Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Plasmodium falciparum |
expression in Escherichia coli | Homo sapiens |
Crystallization (Comment) | Organism |
---|---|
ultraviolet resonance Raman spectroscopy study on the complexes of enzyme with products IMP, GMP, and XMP, both in Homo sapiens and Plasmodium falciparum, in resonance with the purine nucleobase electronic absorption. Human hypoxanthine guanine phosphoribosyltransferase catalyzes the phosphoribosylation of guanine and hypoxanthine, while the Plasmodium falciparum enzyme acts on xanthine as well. Spectra of bound nucleotides show that the enzyme distorts the structure of the nucleotides. The distorted structure resembles that of the deprotonated nucleotide. The two proteins assemble similar active sites for their common substrates. While the human enzyme does not bind XMP, Plasmodium falciparum hypoxanthine guanine phosphoribosyltransferase perturbs the pKa of bound XMP | Plasmodium falciparum |
ultraviolet resonance Raman spectroscopy study on the complexes of enzyme with products IMP, GMP, and XMP, both in Homo sapiens and Plasmodium falciparum, in resonance with the purine nucleobase electronic absorption. Human hypoxanthine guanine phosphoribosyltransferase catalyzes the phosphoribosylation of guanine and hypoxanthine, while the Plasmodium falciparum enzyme acts on xanthine as well. Spectra of bound nucleotides show that the enzyme distorts the structure of the nucleotides. The distorted structure resembles that of the deprotonated nucleotide. The two proteins assemble similar active sites for their common substrates. While the human enzyme does not bind XMP, Plasmodium falciparum hypoxanthine guanine phosphoribosyltransferase perturbs the pKa of bound XMP | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
F36L | wild-type human enzyme does not accept xanthine as substrate, mutant F36L does catalyze the conversion of xanthine to XMP with a kcat much lower than those of hypoxanthine and guanine and fails to perturb the pKa of XMP | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P00492 | - |
- |
Plasmodium falciparum | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
guanine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Plasmodium falciparum | GMP + diphosphate | - |
? | |
guanine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Homo sapiens | GMP + diphosphate | - |
? | |
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Plasmodium falciparum | IMP + diphosphate | - |
? | |
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Homo sapiens | IMP + diphosphate | - |
? | |
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Plasmodium falciparum | XMP + diphosphate | - |
? | |
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate | wild-type human enzyme does not accept xanthine as substrate, mutant F36L does catalyze the conversion of xanthine to XMP with a kcat much lower than those of hypoxanthine and guanine | Homo sapiens | XMP + diphosphate | - |
? |