EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.4.2.8 | K68A | conformational changes, shifted catalytic loop closer to the active site | Homo sapiens |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.4.2.8 | Mg2+ | - |
Homo sapiens |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.4.2.8 | Homo sapiens | - |
purified enzyme | - |
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 | |
2.4.2.8 | IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate | residues I99-L121 form the catalytic loop | Homo sapiens |
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 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.4.2.8 | More | stereoview of the three-dimensional structure of subunit, subunit interaction | Homo sapiens |