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Literature summary extracted from

  • Jardim, A.; Ullman, B.
    The conserved serine-tyrosine dipeptide in Leishmania donovani hypoxanthine-guanine phosphoribosyltransferase is essential for catalytic activity (1997), J. Biol. Chem., 272, 8967-8973.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.2.8 functional expression of wild-type enzyme and mutants in an enzyme-deficient Escherichia coli strain Leishmania donovani

Protein Variants

EC Number Protein Variants Comment Organism
2.4.2.8 additional information wild-type enzyme complements enzyme deficiency of the bacterial enzyme in Escherichia coli Leishmania donovani
2.4.2.8 S95A site-directed mutagenesis, dramatic reduction of catalytic activity, weak complementation of bacterial enzyme deficient strain Leishmania donovani
2.4.2.8 S95C site-directed mutagenesis, 2-3fold reduction of kcat, weak complementation of bacterial enzyme deficient strain Leishmania donovani
2.4.2.8 S95E site-directed mutagenesis, dramatic reduction of catalytic activity, no complementation of bacterial enzyme deficient strain Leishmania donovani
2.4.2.8 S95T site-directed mutagenesis, 2-3fold reduction of kcat, complementation of bacterial enzyme deficient strain Leishmania donovani
2.4.2.8 Y96F site-directed mutagenesis, dramatic reduction of catalytic activity, no complementation of bacterial enzyme deficient strain, 4-5fold decrease of Km value for 5-phosphoribosyl 1-diphosphate Leishmania donovani
2.4.2.8 Y96V site-directed mutagenesis, dramatic reduction of catalytic activity, no complementation of bacterial enzyme deficient strain, 4-5fold decrease of Km value for 5-phosphoribosyl 1-diphosphate Leishmania donovani

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.2.8 diethyl dicarbonate alkylation of Arg155, complete inactivation at pH 9.0, pH dependent Leishmania donovani
2.4.2.8 additional information no effect of iodoacetate, phenylglyoxal, p-chloromercuribenzoate, acetic anhydride, ethyl dimethylaminopropylcarbodiimide/ammonium acetate, and diisopropyl fluorophosphate Leishmania donovani
2.4.2.8 Tetranitromethane complete inactivation at pH 9.0, pH dependent, modifies Tyr96 in the active site Leishmania donovani

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.2.8 additional information
-
 additional information kinetics Leishmania donovani
2.4.2.8 additional information
-
 additional information Km values of mutant enzymes for hypoxanthine, guanine, diphosphate, 5-phosphoribosyl 1-diphosphate, inosine monophosphate Leishmania donovani
2.4.2.8 0.005
-
 guanine wild-type enzyme Leishmania donovani
2.4.2.8 0.0061
-
 hypoxanthine wild-type enzyme Leishmania donovani
2.4.2.8 0.09
-
 inosine monophosphate wild-type enzyme Leishmania donovani
2.4.2.8 0.103
-
 diphosphate wild-type enzyme Leishmania donovani
2.4.2.8 0.134
-
 5-phospho-alpha-D-ribose 1-diphosphate wild-type enzyme Leishmania donovani

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.2.8 Mg2+
-
 Leishmania donovani

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.2.8 guanine + 5-phospho-alpha-D-ribose 1-diphosphate Leishmania donovani
-
 GMP + diphosphate
-
 ?
2.4.2.8 hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate Leishmania donovani
-
 IMP + diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.8 Leishmania donovani
-
-
-

Purification (Commentary)

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

Reaction

EC Number Reaction Comment Organism Reaction ID
2.4.2.8 IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate essential role of Ser95-Tyr96 dyade in catalysis Leishmania donovani
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.2.8 additional information
-
 kinetics Leishmania donovani

Storage Stability

EC Number Storage Stability Organism
2.4.2.8 -70°C, wild-type enzyme and mutants, except mutant S95C, stable up to 6 months Leishmania donovani

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 donovani GMP + diphosphate
-
 ?
2.4.2.8 guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Leishmania donovani GMP + diphosphate
-
 r
2.4.2.8 hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Leishmania donovani IMP + diphosphate
-
 ?
2.4.2.8 hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Leishmania donovani IMP + diphosphate
-
 r
2.4.2.8 additional information kinetic study Leishmania donovani ?
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.2.8 37
-
 assay at Leishmania donovani

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.4.2.8 8.54
-
 hypoxanthine wild-type enzyme Leishmania donovani
2.4.2.8 36.3
-
 5-phospho-alpha-D-ribose 1-diphosphate wild-type enzyme Leishmania donovani
2.4.2.8 41.3
-
 guanine wild-type enzyme Leishmania donovani
2.4.2.8 77
-
 inosine monophosphate wild-type enzyme Leishmania donovani
2.4.2.8 90
-
 diphosphate wild-type enzyme Leishmania donovani

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.2.8 8
-
 assay at Leishmania donovani