Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | all substrates of PH-ATPPase, Mg2+, ATP and XMP, except for ammonia, are required to stabilize the active complex of PH-ATPPase and PH-GATase subunits | Pyrococcus horikoshii |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Pyrococcus horikoshii |
genes ph1346 and ph1347, genetic structure of GMPS, overview. Expressionin Escherichia coli strain BL21(DE3) | Pyrococcus horikoshii |
Crystallization (Comment) | Organism |
---|---|
ATPPase subunit of the two-subunit-type GMPS, sitting drop vapor diffusion at 5°C, mixing of 0.001 ml of protein solution containing 30 mg/ml protein in Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution containing 30% v/v PEG 400, 100 mM Tris-HCl, pH 8.4, and 200 mM MgCl2, equilibration against 0.1 ml of reservoir solution, 3 weeks, X-ray diffraction structure determination and analysis at 1.8 A resolution | Pyrococcus horikoshii |
crystal structure of the ATPPase subunit of the two-subunit-type GMPS, to 1.79 A resolution. ATPPase consists of a N-domain and a C-domain and exists as a homodimer in the crystal and in solution. The N-domain contains an ATP-binding platform called P-loop, whereas the C-domain contains the xanthosine 5'-monophosphate-binding site and also contributes to homodimerization. The glutamine amidotransferase subunit of the two-subunit-type GMPS alone is inactive, and substrates Mg2+, ATP and XMP of PH-ATPPase except for ammonia are required to stabilize the active complex of ATPPase and GATase subunits | Pyrococcus horikoshii |
General Stability | Organism |
---|---|
all substrates of PH-ATPPase, Mg2+, ATP and XMP, except for ammonia, are required to stabilize the active complex of PH-ATPPase and PH-GATase subunits | Pyrococcus horikoshii |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | as Mg-ATP | Pyrococcus horikoshii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus horikoshii | O59071 | GMP synthase [glutamine-hydrolyzing] subunit A | - |
Pyrococcus horikoshii | O59072 | strain OT3 | - |
Pyrococcus horikoshii | O59072 | GMP synthase [glutamine-hydrolyzing] subunit B | - |
Pyrococcus horikoshii OT-3 | O59071 | GMP synthase [glutamine-hydrolyzing] subunit A | - |
Pyrococcus horikoshii OT-3 | O59072 | strain OT3 | - |
Pyrococcus horikoshii OT-3 | O59072 | GMP synthase [glutamine-hydrolyzing] subunit B | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + xanthosine 5'-phosphate + NH3 | overall reaction | Pyrococcus horikoshii | AMP + diphosphate + GMP | - |
? | |
ATP + xanthosine 5'-phosphate + NH3 | overall reaction | Pyrococcus horikoshii OT-3 | AMP + diphosphate + GMP | - |
? | |
L-glutamine + H2O | GATase half-reaction, structure-activity relationship of the functional subunits, overview | Pyrococcus horikoshii | L-glutamate + NH3 | - |
? | |
L-glutamine + H2O | GATase half-reaction, structure-activity relationship of the functional subunits, overview | Pyrococcus horikoshii OT-3 | L-glutamate + NH3 | - |
? | |
additional information | GMPS consists of two functional units that are present as domains or subunits: glutamine amidotransferase, GATase, and ATP pyrophosphatase, ATPPase. GATase hydrolyzes glutamine to yield glutamate and ammonia, while ATPPase utilizes ammonia to convert adenyl-XMP into guanosine 5'-monophosphate. The GATase subunit of the two-subunit-type GMPS alone is inactiv | Pyrococcus horikoshii | ? | - |
? | |
additional information | GMPS consists of two functional units that are present as domains or subunits: glutamine amidotransferase, GATase, and ATP pyrophosphatase, ATPPase. GATase hydrolyzes glutamine to yield glutamate and ammonia, while ATPPase utilizes ammonia to convert adenyl-XMP into guanosine 5'-monophosphate. The GATase subunit of the two-subunit-type GMPS alone is inactiv | Pyrococcus horikoshii OT-3 | ? | - |
? | |
XMP + Mg-ATP2- | ATPPase half-reaction, structure-activity relationship of the functional subunits, overview | Pyrococcus horikoshii | adenyl-XMP + diphosphate + Mg2+ | adenyl-XMP is the overall reaction intermediate | ? | |
XMP + Mg-ATP2- | ATPPase half-reaction, structure-activity relationship of the functional subunits, overview | Pyrococcus horikoshii OT-3 | adenyl-XMP + diphosphate + Mg2+ | adenyl-XMP is the overall reaction intermediate | ? |
Subunits | Comment | Organism |
---|---|---|
dimer | GMPS consists of two functional units that are present as domains or subunits: glutamine amidotransferase, GATase, and 34 kDa ATP pyrophosphatase, ATPPase. Domain structure and interactions, structure-activity relationship of the functional subunits, overview | Pyrococcus horikoshii |
More | the glutamine amidotransferase GATase subunit of the two-subunit-type GMPS alone is inactive, and substrates Mg2+, ATP and XMP of subunit ATP diphosphatase ATPPase except for ammonia are required to stabilize the active complex of ATPPase and GATase subunits | Pyrococcus horikoshii |
Synonyms | Comment | Organism |
---|---|---|
GATase | GMP synthase [glutamine-hydrolyzing] subunit A, glutamine amidotransferase activity | Pyrococcus horikoshii |
GMP synthase [glutamine-hydrolyzing] subunit B | ATPPase, ATP diphosphatase activity | Pyrococcus horikoshii |
GMPS | - |
Pyrococcus horikoshii |
Guanosine 5'-monophosphate synthetase | - |
Pyrococcus horikoshii |
More | GMPS belongs to the class I glutamine amidotransferase, GATase, family | Pyrococcus horikoshii |
two-subunit-type GMP synthetase | - |
Pyrococcus horikoshii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
assay at | Pyrococcus horikoshii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Pyrococcus horikoshii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | as Mg-ATP | Pyrococcus horikoshii |
General Information | Comment | Organism |
---|---|---|
metabolism | GMPS catalyzes the final step of the de novo synthetic pathway of purine nucleotides | Pyrococcus horikoshii |