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Literature summary for 2.4.2.8 extracted from

  • Ducati, R.G.; Firestone, R.S.; Schramm, V.L.
    Kinetic isotope effects and transition state structure for hypoxanthine-guanine-xanthine phosphoribosyltransferase from Plasmodium falciparum (2017), Biochemistry, 56, 6368-6376 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.2.8

Cloned(Commentary)

Cloned (Comment) Organism
gene PF3D7_1012400, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21-AI Plasmodium falciparum

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ dependent on Plasmodium falciparum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate Plasmodium falciparum
-
 GMP + diphosphate
-
 r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate Plasmodium falciparum
-
 IMP + diphosphate
-
 r

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum Q8IJS1
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Plasmodium falciparum GMP + diphosphate
-
 r
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate a freely reversible Mg2+-dependent conversion Plasmodium falciparum GMP + diphosphate
-
 r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Plasmodium falciparum IMP + diphosphate
-
 r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate a freely reversible Mg2+-dependent conversion Plasmodium falciparum IMP + diphosphate
-
 r

Subunits

Subunits Comment Organism
More transition state structure of PfHGXPRT, overview Plasmodium falciparum

Synonyms

Synonyms Comment Organism
HGXPRT
-
 Plasmodium falciparum
hypoxanthine-guanine-xanthine phosphoribosyltransferase
-
 Plasmodium falciparum
More cf. EC 2.4.2.22 Plasmodium falciparum
PF3D7_1012400 locus name Plasmodium falciparum

General Information

General Information Comment Organism
additional information determination of primary (1-14C and 9-15N) and secondary (1-3H and 7-15N) intrinsic kinetic isotope effect (KIE) values for PfHGXPRT, mass spectrometry. Intrinsic isotope effects contain information for understanding enzymatic transition state properties. The transition state of PfHGXPRT is explored by matching KIE values predicted from quantum mechanical calculations to the intrinsic values determined experimentally. This approach provides information about PfHGXPRT transition state bond lengths, geometry, and atomic charge distribution. The transition state structure of PfHGXPRT is determined in the physiological direction of addition of ribose 5-phosphate to hypoxanthine by overcoming the chemical instability of PRPP. The transition state for PfHGXPRT forms nucleotides through a well-developed and near-symmetrical DN*AN, SN1-like transition state. Structure comparisons to the human enzyme, overview Plasmodium falciparum
physiological function hypoxanthine is a key precursor salvaged for purine nucleotide synthesis in Plasmodium falciparum, and the most critical enzyme is hypoxanthine-guanine-xanthine phosphoribosyltransferase (HGXPRT) which catalyzes the freely reversible Mg2+-dependent conversion of 6-oxopurine bases to their respective nucleotides and diphosphate. The phosphoribosyl group is derived from 5-phospho-alpha-D-ribosyl 1-diphosphate (PRPP). The enzyme from malaria parasites (PfHGXPRT) is essential as hypoxanthine is the major precursor in purine metabolism Plasmodium falciparum