae
2.4.2.8 0.127
-
5-phosphoribosyl 1-diphosphate recombinant enzyme, with guanine Leishmania tarentolae
2.4.2.8 0.138
-
5-phosphoribosyl 1-diphosphate recombinant enzyme, with hypoxanthine Leishmania tarentolae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.2.8 23000
-
2 * 23000, recombinant enzyme, SDS-PAGE Leishmania tarentolae
2.4.2.8 50000
-
recombinant enzyme, gel filtration Leishmania tarentolae

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.8 Leishmania tarentolae Q9NJI5 gene hgprt
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.2.8 recombinant from Escherichia coli Leishmania tarentolae

Substrates and Products (Substrate)

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

Subunits

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

pH Optimum

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