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Literature summary for 2.7.4.8 extracted from

  • Hible, G.; Daalova, P.; Gilles, A.M.; Cherfils, J.
    Crystal structures of GMP kinase in complex with ganciclovir monophosphate and Ap5G (2006), Biochimie, 88, 1157-1164.
    View publication on PubMed

Application

Application Comment Organism
medicine GMPK from bacterial pathogens, in which this enzyme is essential, are potential targets for therapeutic inhibition. Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
vapour diffusion method Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
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

Organism

Organism UniProt Comment Textmining
Escherichia coli P60546
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
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

Subunits

Subunits Comment Organism
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
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

Synonyms

Synonyms Comment Organism
apo-EcGMPK
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Escherichia coli
guanosine monophosphate kinase (EcGMPK)
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Escherichia coli

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.0005
-
The crystal structure of EcGMPK in complex with Ap5G solved at 2.5 Å resolution. Escherichia coli Ap5G