Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.4.2.8 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

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
purified enzyme
-

Reaction

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
Homo sapiens GMP + diphosphate
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
Homo sapiens IMP + diphosphate
-
r
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

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