EC Number | Cloned (Comment) | Organism |
---|---|---|
6.3.5.2 | cloning of ATPP/DD (a construct that contains the ATP-pyrophosphatase domain as well as the predicted dimerization domain), expression and purification of the corresponding protein, as both a His-tagged fusion protein (His-ATPP/DD) and as a non-fusion protein (NF-ATPP/DD). Both His-ATPP/DD and NF-ATPP/DD are active proteins, capable of catalyzing the conversion of XMP to GMP using exogenously added ammonia | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.3.5.2 | 0.041 | - |
XMP | 40°C, pH 8.0, NF-ATPP/DD | Escherichia coli | |
6.3.5.2 | 0.09 | - |
NH3 | 40°C, pH 8.0, His-ATPP/DD | Escherichia coli | |
6.3.5.2 | 0.096 | - |
XMP | 40°C, pH 8.0, His-ATPP/DD | Escherichia coli | |
6.3.5.2 | 0.103 | - |
NH3 | 40°C, pH 8.0, wild-type enzyme | Escherichia coli | |
6.3.5.2 | 0.104 | - |
ATP | 40°C, pH 8.0, wild-type enzyme | Escherichia coli | |
6.3.5.2 | 0.127 | - |
NH3 | 40°C, pH 8.0, NF-ATPP/DD | Escherichia coli | |
6.3.5.2 | 0.166 | - |
XMP | 40°C, pH 8.0, wild-type enzyme | Escherichia coli | |
6.3.5.2 | 0.181 | - |
ATP | 40°C, pH 8.0, NF-ATPP/DD | Escherichia coli | |
6.3.5.2 | 0.2 | - |
ATP | 40°C, pH 8.0, His-ATPP/DD | Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.3.5.2 | Escherichia coli | P04079 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.3.5.2 | ATP + xanthosine 5'-phosphate + L-glutamine + H2O | GMP synthetase catalyzes the conversion of XMP to GMP. Ammonia, generated in the amino-terminal glutamine amidotransferase (GAT) domain, is transferred to the ATP-pyrophosphatase (ATPP) domain, where it attacks a highly reactive adenyl-XMP intermediate, leading to GMP formation | Escherichia coli | AMP + diphosphate + GMP + L-glutamate | - |
? | |
6.3.5.2 | ATP + xanthosine 5'-phosphate + NH3 | ATPP/DD (a construct that contains the ATP-pyrophosphatase domain as well as the predicted dimerization domain) expressed as both a His-tagged fusion protein (His-ATPP/DD) and as a non-fusion protein (NF-ATPP/DD) is capable of catalyzing the conversion of XMP to GMP using exogenously added ammonia | Escherichia coli | AMP + diphosphate + GMP | - |
? |