Crystallization (Comment) | Organism |
---|---|
structures of the apoenzyme and of ligand-bound enzyme in the presence of 8-oxo-GTP or 8-oxo-dGTP. The molecules arrange themselves in a head-to-tail fashion in which domain 1 is brought into contact with domain 2 of a neighbouring molecule. The binding site for NTP (site A) is almost exclusively made up of residues from domain 1, while those for NDP (site B) and NMP (site C) are at the interface between domain 1 and neighbour domain 2 | Mycolicibacterium smegmatis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Mycolicibacterium smegmatis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycolicibacterium smegmatis | A0QUZ2 | - |
- |
Mycolicibacterium smegmatis ATCC 700084 | A0QUZ2 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
8-oxo-dGTP + H2O | - |
Mycolicibacterium smegmatis | 8-oxo-dGDP + phosphate | - |
? | |
8-oxo-dGTP + H2O | - |
Mycolicibacterium smegmatis ATCC 700084 | 8-oxo-dGDP + phosphate | - |
? | |
8-oxo-GTP + H2O | - |
Mycolicibacterium smegmatis | 8-oxo-GDP + phosphate | - |
? | |
8-oxo-GTP + H2O | - |
Mycolicibacterium smegmatis ATCC 700084 | 8-oxo-GDP + phosphate | - |
? | |
additional information | under high concentrations and over long periods, the full-length enzyme as well as domain 1 catalyses the hydrolysis of the nucleoside triphosphates to the respective nucleoside monophosphates and pyrophosphate. No substrates: GTP, dGTP | Mycolicibacterium smegmatis | ? | - |
? | |
additional information | under high concentrations and over long periods, the full-length enzyme as well as domain 1 catalyses the hydrolysis of the nucleoside triphosphates to the respective nucleoside monophosphates and pyrophosphate. No substrates: GTP, dGTP | Mycolicibacterium smegmatis ATCC 700084 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
MSMEG_2390 | - |
Mycolicibacterium smegmatis |
General Information | Comment | Organism |
---|---|---|
physiological function | enzyme is made up of a Nudix domain (domain1) and a histidine phosphatase domain (domain 2). Domain 1 alone hydrolyses nucleoside triphosphates less efficiently | Mycolicibacterium smegmatis |