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Literature summary for 2.4.2.8 extracted from
- Crystal structure of a chimera of human and Plasmodium falciparum hypoxanthine guanine phosphoribosyltransferases provides insights into oligomerization (2008), Proteins, 73, 1010-1020.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overexpression of the chimeric mutant enzyme in Escherichia coli strain Su609 | Homo sapiens |
| overexpression of the chimeric mutant enzyme in Escherichia coli strain Su609 | Plasmodium falciparum |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| 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 |
| 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
| Protein Variants | Comment | Organism |
|---|---|---|
| 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 |
| 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]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0011 | - |
guanine | pH 7.4, 28°C, recombinant chimeric mutant enzyme | Homo sapiens |  |
| 0.0011 | - |
guanine | pH 7.4, 28°C, recombinant chimeric mutant enzyme | Plasmodium falciparum | |
| 0.0018 | - |
hypoxanthine | pH 7.4, 28°C, recombinant chimeric mutant enzyme | Homo sapiens | |
| 0.0018 | - |
hypoxanthine | pH 7.4, 28°C, recombinant chimeric mutant enzyme | Plasmodium falciparum | |
| 0.332 | - |
xanthine | pH 7.4, 28°C, recombinant chimeric mutant enzyme | Homo sapiens | |
| 0.332 | - |
xanthine | pH 7.4, 28°C, recombinant chimeric mutant enzyme | Plasmodium falciparum | |
| 0.546 | - |
5-phospho-alpha-D-ribose 1-diphosphate | pH 7.4, 28°C, recombinant chimeric mutant enzyme with substrate hypoxanthine | Homo sapiens | |
| 0.546 | - |
5-phospho-alpha-D-ribose 1-diphosphate | pH 7.4, 28°C, recombinant chimeric mutant enzyme with substrate hypoxanthine | Plasmodium falciparum | |
| 1.075 | - |
5-phospho-alpha-D-ribose 1-diphosphate | pH 7.4, 28°C, recombinant chimeric mutant enzyme, with substrate guanine | Homo sapiens | |
| 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
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | activates | Homo sapiens | |
| Mg2+ | activates | Plasmodium falciparum | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| guanine + 5-phospho-alpha-D-ribose 1-diphosphate | Homo sapiens | - |
GMP + diphosphate | - |
? | |
| guanine + 5-phospho-alpha-D-ribose 1-diphosphate | Plasmodium falciparum | - |
GMP + diphosphate | - |
? | |
| hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | Homo sapiens | - |
IMP + diphosphate | - |
? | |
| hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | Plasmodium falciparum | - |
IMP + diphosphate | - |
? | |
| xanthine + 5-phospho-alpha-D-ribose 1-diphosphate | Homo sapiens | - |
? + diphosphate | - |
? | |
| xanthine + 5-phospho-alpha-D-ribose 1-diphosphate | Plasmodium falciparum | - |
? + diphosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P00492 | - |
- |
| Plasmodium falciparum | P20035 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant chimeric mutant enzyme from Escherichia coli strain Su609 by anion exchange chromatography | Homo sapiens |
| recombinant chimeric mutant enzyme from Escherichia coli strain Su609 by anion exchange chromatography | Plasmodium falciparum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| guanine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Homo sapiens | GMP + diphosphate | - |
? | |
| guanine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Plasmodium falciparum | GMP + diphosphate | - |
? | |
| 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 | ? | |
| 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 | ? | |
| hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Homo sapiens | IMP + diphosphate | - |
? | |
| hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Plasmodium falciparum | IMP + diphosphate | - |
? | |
| hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | wild-type and chimeric mutant enzyme | Homo sapiens | IMP + diphosphate | - |
? | |
| hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | wild-type and chimeric mutant enzyme | Plasmodium falciparum | IMP + diphosphate | - |
? | |
| xanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Homo sapiens | ? + diphosphate | - |
? | |
| xanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Plasmodium falciparum | ? + diphosphate | - |
? | |
| xanthine + 5-phospho-alpha-D-ribose 1-diphosphate | wild-type and chimeric mutant enzyme | Homo sapiens | ? + diphosphate | - |
? | |
| xanthine + 5-phospho-alpha-D-ribose 1-diphosphate | wild-type and chimeric mutant enzyme | Plasmodium falciparum | ? + diphosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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
| Synonyms | Comment | Organism |
|---|---|---|
| HGPRT | - |
Homo sapiens |
| HGPRT | - |
Plasmodium falciparum |
| hypoxanthine guanine phosphoribosyltransferase | - |
Homo sapiens |
| hypoxanthine guanine phosphoribosyltransferase | - |
Plasmodium falciparum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 28 | - |
assay at | Homo sapiens |
| 28 | - |
assay at | Plasmodium falciparum |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.08 | - |
xanthine | pH 7.4, 28°C, recombinant chimeric mutant enzyme | Homo sapiens | |
| 0.08 | - |
xanthine | pH 7.4, 28°C, recombinant chimeric mutant enzyme | Plasmodium falciparum | |
| 0.37 | - |
guanine | pH 7.4, 28°C, recombinant chimeric mutant enzyme | Homo sapiens | |
| 0.37 | - |
guanine | pH 7.4, 28°C, recombinant chimeric mutant enzyme | Plasmodium falciparum | |
| 0.47 | - |
hypoxanthine | pH 7.4, 28°C, recombinant chimeric mutant enzyme | Homo sapiens | |
| 0.47 | - |
hypoxanthine | pH 7.4, 28°C, recombinant chimeric mutant enzyme | Plasmodium falciparum | |
| 1.13 | - |
hypoxanthine | pH 7.4, 28°C, wild-type enzyme | Homo sapiens | |
| 1.2 | - |
guanine | pH 7.4, 28°C, wild-type enzyme | Homo sapiens | |
| 2.9 | - |
xanthine | pH 7.4, 28°C, wild-type enzyme | Homo sapiens | |
| 7.1 | - |
hypoxanthine | pH 7.4, 28°C, wild-type enzyme | Plasmodium falciparum | |
| 25.5 | - |
guanine | pH 7.4, 28°C, wild-type enzyme | Plasmodium falciparum | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Homo sapiens |
| 7.4 | - |
assay at | Plasmodium falciparum |
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