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Literature summary for 2.4.2.8 extracted from

  • Gogia, S.; Balaram, H.; Puranik, M.
    Hypoxanthine guanine phosphoribosyltransferase distorts the purine ring of nucleotide substrates and perturbs the pKa of bound xanthosine monophosphate (2011), Biochemistry, 50, 4184-4193.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Plasmodium falciparum
expression in Escherichia coli Homo sapiens

Crystallization (Commentary)

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

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

Organism UniProt Comment Textmining
Homo sapiens P00492
-
-
Plasmodium falciparum
-
-
-

Substrates and Products (Substrate)

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
-
?