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Literature summary extracted from

  • Wang, F.; Shi, W.; Nieves, E.; Angeletti, R.H.; Schramm, V.L.; Grubmeyer, C.
    A transition-state analogue reduces protein dynamics in hypoxanthine-guanine phosphoribosyltransferase (2001), Biochemistry, 40, 8043-8054.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.4.2.8 K68A conformational changes, shifted catalytic loop closer to the active site Homo sapiens

Metals/Ions

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

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
2.4.2.8 IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate catalytic mechanism Homo sapiens
a
2.4.2.8 IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate residues I99-L121 form the catalytic loop Homo sapiens
a

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 dynamic and conformational properties of purified enzyme alone, in complex with GMP and Mg2+, and in equilibration mixture of enzyme with IMP, Mg2+/diphosphate and hypoxanthine, Mg2+/5-phosphoribosyl 1-diphosphate, and in transition-state analogue complex of enzyme, immucillin-GP and Mg2+/diphosphate Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.2.8 More stereoview of the three-dimensional structure of subunit, subunit interaction Homo sapiens