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Information on EC 2.7.4.8 - guanylate kinase and Organism(s) Escherichia coli and UniProt Accession P60546
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2.7.4.8 guanylate kinaseIUBMB Comments
dGMP can also act as acceptor, and dATP can act as donor.
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Word Map
- 2.7.4.8
- junction
- synapses
- drosophila
- nmda
-
cell-cell
- src
-
excitatory
-
synapse-associated
- hippocampal
-
domain-containing
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magi-1
- adaptor
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spine
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palmitoylated
- n-methyl-d-aspartate
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presynaptic
-
glutamatergic
-
kinase-like
-
adherens
-
pdz-binding
-
zonula
- carma1
-
crumbs
- bcl10
-
neurexins
-
discs-large
- dgmp
-
septate
-
occludens
-
kinase-associated
-
junction-associated
-
tcr-induced
-
ampars
-
shank
-
mucosa-associated
-
card-containing
-
neuroligins
- drug development
- medicine
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
maguk, guanylate kinase, membrane-associated guanylate kinase, maguks, membrane-associated guanylate kinases, guanylate kinase (gk), gmp kinase, membrane associated guanylate kinase, gmpk, cavbeta2a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-GMP kinase
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ATP:GMP phosphotransferase
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-
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deoxyguanylate kinase
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-
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GMP kinase
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guanosine monophosphate kinase
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kinase, guanylate (phosphorylating)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
phospho group transfer
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SYSTEMATIC NAME
IUBMB Comments
ATP:(d)GMP phosphotransferase
dGMP can also act as acceptor, and dATP can act as donor.
CAS REGISTRY NUMBER
COMMENTARY
9026-59-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dGMP + ATP
dGDP + ADP
GMPKs catalyze the reversible phosphorylation of GMP and dGMP to their diphosphate form in the cell using ATP as a preferred phosphate donor.
-
-
r
GMP + ATP
GDP + ADP
GMPKs catalyze the reversible phosphorylation of GMP and dGMP to their diphosphate form in the cell using ATP as a preferred phosphate donor.
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-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dGMP + ATP
dGDP + ADP
GMPKs catalyze the reversible phosphorylation of GMP and dGMP to their diphosphate form in the cell using ATP as a preferred phosphate donor.
-
-
r
GMP + ATP
GDP + ADP
GMPKs catalyze the reversible phosphorylation of GMP and dGMP to their diphosphate form in the cell using ATP as a preferred phosphate donor.
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-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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.
additional information
-
no inhibition of the cytosolic isozyme by guanosine 3',5'-bisdiphosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
guanylate kinase is a key enzyme in guanine nucleotide biosynthesis, purine biosynthetic pathways in plant cells and bacteria, overview. Accumulation of guanosine 3',5'-bisdiphosphate has little effect on the guanine nucleotide profile of Escherichia coli
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23462
x * 23462, thermodynamic analysis, the enzyme is in equilibrium between a dimer and higher order oligomers, whose relative amounts depend on protein concentration, ionic strength, and the presence of ATP
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
oligomer
x * 23462, thermodynamic analysis, the enzyme is in equilibrium between a dimer and higher order oligomers, whose relative amounts depend on protein concentration, ionic strength, and the presence of ATP
additional information
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.
additional information
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.
additional information
-
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.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable in dilute solutions, below 0.005 mg/ml, bovine serum albumin or other suitable proteins protect, highly purified enzyme is stabilized by the presence of lactic dehydrogenase and pyruvate kinase
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for several months after purification by Blue Sepharose and gel filtration
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant ecGMPK is purified by a two-step chromatography procedure involving affinity chromatography on Blue Sepharose and gel filtration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
complete denaturation of the protein is not reversible due to aggregation at the unfolded state
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
GMPK from bacterial pathogens, in which this enzyme is essential, are potential targets for therapeutic inhibition.
drug development
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the guanylate-kinase-deficient Escherichia coli strain relies on the presence of a plasmid-borne, functional guanylate kinase for viability. Such a strain will be beneficial to assess the role of specific amino acids of guanylate kinase in structure, function, drug activation, and drug resistance
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Oeschger, M.
Guanylate kinase from Escherichia coli B
Methods Enzymol.
51
473-482
1978
Escherichia coli, Escherichia coli B / ATCC 11303
Hiraga, S.; Sugino, Y.
Nucleoside monophosphokinases of Escherichia coli infected and uninfected with an RNA phage
Biochim. Biophys. Acta
114
416-418
1966
Escherichia coli, Escherichia coli JE24F+
Stolworthy, T.S.; Krabbenhoft, E.; Black, M.E.
A novel Escherichia coli strain allows functional analysis of guanylate kinase drug resistance and sensitivity
Anal. Biochem.
322
40-47
2003
Escherichia coli, Escherichia coli TS202A
Hible, G.; Renault, L.; Schaeffer, F.; Christova, P.; Zoe Radulescu, A.; Evrin, C.; Gilles, A.M.; Cherfils, J.
Calorimetric and crystallographic analysis of the oligomeric structure of Escherichia coli GMP kinase
J. Mol. Biol.
352
1044-1059
2005
Escherichia coli (P60546), Escherichia coli
Hible, G.; Daalova, P.; Gilles, A.M.; Cherfils, J.
Crystal structures of GMP kinase in complex with ganciclovir monophosphate and Ap5G
Biochimie
88
1157-1164
2006
Escherichia coli (P60546), Escherichia coli
Nomura, Y.; Izumi, A.; Fukunaga, Y.; Kusumi, K.; Iba, K.; Watanabe, S.; Nakahira, Y.; Weber, A.P.; Nozawa, A.; Tozawa, Y.
Diversity in guanosine 3,5-bisdiphosphate (ppGpp) sensitivity among guanylate kinases of bacteria and plants
J. Biol. Chem.
289
15631-15641
2014
Arabidopsis thaliana (Q94JM2), Bacillus subtilis, Escherichia coli, Oryza sativa Japonica Group (Q10M74), Oryza sativa Japonica Group (Q2QPW1), Oryza sativa Japonica Group Nipponbare (Q10M74), Oryza sativa Japonica Group Nipponbare (Q2QPW1), Pisum sativum (W8VNI6), Pisum sativum (W8VZ39), Pisum sativum, Saccharomyces cerevisiae (P15454), Saccharomyces cerevisiae, Synechococcus elongatus, Synechococcus elongatus PCC 7942
EXTERNAL LINKS (specific for EC-Number 2.7.4.8)
Transporter Classification Database (TCDB): 8.A.24.1.8
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