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Literature summary extracted from

  • Keough, D.T.; Brereton, I.M.; de Jersey, J.; Guddat, L.W.
    The crystal structure of free human hypoxanthine-guanine phosphoribosyltransferase reveals extensive conformational plasticity throughout the catalytic cycle (2005), J. Mol. Biol., 351, 170-181.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.2.8 purified recombinant mutant C22A/C105A/C205A enzyme 1. free or 2. in complex with inactive purine base analogue 7-hydroxy [4,3d] pyrazolo pyrimidine and 5-phospho-alpha-D-ribose 1-diphosphate, or 3. complexed with IMP or GMP, or 4. complexed with transition state analogue immuncillinHP-Mg2+-diphosphate, hanging drop vapour diffusion method, 18 mg/ml protein in 0.05 M Tris-HCl, pH 7.4, 1 mM MgCl2, 1 mM DTT, mixing of 0.002 ml of both protein and reservoir solution, the latter containing 0.2 M ammonium acetate, 0.1 m sodium acetate, pH 4.6, 30% w/v PEG 4000, 17°C, 2-7 days, cryoprotection by 30% glycerol in reservoir solution, X-ray diffraction structure determination and analysis at 1.9 A resolution Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.4.2.8 C22A/C105A/C205A site-directed mutagenesis, kinetic and physical properties are similar to the wild-type enzyme, but the mutant enzyme is more resistant to oxidation Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.2.8 Mg2+ required Homo sapiens

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
-
 r
2.4.2.8 hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate Homo sapiens
-
 IMP + diphosphate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.8 Homo sapiens
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.4.2.8 IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate sequential mechanism with 5-phospho-alpha-D-ribose 1-diphosphate binding first, active site helix comprising D137-D153 with key active site residues K68, D137, and K165, substrate binding sites and structures, overview Homo sapiens
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.2.8 erythrocyte
-
 Homo sapiens
-

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
-
 r
2.4.2.8 hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Homo sapiens IMP + diphosphate
-
 r
2.4.2.8 additional information substrate binding induces conformational changes required for catalysis Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.2.8 tetramer
-
 Homo sapiens

Synonyms

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