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Literature summary extracted from

  • Gayathri, P.; Sujay Subbayya, I.; Ashok, C.; Senthamizh Selvi, T.; Balaram, H.; Murthy, M.
    Crystal structure of a chimera of human and Plasmodium falciparum hypoxanthine guanine phosphoribosyltransferases provides insights into oligomerization (2008), Proteins, 73, 1010-1020.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.2.8 overexpression of the chimeric mutant enzyme in Escherichia coli strain Su609 Homo sapiens
2.4.2.8 overexpression of the chimeric mutant enzyme in Escherichia coli strain Su609 Plasmodium falciparum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.2.8 recombinant chimeric mutant enzyme complex with the product GMP, 12 mg/ml protein and 5 mM GMP in 0.1 M Tris, pH 8.0, and 2.0 M ammonium sulfate, 2-5 days, X-ray diffraction structure determination and analysis at 2.8 A resolution, modeling Homo sapiens
2.4.2.8 recombinant chimeric mutant enzyme complex with the product GMP, 12 mg/ml protein and 5 mM GMP in 0.1 M Tris, pH 8.0, and 2.0 M ammonium sulfate, 2-5 days, X-ray diffraction structure determination and analysis at 2.8 A resolution, modeling Plasmodium falciparum

Protein Variants

EC Number Protein Variants Comment Organism
2.4.2.8 additional information construction of a chimera of Plasmodium falciparum and human HGPRTs, which consists of the core of the protein from the human enzyme and the hood region from the parasite enzyme. Replacement of Tyr197 of human HGPRT by Ile207 in the chimera disrupts the interaction at the AB interface in the absence of PRPP. In the presence of PRPP, the interaction between Pro93 and His26 can restore the AB interface, shifting the chimeric enzyme to a tetrameric state, active site structure, overview Homo sapiens
2.4.2.8 additional information construction of a chimera of Plasmodium falciparum and human HGPRTs, which consists of the core of the protein from the human enzyme and the hood region from the parasite enzyme. Replacement of Tyr197 of human HGPRT by Ile207 in the chimera disrupts the interaction at the AB interface in the absence of PRPP. In the presence of PRPP, the interaction between Pro93 and His26 can restore the AB interface, shifting the chimeric enzyme to a tetrameric state, active site structure, overview Plasmodium falciparum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.2.8 0.0011
-
 guanine pH 7.4, 28°C, recombinant chimeric mutant enzyme Homo sapiens
2.4.2.8 0.0011
-
 guanine pH 7.4, 28°C, recombinant chimeric mutant enzyme Plasmodium falciparum
2.4.2.8 0.0018
-
 hypoxanthine pH 7.4, 28°C, recombinant chimeric mutant enzyme Homo sapiens
2.4.2.8 0.0018
-
 hypoxanthine pH 7.4, 28°C, recombinant chimeric mutant enzyme Plasmodium falciparum
2.4.2.8 0.332
-
 xanthine pH 7.4, 28°C, recombinant chimeric mutant enzyme Homo sapiens
2.4.2.8 0.332
-
 xanthine pH 7.4, 28°C, recombinant chimeric mutant enzyme Plasmodium falciparum
2.4.2.8 0.546
-
 5-phospho-alpha-D-ribose 1-diphosphate pH 7.4, 28°C, recombinant chimeric mutant enzyme with substrate hypoxanthine Homo sapiens
2.4.2.8 0.546
-
 5-phospho-alpha-D-ribose 1-diphosphate pH 7.4, 28°C, recombinant chimeric mutant enzyme with substrate hypoxanthine Plasmodium falciparum
2.4.2.8 1.075
-
 5-phospho-alpha-D-ribose 1-diphosphate pH 7.4, 28°C, recombinant chimeric mutant enzyme, with substrate guanine Homo sapiens
2.4.2.8 1.075
-
 5-phospho-alpha-D-ribose 1-diphosphate pH 7.4, 28°C, recombinant chimeric mutant enzyme, with substrate guanine Plasmodium falciparum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.2.8 Mg2+ activates Homo sapiens
2.4.2.8 Mg2+ activates Plasmodium falciparum

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 Homo sapiens
-
 GMP + diphosphate
-
 ?
2.4.2.8 guanine + 5-phospho-alpha-D-ribose 1-diphosphate Plasmodium falciparum
-
 GMP + diphosphate
-
 ?
2.4.2.8 hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate Homo sapiens
-
 IMP + diphosphate
-
 ?
2.4.2.8 hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate Plasmodium falciparum
-
 IMP + diphosphate
-
 ?
2.4.2.8 xanthine + 5-phospho-alpha-D-ribose 1-diphosphate Homo sapiens
-
 ? + diphosphate
-
 ?
2.4.2.8 xanthine + 5-phospho-alpha-D-ribose 1-diphosphate Plasmodium falciparum
-
 ? + diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.8 Homo sapiens P00492
-
-
2.4.2.8 Plasmodium falciparum P20035
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.2.8 recombinant chimeric mutant enzyme from Escherichia coli strain Su609 by anion exchange chromatography Homo sapiens
2.4.2.8 recombinant chimeric mutant enzyme from Escherichia coli strain Su609 by anion exchange chromatography Plasmodium falciparum

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
-
 Homo sapiens GMP + diphosphate
-
 ?
2.4.2.8 guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Plasmodium falciparum GMP + diphosphate
-
 ?
2.4.2.8 guanine + 5-phospho-alpha-D-ribose 1-diphosphate wild-type and chimeric mutant enzyme Homo sapiens GMP + diphosphate modeling of GMP binding to the chimeric enzyme ?
2.4.2.8 guanine + 5-phospho-alpha-D-ribose 1-diphosphate wild-type and chimeric mutant enzyme Plasmodium falciparum GMP + diphosphate modeling of GMP binding to the chimeric enzyme ?
2.4.2.8 hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Homo sapiens IMP + diphosphate
-
 ?
2.4.2.8 hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Plasmodium falciparum IMP + diphosphate
-
 ?
2.4.2.8 hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate wild-type and chimeric mutant enzyme Homo sapiens IMP + diphosphate
-
 ?
2.4.2.8 hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate wild-type and chimeric mutant enzyme Plasmodium falciparum IMP + diphosphate
-
 ?
2.4.2.8 xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Homo sapiens ? + diphosphate
-
 ?
2.4.2.8 xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Plasmodium falciparum ? + diphosphate
-
 ?
2.4.2.8 xanthine + 5-phospho-alpha-D-ribose 1-diphosphate wild-type and chimeric mutant enzyme Homo sapiens ? + diphosphate
-
 ?
2.4.2.8 xanthine + 5-phospho-alpha-D-ribose 1-diphosphate wild-type and chimeric mutant enzyme Plasmodium falciparum ? + diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.2.8 monomer or dimer the recombinant chimeric enzyme exists as a mixture of monomeric and dimeric protein in solution, but shifts to a tetramer on addition of phosphoribosyl diphosphate Homo sapiens
2.4.2.8 monomer or dimer the recombinant chimeric enzyme exists as a mixture of monomeric and dimeric protein in solution, but shifts to a tetramer on addition of phosphoribosyl diphosphate Plasmodium falciparum
2.4.2.8 More Pro93 and Tyr197 form part of crucial interactions holding together the AB interface in the unliganded or GMP-bound forms of HGPRT, while Pro93 and His26 interact at the interface after binding of phosphoribosyl diphosphate Homo sapiens
2.4.2.8 More Pro93 and Tyr197 form part of crucial interactions holding together the AB interface in the unliganded or GMP-bound forms of HGPRT, while Pro93 and His26 interact at the interface after binding of phosphoribosyl diphosphate Plasmodium falciparum
2.4.2.8 tetramer the recombinant chimeric enzyme exists as a mixture of monomeric and dimeric protein in solution, but shifts to a tetramer on addition of phosphoribosyl diphosphate Homo sapiens
2.4.2.8 tetramer the recombinant chimeric enzyme exists as a mixture of monomeric and dimeric protein in solution, but shifts to a tetramer on addition of phosphoribosyl diphosphate Plasmodium falciparum

Synonyms

EC Number Synonyms Comment Organism
2.4.2.8 HGPRT
-
 Homo sapiens
2.4.2.8 HGPRT
-
 Plasmodium falciparum
2.4.2.8 hypoxanthine guanine phosphoribosyltransferase
-
 Homo sapiens
2.4.2.8 hypoxanthine guanine phosphoribosyltransferase
-
 Plasmodium falciparum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.2.8 28
-
 assay at Homo sapiens
2.4.2.8 28
-
 assay at Plasmodium falciparum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.4.2.8 0.08
-
 xanthine pH 7.4, 28°C, recombinant chimeric mutant enzyme Homo sapiens
2.4.2.8 0.08
-
 xanthine pH 7.4, 28°C, recombinant chimeric mutant enzyme Plasmodium falciparum
2.4.2.8 0.37
-
 guanine pH 7.4, 28°C, recombinant chimeric mutant enzyme Homo sapiens
2.4.2.8 0.37
-
 guanine pH 7.4, 28°C, recombinant chimeric mutant enzyme Plasmodium falciparum
2.4.2.8 0.47
-
 hypoxanthine pH 7.4, 28°C, recombinant chimeric mutant enzyme Homo sapiens
2.4.2.8 0.47
-
 hypoxanthine pH 7.4, 28°C, recombinant chimeric mutant enzyme Plasmodium falciparum
2.4.2.8 1.13
-
 hypoxanthine pH 7.4, 28°C, wild-type enzyme Homo sapiens
2.4.2.8 1.2
-
 guanine pH 7.4, 28°C, wild-type enzyme Homo sapiens
2.4.2.8 2.9
-
 xanthine pH 7.4, 28°C, wild-type enzyme Homo sapiens
2.4.2.8 7.1
-
 hypoxanthine pH 7.4, 28°C, wild-type enzyme Plasmodium falciparum
2.4.2.8 25.5
-
 guanine pH 7.4, 28°C, wild-type enzyme Plasmodium falciparum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.2.8 7.4
-
 assay at Homo sapiens
2.4.2.8 7.4
-
 assay at Plasmodium falciparum