EC Number | Application | Comment | Organism |
---|---|---|---|
2.7.4.8 | medicine | GMPK from bacterial pathogens, in which this enzyme is essential, are potential targets for therapeutic inhibition. | Escherichia coli |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.7.4.8 | vapour diffusion method | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.7.4.8 | Ap5G | Ap5G locks an incompletely closed conformation of the enzyme, in which the adenine moiety is located outside its expected binding site. Instead, it binds at a subunit interface that is unique to the bacterial enzyme, which is in equilibrium between a dimeric and an hexameric form in solution. | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.4.8 | dGMP + ATP | Escherichia coli | GMPKs catalyze the reversible phosphorylation of GMP and dGMP to their diphosphate form in the cell using ATP as a preferred phosphate donor. | dGDP + ADP | - |
r | |
2.7.4.8 | GMP + ATP | Escherichia coli | GMPKs catalyze the reversible phosphorylation of GMP and dGMP to their diphosphate form in the cell using ATP as a preferred phosphate donor. | GDP + ADP | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.4.8 | Escherichia coli | P60546 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.4.8 | dGMP + ATP | GMPKs catalyze the reversible phosphorylation of GMP and dGMP to their diphosphate form in the cell using ATP as a preferred phosphate donor. | Escherichia coli | dGDP + ADP | - |
r | |
2.7.4.8 | GMP + ATP | GMPKs catalyze the reversible phosphorylation of GMP and dGMP to their diphosphate form in the cell using ATP as a preferred phosphate donor. | Escherichia coli | GDP + ADP | - |
r |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.7.4.8 | hexamer | X-ray diffraction data for EcGMPK in complex with GCV-MP were collected at 100 K from a single crystal on beamline ID23-1 (lambda = 0.980 A) at the European Synchrotron Radiation Facility (Grenoble, France), and is indexed and scaled using XDS and XSCALE to a resolution of 3.16 A. Crystals of EcGMPK GCV-MP belong to space group P41212 and are isomorphous to those of apo-EcGMPK, with 6 molecules related by D3 symmetry in the asymmetric unit. Each monomer was first divided in 3 domains corresponding to the LID, CORE and GMP-binding domains (except for subunit F whose GMP-binding domain is not visible in apo-EcGMPK), which were submitted to rigid body refinement. | Escherichia coli |
2.7.4.8 | More | GMPKs share a highly conserved structure comprising a GMP-binding domain, a central CORE domain that carries the ATP beta-phosphate binding loop (P-loop) and a LID domain which binds the adenine base of ATP and provides catalytic residues to the phosphoryl transfer reaction. | Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.7.4.8 | apo-EcGMPK | - |
Escherichia coli |
2.7.4.8 | guanosine monophosphate kinase (EcGMPK) | - |
Escherichia coli |
EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|---|
2.7.4.8 | 0.0005 | - |
The crystal structure of EcGMPK in complex with Ap5G solved at 2.5 Å resolution. | Escherichia coli | Ap5G |