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aciclovir (ACV-MP)
?
-
-
-
-
?
ATP + (R)-3-((2-amino-1,6-dihydro-6-oxo-9H-purin-9-yl)methoxy)-4-hydroxybutylphosphonic acid
(R)-ganciclovir phosphonate monophosphate
ATP + (R)-ganciclovir phosphonate
?
-
-
-
-
?
ATP + 6-thioguanosine 5'-monophosphate
ADP + 8-thioguanosine 5'-diphosphate
ATP + 8-azaguanosine 5'-monophosphate
ADP + 8-azaguanosine 5'-diphosphate
ATP + 8-bromoguanosine 5'-monophosphate
ADP + 8-bromoguanosine 5'-diphosphate
-
poor substrate
-
-
?
ATP + 9-(1,3-dihydroxy-2-propoxymethyl)guanine 5'-monophosphate
ADP + 9-(1,3-dihydroxy-2-propoxymethyl)guanine 5'-diphosphate
-
no substrate: 9-(5,5-difluoro-5-phosphonopentyl)guanine 5'-monophosphate
-
-
?
ATP + 9-(2-hydroxyethoxymethyl)guanine 5'-monophosphate
ADP + 9-(2-hydroxyethoxymethyl)guanine 5'-diphosphate
-
i.e. acyclovir 5'-monophosphate
-
-
?
ATP + 9-(5-phosphonopentyl)guanine
?
-
9-(5,5'-difluoro-5-phosphonopenthyl)guanine is not a substrate
-
-
?
ATP + AMP
2 ADP
-
-
-
-
?
ATP + AMP
ADP + ADP
-
very low activity with AMP
-
-
?
ATP + ganciclovir
ADP + ganciclovir phosphate
-
-
-
-
?
ATP + ganciclovir monophosphate
?
-
-
-
-
?
ATP + ganciclovir monophosphate
ADP + ganciclovir-diphosphate
-
-
-
-
?
ATP + IMP
ADP + IDP
-
very poor substrate
-
-
?
GDP + GDP
GTP + GMP
-
-
?
GMP + MgATP2-
MgADP- + GDP
GTP + dAMP
GDP + dADP
-
-
-
r
GTP + GDP
GMP + guanosine 5'-tetraphosphate
-
-
?
guanosine monophosphate + adenosine triphosphate
guanosine diphosphate + adenosine diphosphate
additional information
?
-
ATP + (R)-3-((2-amino-1,6-dihydro-6-oxo-9H-purin-9-yl)methoxy)-4-hydroxybutylphosphonic acid
(R)-ganciclovir phosphonate monophosphate
-
i.e. R-ganciclovir phosphonate, (S) enantiomer 100fold less efficient, used for racemic resolution
-
?
ATP + (R)-3-((2-amino-1,6-dihydro-6-oxo-9H-purin-9-yl)methoxy)-4-hydroxybutylphosphonic acid
(R)-ganciclovir phosphonate monophosphate
-
i.e. R-ganciclovir phosphonate, (S) enantiomer 100fold less efficient, used for racemic resolution
-
?
ATP + 6-thioguanosine 5'-monophosphate
ADP + 8-thioguanosine 5'-diphosphate
-
-
-
-
?
ATP + 6-thioguanosine 5'-monophosphate
ADP + 8-thioguanosine 5'-diphosphate
-
-
-
-
?
ATP + 6-thioguanosine 5'-monophosphate
ADP + 8-thioguanosine 5'-diphosphate
-
not thiodeoxyguanosine derivative
-
-
?
ATP + 6-thioguanosine 5'-monophosphate
ADP + 8-thioguanosine 5'-diphosphate
-
-
-
-
?
ATP + 8-azaguanosine 5'-monophosphate
ADP + 8-azaguanosine 5'-diphosphate
-
-
-
-
?
ATP + 8-azaguanosine 5'-monophosphate
ADP + 8-azaguanosine 5'-diphosphate
-
-
-
-
?
ATP + 8-azaguanosine 5'-monophosphate
ADP + 8-azaguanosine 5'-diphosphate
-
-
-
-
?
ATP + dGMP
ADP + dGDP
-
-
-
-
r
ATP + dGMP
ADP + dGDP
-
phosphorylation at 48% the rate of GMP
-
r
ATP + dGMP
ADP + dGDP
-
-
-
r
ATP + dGMP
ADP + dGDP
-
-
-
r
ATP + dGMP
ADP + dGDP
-
-
-
-
r
ATP + dGMP
ADP + dGDP
-
-
-
r
ATP + dGMP
ADP + dGDP
-
-
-
r
ATP + dGMP
ADP + dGDP
-
-
-
-
r
ATP + dGMP
ADP + dGDP
-
-
-
-
r
ATP + dGMP
ADP + dGDP
-
-
-
-
?
ATP + dGMP
ADP + dGDP
-
-
-
-
r
ATP + dGMP
ADP + dGDP
-
-
-
-
?
ATP + dGMP
ADP + dGDP
-
low activity, dGMP acts also as inhibitor
-
-
?
ATP + dGMP
ADP + dGDP
-
dGMP is a poor substrate, the Kcat for dGMP is about 22fold lower than that observed for GMP. The value of kcat/Km for dGMP is at least 70fold lower than that of GMP
-
-
?
ATP + dGMP
ADP + dGDP
-
-
-
-
r
ATP + dGMP
ADP + dGDP
-
-
-
-
r
ATP + dGMP
ADP + dGDP
-
-
-
-
r
ATP + GDP
ADP + GTP
-
-
-
-
?
ATP + GDP
ADP + GTP
-
-
?
ATP + GMP
ADP + GDP
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
specificity
-
-
?, r
ATP + GMP
ADP + GDP
-
best substrates
-
?
ATP + GMP
ADP + GDP
-
no donor substrates are ITP, dGTP, dCTP or dTTP
-
-
?, r
ATP + GMP
ADP + GDP
-
dCMP is no acceptor substrate
-
-
?, r
ATP + GMP
ADP + GDP
-
dTMP is no acceptor substrate
-
-
?, r
ATP + GMP
ADP + GDP
-
AMP is no acceptor substrate
-
?
ATP + GMP
ADP + GDP
-
AMP is no acceptor substrate
-
-
?, r
ATP + GMP
ADP + GDP
-
dAMP is no acceptor substrate
-
?
ATP + GMP
ADP + GDP
-
dAMP is no acceptor substrate
-
-
?, r
ATP + GMP
ADP + GDP
-
no donor substrates are GTP, CTP, UTP
-
?
ATP + GMP
ADP + GDP
-
no donor substrates are GTP, CTP, UTP
-
-
?, r
ATP + GMP
ADP + GDP
-
CMP, UMP are no acceptor substrates
-
?
ATP + GMP
ADP + GDP
-
CMP, UMP are no acceptor substrates
-
-
?, r
ATP + GMP
ADP + GDP
-
first step in 'cGMP-cycle' toward re-synthesis of cGMP
-
-
?
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
r
ATP + GMP
ADP + GDP
GMP and ATP served as the most effective phosphate acceptor and donor, respectively
-
-
r
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
r
ATP + GMP
ADP + GDP
-
specificity
-
?
ATP + GMP
ADP + GDP
-
signal transduction
-
-
?
ATP + GMP
ADP + GDP
-
specificity
-
?
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
signal transduction
-
-
?
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
specificity
-
-
?
ATP + GMP
ADP + GDP
-
nucleoside monophosphate binding site is highly specific for guanine moiety
-
-
?
ATP + GMP
ADP + GDP
-
deoxyguanosine, guanosine are no acceptor substrates
-
-
?
ATP + GMP
ADP + GDP
-
6-thio-IMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
XMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
AMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
CMP, UMP are no acceptor substrates
-
-
?
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
specificity
-
-
?
ATP + GMP
ADP + GDP
-
AMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
dAMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
guanylate kinase is an essential enzyme
-
-
?
ATP + GMP
ADP + GDP
upon substrate binding, the LID and nucleotide-monophosphate-binding domains are brought together and toward the CORE with large concerted movements about the alpha3, helix 3, axis
-
-
?
ATP + GMP
ADP + GDP
guanylate kinase is an essential enzyme
-
-
?
ATP + GMP
ADP + GDP
upon substrate binding, the LID and nucleotide-monophosphate-binding domains are brought together and toward the CORE with large concerted movements about the alpha3, helix 3, axis
-
-
?
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
specificity
-
-
?
ATP + GMP
ADP + GDP
-
nucleoside monophosphate binding site is highly specific for guanine moiety
-
-
?
ATP + GMP
ADP + GDP
-
deoxyguanosine, guanosine are no acceptor substrates
-
-
?
ATP + GMP
ADP + GDP
-
TMP is not an acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
dCMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
IMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
6-thio-IMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
XMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
AMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
dAMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
CMP, UMP are no acceptor substrates
-
-
?
ATP + GMP
ADP + GDP
-
regulation of cellular adhesion and signal transduction at sites of cell-cell contact
-
-
?
ATP + GMP
ADP + GDP
-
CASK construct has no activity
-
-
?
ATP + GMP
ADP + GDP
-
PSD-95 construct has no activity
-
-
?
ATP + GMP
ADP + GDP
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
r
ATP + GMP
ADP + GDP
-
-
-
?
ATP + GMP
ADP + GDP
-
best substrates
-
-
?
ATP + GMP
ADP + GDP
-
best substrates
-
?
ATP + GMP
ADP + GDP
-
IMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
XMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
AMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
AMP is no acceptor substrate
-
?
ATP + GMP
ADP + GDP
GMP binding induces conformational changes in non-acetylated N-terminus mutants
-
-
?
ATP + GMP
ADP + GDP
-
two specific binding sites: ATP- and GMP-binding site
-
-
?
ATP + GMP
ADP + GDP
-
CMP, UMP are no acceptor substrates
-
-
?
ATP + GMP
ADP + GDP
-
regulation of cellular adhesion and signal transduction at sites of cell-cell contact
-
-
?
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
specificity
-
-
?
ATP + GMP
ADP + GDP
-
nucleoside monophosphate binding site is highly specific for guanine moiety
-
-
?
ATP + GMP
ADP + GDP
-
deoxyguanosine, guanosine are no acceptor substrates
-
-
?
ATP + GMP
ADP + GDP
-
6-thio-IMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
XMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
AMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
CMP, UMP are no acceptor substrates
-
-
?
ATP + GMP
ADP + GDP
-
key enzyme of biosynthetic pathway of GTP or dGTP
-
r
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
-
?
dATP + dGMP
dADP + dGDP
-
as good as ATP
-
-
?
dATP + dGMP
dADP + dGDP
-
phosphorylation at 22% the rate of ATP
-
?
dATP + dGMP
dADP + dGDP
-
-
-
?
dATP + dGMP
dADP + dGDP
-
-
-
?
dATP + dGMP
dADP + dGDP
-
-
-
-
?
dATP + dGMP
dADP + dGDP
-
-
-
-
?
dATP + dGMP
dADP + dGDP
-
-
-
-
?
dATP + dGMP
dADP + dGDP
-
-
-
-
?
dATP + dGMP
dADP + dGDP
-
-
-
-
?
dATP + GMP
dADP + GDP
-
as good as ATP
-
-
?
dATP + GMP
dADP + GDP
-
phosphorylation at 81% the rate of ATP
-
?
dATP + GMP
dADP + GDP
-
-
-
r
dATP + GMP
dADP + GDP
-
-
-
?
dATP + GMP
dADP + GDP
-
-
-
?
dATP + GMP
dADP + GDP
-
-
-
-
?
dATP + GMP
dADP + GDP
-
-
-
-
?
dATP + GMP
dADP + GDP
-
-
-
-
?
dATP + GMP
dADP + GDP
-
-
-
-
?
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
dGMP + ATP
dGDP + ADP
-
-
-
-
?
dGMP + ATP
dGDP + ADP
-
-
-
-
?
dGMP + ATP
dGDP + ADP
-
Catalyses reversible phosphoryl transfer from a nucleotide donor to a nucleotide acceptor. Phosphorylation of (d)GMP to (d)GDP using ATP as phosphoryl donor. Guanylate monophosphate kinases are involved in the synthesis of nucleotide precursors, they indirectly modulate the synthesis of DNA and RNA.
-
-
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.
-
-
r
GMP + ATP
GDP + ADP
-
-
-
-
?
GMP + ATP
GDP + ADP
-
-
-
-
?
GMP + ATP
GDP + ADP
-
Catalyses reversible phosphoryl transfer from a nucleotide donor to a nucleotide acceptor. Phosphorylation of (d)GMP to (d)GDP using ATP as phosphoryl donor. Guanylate monophosphate kinases are involved in the synthesis of nucleotide precursors, they indirectly modulate the synthesis of DNA and RNA.
-
-
r
GMP + MgATP2-
MgADP- + GDP
-
-
-
-
?
GMP + MgATP2-
MgADP- + GDP
-
-
-
-
?
guanosine monophosphate + adenosine triphosphate
guanosine diphosphate + adenosine diphosphate
Guanylate kinase (GK) is an essential enzyme that catalyzes the transfer of a phosphate from adenosine triphosphate (ATP) to guanosine monophosphate (GMP).
-
-
?
guanosine monophosphate + adenosine triphosphate
guanosine diphosphate + adenosine diphosphate
in the presence of Mg2+
-
-
r
additional information
?
-
recombinant enzyme BmGK utilizes both GMP and dGMP as substrates. No activity with dTMP, UMP, CMP, dCMP, IMP, XMP, CTP, UTP, and TTP
-
-
?
additional information
?
-
-
recombinant enzyme BmGK utilizes both GMP and dGMP as substrates. No activity with dTMP, UMP, CMP, dCMP, IMP, XMP, CTP, UTP, and TTP
-
-
?
additional information
?
-
-
MAGUKs contain three PSD-95/Discs large/Zona occludens 1, i.e. PDZ, domains, an src-homology 3, i.e. SH3, domain and a C-terminal guanylate kinase domain and play a key role in the regulation of the intracellular trafficking and synaptic localization of ionotropic glutamate receptors. In particular, the postsynaptic density-95-like subfamily of MAGUKs, PSD-MAGUKs, organizes ionotropic glutamate receptors and their associated signaling proteins in the postsynaptic density of the excitatory synapse regulating the strength of synaptic activity. Alterations of PSD-MAGUK protein interaction with N-methyl-D-aspartate, NMDA, receptors regulatory subunits are common events in several CNS disorders, overview. NMDA receptors' synaptic localization and binding to PSD-MAGUK protein family play a key role in the control of downstream signals resulting from receptor activation, physiological function, overview. The enzyme plays a role in excitotoxicity and neurodegenerative disorders, e.g. in Parkinson disease and Alzheimer disease. Physiological functions, detailed overview
-
-
?
additional information
?
-
-
the post-synaptic density-95 membrane associated guanylate kinase family of scaffolding proteins, MAGUK, associate with N-methyl-D-aspartate receptor NR2 subunits via their C-terminal glutamate serine, or aspartate/glutamate, valine motifs. N-methyl-D-aspartate receptors are a subclass of ionotropic glutamate receptors that are trafficked and/or clustered at synapses by MAGUK. Receptor binding of PSD variants differin the impact on the stabilisation, turnover and compartmentalisation of N-methyl-D-aspartate receptor subtypes in neurones during development and in the mature brain
-
-
?
additional information
?
-
-
binding of N-methyl-D-aspartate receptors NR2B and NR2A, wild-type and mutant proteins, by PSD variants, overview
-
-
?
additional information
?
-
-
MAGUKs contain three PSD-95/Discs large/Zona occludens 1, i.e. PDZ, domains, an src-homology 3, i.e. SH3, domain and a C-terminal guanylate kinase domain and play a key role in the regulation of the intracellular trafficking and synaptic localization of ionotropic glutamate receptors. In particular, the postsynaptic density-95-like subfamily of MAGUKs, PSD-MAGUKs, organizes ionotropic glutamate receptors and their associated signaling proteins in the postsynaptic density of the excitatory synapse regulating the strength of synaptic activity. Alterations of PSD-MAGUK protein interaction with N-methyl-D-aspartate, NMDA, receptors regulatory subunits are common events in several CNS disorders, overview, NMDA receptors' synaptic localization and binding to PSD-MAGUK protein family play a key role in the control of downstream signals resulting from receptor activation, physiological function, overview
-
-
?
additional information
?
-
-
the enzyme forms complexes with DNA
-
-
?
additional information
?
-
the enzyme forms complexes with DNA
-
-
?
additional information
?
-
the enzyme forms complexes with DNA
-
-
?
additional information
?
-
-
the cytosolic isozyme is indispensable for the growth and development of plants, but not for chloroplast development, while the plastid/mitochondrial isozyme is is essential for chloroplast differentiation, overview
-
-
?
additional information
?
-
-
no activity with CMP, dTMP, dAMP, dCMP, and UMP
-
-
?
additional information
?
-
-
MAGUKs contain three PSD-95/Discs large/Zona occludens 1, i.e. PDZ, domains, an src-homology 3, i.e. SH3, domain and a C-terminal guanylate kinase domain and play a key role in the regulation of the intracellular trafficking and synaptic localization of ionotropic glutamate receptors. In particular, the postsynaptic density-95-like subfamily of MAGUKs, PSD-MAGUKs, organizes ionotropic glutamate receptors and their associated signaling proteins in the postsynaptic density of the excitatory synapse regulating the strength of synaptic activity. Alterations of PSD-MAGUK protein interaction with N-methyl-D-aspartate, NMDA, receptors regulatory subunits are common events in several CNS disorders, overview, NMDA receptors' synaptic localization and binding to PSD-MAGUK protein family play a key role in the control of downstream signals resulting from receptor activation, physiological function, overview
-
-
?
additional information
?
-
-
synaptic scaffolding molecule, S-SCAM, is a synaptic protein, which harbors five or six PSD-95/Discs large/ZO-1, a guanylate kinase, and two WW domains. S-SCAM is associated with beta-DG and neuroligin 2 at inhibitory synapses, and functions as a linker between the dystrophin glycoprotein complex and the neurexin-neuroligin complex, complex formation analysis, overview
-
-
?
additional information
?
-
-
the voltage-gated calcium channel beta1b contains a conserved guanylate kinase domain, which is alone recapitulating calcium channel beta-subunit CaVbeta-mediated modulation of channel activation facilitating inactivation of the voltage-gated channel. CaVbeta can switch the inactivation phenotype conferred to CaV2.3 from slow to fast after posttranslational modifications during channel biogenesis, modulation mechanism, overview
-
-
?
additional information
?
-
the voltage-gated calcium channel beta1b contains a conserved guanylate kinase domain, which is alone recapitulating calcium channel beta-subunit CaVbeta-mediated modulation of channel activation facilitating inactivation of the voltage-gated channel. CaVbeta can switch the inactivation phenotype conferred to CaV2.3 from slow to fast after posttranslational modifications during channel biogenesis, modulation mechanism, overview
-
-
?
additional information
?
-
-
the voltage-gated calcium channel beta2a contains a conserved guanylate kinase domain, which is alone recapitulating calcium channel beta-subunit CaVbeta-mediated modulation of channel activation inhibiting inactivation of the voltage-gated channel. CaVbeta can switch the inactivation phenotype conferred to CaV2.3 from slow to fast after posttranslational modifications during channel biogenesis, modulation mechanism, overview
-
-
?
additional information
?
-
the voltage-gated calcium channel beta2a contains a conserved guanylate kinase domain, which is alone recapitulating calcium channel beta-subunit CaVbeta-mediated modulation of channel activation inhibiting inactivation of the voltage-gated channel. CaVbeta can switch the inactivation phenotype conferred to CaV2.3 from slow to fast after posttranslational modifications during channel biogenesis, modulation mechanism, overview
-
-
?
additional information
?
-
-
guanylate kinase binds a fragment of microtubule-associated protein-1a, i.e. MAP1a, in the GMP-binding site, the minimal GK binding site comprised by residues 1862-1878. MAP1a, which helps remodel the microtubule cytoskeleton in an activity-dependent manner, a is a common binding partner of PSD-95 GK and binds GK in an extended conformation, PSD-95 GK ligand consensus is not strongly constrained, binding via binding intermediate, structure, molecular dynamics simulation, overview
-
-
?
additional information
?
-
functionally, the guanylate kinase domain is able to interact with a variety of phospho-peptide ligands with high affinity but its binding ability to GMP is low
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
aciclovir (ACV-MP)
?
-
-
-
-
?
ATP + ganciclovir
ADP + ganciclovir phosphate
-
-
-
-
?
additional information
?
-
ATP + dGMP
ADP + dGDP
-
-
-
r
ATP + dGMP
ADP + dGDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
first step in 'cGMP-cycle' toward re-synthesis of cGMP
-
-
?
ATP + GMP
ADP + GDP
-
-
-
r
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
r
ATP + GMP
ADP + GDP
-
signal transduction
-
-
?
ATP + GMP
ADP + GDP
-
signal transduction
-
-
?
ATP + GMP
ADP + GDP
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
guanylate kinase is an essential enzyme
-
-
?
ATP + GMP
ADP + GDP
guanylate kinase is an essential enzyme
-
-
?
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
regulation of cellular adhesion and signal transduction at sites of cell-cell contact
-
-
?
ATP + GMP
ADP + GDP
-
-
-
?
ATP + GMP
ADP + GDP
-
regulation of cellular adhesion and signal transduction at sites of cell-cell contact
-
-
?
ATP + GMP
ADP + GDP
-
key enzyme of biosynthetic pathway of GTP or dGTP
-
r
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
-
?
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
dGMP + ATP
dGDP + ADP
-
-
-
-
?
dGMP + ATP
dGDP + ADP
-
-
-
-
?
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.
-
-
r
GMP + ATP
GDP + ADP
-
-
-
-
?
GMP + ATP
GDP + ADP
-
-
-
-
?
additional information
?
-
-
MAGUKs contain three PSD-95/Discs large/Zona occludens 1, i.e. PDZ, domains, an src-homology 3, i.e. SH3, domain and a C-terminal guanylate kinase domain and play a key role in the regulation of the intracellular trafficking and synaptic localization of ionotropic glutamate receptors. In particular, the postsynaptic density-95-like subfamily of MAGUKs, PSD-MAGUKs, organizes ionotropic glutamate receptors and their associated signaling proteins in the postsynaptic density of the excitatory synapse regulating the strength of synaptic activity. Alterations of PSD-MAGUK protein interaction with N-methyl-D-aspartate, NMDA, receptors regulatory subunits are common events in several CNS disorders, overview. NMDA receptors' synaptic localization and binding to PSD-MAGUK protein family play a key role in the control of downstream signals resulting from receptor activation, physiological function, overview. The enzyme plays a role in excitotoxicity and neurodegenerative disorders, e.g. in Parkinson disease and Alzheimer disease. Physiological functions, detailed overview
-
-
?
additional information
?
-
-
the post-synaptic density-95 membrane associated guanylate kinase family of scaffolding proteins, MAGUK, associate with N-methyl-D-aspartate receptor NR2 subunits via their C-terminal glutamate serine, or aspartate/glutamate, valine motifs. N-methyl-D-aspartate receptors are a subclass of ionotropic glutamate receptors that are trafficked and/or clustered at synapses by MAGUK. Receptor binding of PSD variants differin the impact on the stabilisation, turnover and compartmentalisation of N-methyl-D-aspartate receptor subtypes in neurones during development and in the mature brain
-
-
?
additional information
?
-
-
MAGUKs contain three PSD-95/Discs large/Zona occludens 1, i.e. PDZ, domains, an src-homology 3, i.e. SH3, domain and a C-terminal guanylate kinase domain and play a key role in the regulation of the intracellular trafficking and synaptic localization of ionotropic glutamate receptors. In particular, the postsynaptic density-95-like subfamily of MAGUKs, PSD-MAGUKs, organizes ionotropic glutamate receptors and their associated signaling proteins in the postsynaptic density of the excitatory synapse regulating the strength of synaptic activity. Alterations of PSD-MAGUK protein interaction with N-methyl-D-aspartate, NMDA, receptors regulatory subunits are common events in several CNS disorders, overview, NMDA receptors' synaptic localization and binding to PSD-MAGUK protein family play a key role in the control of downstream signals resulting from receptor activation, physiological function, overview
-
-
?
additional information
?
-
-
the cytosolic isozyme is indispensable for the growth and development of plants, but not for chloroplast development, while the plastid/mitochondrial isozyme is is essential for chloroplast differentiation, overview
-
-
?
additional information
?
-
-
MAGUKs contain three PSD-95/Discs large/Zona occludens 1, i.e. PDZ, domains, an src-homology 3, i.e. SH3, domain and a C-terminal guanylate kinase domain and play a key role in the regulation of the intracellular trafficking and synaptic localization of ionotropic glutamate receptors. In particular, the postsynaptic density-95-like subfamily of MAGUKs, PSD-MAGUKs, organizes ionotropic glutamate receptors and their associated signaling proteins in the postsynaptic density of the excitatory synapse regulating the strength of synaptic activity. Alterations of PSD-MAGUK protein interaction with N-methyl-D-aspartate, NMDA, receptors regulatory subunits are common events in several CNS disorders, overview, NMDA receptors' synaptic localization and binding to PSD-MAGUK protein family play a key role in the control of downstream signals resulting from receptor activation, physiological function, overview
-
-
?
additional information
?
-
-
synaptic scaffolding molecule, S-SCAM, is a synaptic protein, which harbors five or six PSD-95/Discs large/ZO-1, a guanylate kinase, and two WW domains. S-SCAM is associated with beta-DG and neuroligin 2 at inhibitory synapses, and functions as a linker between the dystrophin glycoprotein complex and the neurexin-neuroligin complex, complex formation analysis, overview
-
-
?
additional information
?
-
-
the voltage-gated calcium channel beta1b contains a conserved guanylate kinase domain, which is alone recapitulating calcium channel beta-subunit CaVbeta-mediated modulation of channel activation facilitating inactivation of the voltage-gated channel. CaVbeta can switch the inactivation phenotype conferred to CaV2.3 from slow to fast after posttranslational modifications during channel biogenesis, modulation mechanism, overview
-
-
?
additional information
?
-
the voltage-gated calcium channel beta1b contains a conserved guanylate kinase domain, which is alone recapitulating calcium channel beta-subunit CaVbeta-mediated modulation of channel activation facilitating inactivation of the voltage-gated channel. CaVbeta can switch the inactivation phenotype conferred to CaV2.3 from slow to fast after posttranslational modifications during channel biogenesis, modulation mechanism, overview
-
-
?
additional information
?
-
-
the voltage-gated calcium channel beta2a contains a conserved guanylate kinase domain, which is alone recapitulating calcium channel beta-subunit CaVbeta-mediated modulation of channel activation inhibiting inactivation of the voltage-gated channel. CaVbeta can switch the inactivation phenotype conferred to CaV2.3 from slow to fast after posttranslational modifications during channel biogenesis, modulation mechanism, overview
-
-
?
additional information
?
-
the voltage-gated calcium channel beta2a contains a conserved guanylate kinase domain, which is alone recapitulating calcium channel beta-subunit CaVbeta-mediated modulation of channel activation inhibiting inactivation of the voltage-gated channel. CaVbeta can switch the inactivation phenotype conferred to CaV2.3 from slow to fast after posttranslational modifications during channel biogenesis, modulation mechanism, overview
-
-
?
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5,5'-dithiobis(2-nitrobenzoate)
6-Selenoguanosine 5'-phosphate
-
GMP-phosphorylation, pI 4.9-isozyme, competitive with respect to GMP
6-Thioguanosine 5'-phosphate
8-azaguanosine 5'-monophosphate
-
(d)GMP-phosphorylation
8-bromoguanosine 5'-monophosphate
-
(d)GMP-phosphorylation
9-(1,3-dihydroxy-2-propylmethyl)guanine 5'-monophosphate
-
-
9-(2-hydroxyethoxymethyl)guanine 5'-monophosphate
-
-
9-(6,6-difluoro-6-phosphonohexyl)guanine
-
competitive with respect to GMP, non-competitive with respect to ATP
9-(6-phosphonohexyl)guanine
-
competitive with respect to GMP, non-competitive with respect to ATP
AMP
-
10-15% inhibition at 5 mM
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.
aurin
82% inhibition at 0.05 mM
CMP
-
10-15% inhibition at 5 mM
dAMP
-
10-15% inhibition at 5 mM
dCMP
-
10-15% inhibition at 5 mM
GTP
-
GMP-phosphorylation
guanosine 3',5'-bisdiphosphate
indol-3-acetic acid
-
GMP + ATP protect
Ni2+
high inhibition at 1 mM
p-chloromercuribenzoic acid
P1 -(5'-adenosyl)-P5 -(5'-guanosyl)pentaphosphate
a non-hydrolysable bi-substrate analogue
PMSF
inhibits 65% at 5 mM
suramin
83.5% inhibition at 0.01 mM
UMP
-
10-15% inhibition at 5 mM
Zn2+
high inhibition at 1 mM
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
6-Thioguanosine 5'-phosphate
-
dGMP-phosphorylation; not thiodeoxyguanosine derivative
6-Thioguanosine 5'-phosphate
-
GMP-phosphorylation, pI 4.9-isozyme, competitive with respect to GMP
ATP
-
free form, substrate inhibition, competitive toward MgATP2-
Ca2+
-
in the presence of Mg2+
Ca2+
high inhibition at 1 mM
dGMP
-
competitive inhibitor to GMP
dGMP
-
competitive versus GMP and mixed-type versus ATP
EDTA
complete inhibition at 1 mM
EDTA
-
85% inhibition at 3 mM
GDP
-
GMP-phosphorylation
GMP
-
competitive inhibitor to dGMP
GMP
-
non competitive with respect to MgATP2- because of the formation of an abortive complex guanylate kinase-MgATP2-GMP
guanosine 3',5'-bisdiphosphate
specific inhibition of the organellar isozyme
guanosine 3',5'-bisdiphosphate
-
specific inhibition of the isozyme
guanosine 3',5'-bisdiphosphate
specific inhibition of the organellar isozyme
guanosine 3',5'-bisdiphosphate
specific inhibition of the organellar isozyme
Li+
-
-
N-ethylmaleimide
-
-
p-chloromercuribenzoic acid
-
1,4-dithiothreitol reverses
p-chloromercuribenzoic acid
-
1,4-dithiothreitol reverses
p-chloromercuribenzoic acid
-
1,4-dithiothreitol reverses
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
no effect at 0.25 mM, 30% activity at 2.5 mM
p-hydroxymercuribenzoate
-
-
additional information
no or poor inhibition by sulfhydryl group inhibitors p-chloromercuribenzoate and N-ethylmaleimide, reducing agents (DTT and BME) and His modification by diethyl dicarbonate. No or poor inhibition by DEC, ivermectin and levamisole
-
additional information
-
no or poor inhibition by sulfhydryl group inhibitors p-chloromercuribenzoate and N-ethylmaleimide, reducing agents (DTT and BME) and His modification by diethyl dicarbonate. No or poor inhibition by DEC, ivermectin and levamisole
-
additional information
-
no inhibition of the cytosolic isozyme by guanosine 3',5'-bisdiphosphate
-
additional information
-
guanylic nucleotides strongly inhibit, compete with GMP
-
additional information
-
no inhibition by 2-mercaptoethanol, 1,4-dithiothreitol; no inhibition by guanosine, AMP, CMP, UMP, XMP, 6-thioinosine 5'-phosphate
-
additional information
-
in silico identification of novel antagonists and binding insights by structural and functional analyses of guanylate kinase of Leishmania donovani and interaction with inhibitors
-
additional information
no inhibition of the cytosolic isozyme by guanosine 3',5'-bisdiphosphate
-
additional information
no inhibition of the cytosolic isozyme by guanosine 3',5'-bisdiphosphate
-
additional information
no inhibition of the cytosolic isozyme by guanosine 3',5'-bisdiphosphate
-
additional information
no inhibition of the cytosolic isozyme by guanosine 3',5'-bisdiphosphate
-
additional information
-
no inhibition of the cytosolic isozyme by guanosine 3',5'-bisdiphosphate
-
additional information
-
no inhibition by TMP and by 2-mercaptoethanol up to 5 mM
-
additional information
-
GMP-phosphorylation is less sensitive to metal ions than dGMP-phosphorylation; minimal inactivation by iodoacetate and iodoacetamide not affected by the presence or absence of KCl; no inhibition by 2-mercaptoethanol, 1,4-dithiothreitol
-
additional information
-
no inhibition by 2-mercaptoethanol, 1,4-dithiothreitol; no inhibition by guanosine, AMP, CMP, UMP, XMP, 6-thioinosine 5'-phosphate
-
additional information
no inhibition of the cytosolic isozyme by guanosine 3',5'-bisdiphosphate
-
additional information
-
no inhibition of the cytosolic isozyme by guanosine 3',5'-bisdiphosphate
-
additional information
-
no inhibition by 2-mercaptoethanol, 1,4-dithiothreitol; no inhibition by guanosine, AMP, CMP, UMP, XMP, 6-thioinosine 5'-phosphate
-
additional information
-
no inhibition by 9-(5-phosphonopentyl)guanine (i.e. isosteric analogue of acyclovir 5'-monophosphate)
-
additional information
-
no inhibition of the cytosolic isozyme by guanosine 3',5'-bisdiphosphate
-
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drug target
-
success for treatment with 5'-guanylic acid in conjunction first-line antileishmanial therapies
malfunction
-
removal of membrane-associated guanylate kinase (MAGUK) via RNAi-mediated knockdown in the CA1 hippocampal region in immature animals causes rapid and lasting reductions in glutamatergic transmission. In mature animals, the same manipulation has little acute effect. The hippocampal dentate gyrus, a region with ongoing adult neurogenesis, is sensitive to MAGUK loss in mature animals, behaving like an immature CA1 cell
evolution
DLG1 is a member of the membrane associated guanylate kinase (MAGUK) family of proteins. The GK domains of the MAGUK family proteins are catalytically inactive, and instead are involved in protein-protein interactions
evolution
GMPK is a member of the family of ATP:NMP phosphoryltransferases, nucleoside monophosphate kinases, NMP kinases, or NMPKs
metabolism
-
guanylate kinase is a key enzyme in guanine nucleotide biosynthesis, purine biosynthetic pathways in plant cells and bacteria, overview
metabolism
-
guanylate kinase is a key enzyme in guanine nucleotide biosynthesis, purine biosynthetic pathways in plant cells and bacteria, overview
metabolism
guanylate kinase is a key enzyme in guanine nucleotide biosynthesis, purine biosynthetic pathways in plant cells and bacteria, overview
metabolism
guanylate kinase is a key enzyme in guanine nucleotide biosynthesis, purine biosynthetic pathways in plant cells and bacteria, overview
metabolism
guanylate kinase is a key enzyme in guanine nucleotide biosynthesis, purine biosynthetic pathways in plant cells and bacteria, overview
metabolism
guanylate kinase is a key enzyme in guanine nucleotide biosynthesis, purine biosynthetic pathways in plant cells and bacteria, overview
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
metabolism
critical role in metabolic activation of antiviral and antineoplastic nucleoside-analog prodrugs
metabolism
-
guanylate kinase is one of the key enzymes in nucleotide biosynthesis
metabolism
-
the enzyme catalyzes the transfer of a phosphate from ATP to GMP. It is indispensable for converting GMP to GDP and therefore synthesis of GTP
metabolism
the only known enzyme responsible for cellular GDP production, making it essential for cellular viability and proliferation
metabolism
-
guanylate kinase is a key enzyme in guanine nucleotide biosynthesis, purine biosynthetic pathways in plant cells and bacteria, overview
-
metabolism
-
guanylate kinase is a key enzyme in guanine nucleotide biosynthesis, purine biosynthetic pathways in plant cells and bacteria, overview
-
physiological function
-
guanylate kinase is the sole molecular target for the development of acquired resistance to the cytotoxic nucleotide 9-[2-(phosphonomethoxyethyl)]-guanine
physiological function
-
the guanylate kinase domain of DLG1/SAP97 binds to asymmetric cell division regulatory protein LGN in a phosphorylation-dependent manner
physiological function
the guanylate kinase domain of DLG1/SAP97 binds to asymmetric cell division regulatory protein LGN in a phosphorylation-dependent manner
physiological function
enzyme GMPK plays an important role in the recycling of the secondary messenger cGMP and thereby regulates the supply of guanine nucleotides to various signal transduction pathways. In addition to its physiological roles, GMPK is also required for the intracellular activation of numerous antiviral and anticancer purine nucleoside analog prodrugs
physiological function
guanylate kinase is a key enzyme in guanine nucleotide biosynthesis that catalyzes the conversion of GMP to GDP, is a target of regulation by guanosine 3',5'-bisdiphosphate in chloroplasts. Plants have two distinct types of GK that are localized to organelles (GKpm) or to the cytosol (GKc) and both are essential for growth and development
physiological function
guanylate kinase is a key enzyme in guanine nucleotide biosynthesis that catalyzes the conversion of GMP to GDP, is a target of regulation by guanosine 3',5'-bisdiphosphate in chloroplasts. Plants have two distinct types of GK that are localized to organelles (GKpm) or to the cytosol (GKc) and both are essential for growth and development. guanosine 3',5'-bisdiphosphate plays a pivotal role in the regulation of GTP biosynthesis in chloroplasts through specific inhibition of GKpm activity, with the regulation of GTP biosynthesis in chloroplasts thus being independent of that in the cytosol
physiological function
guanylate kinase is a key enzyme in guanine nucleotide biosynthesis that catalyzes the conversion of GMP to GDP, is a target of regulation by guanosine 3',5'-bisdiphosphate in chloroplasts. Plants have two distinct types of GK that are localized to organelles (GKpm) or to the cytosol (GKc) and both are essential for growth and development. guanosine 3',5'-bisdiphosphate plays a pivotal role in the regulation of GTP biosynthesis in chloroplasts through specific inhibition ofGKpmactivity, with the regulation of GTP biosynthesis in chloroplasts thus being independent of that in the cytosol
physiological function
guanylate kinase is a key enzyme in guanine nucleotide biosynthesis that catalyzes the conversion of GMP to GDP, is a target of regulation by guanosine 3',5'-bisdiphosphate in chloroplasts. Plants have two distinct types of GK that are localized to organelles (GKpm) or to the cytosol (GKc) and both are essential for growth and development. guanosine 3',5'-bisdiphosphate plays a pivotal role in the regulation of GTP biosynthesis in chloroplasts through specific inhibition ofGKpmactivity, with the regulation of GTP biosynthesis in chloroplasts thus being independent of that in the cytosol
physiological function
tumor suppressor discs large homolog 1, i.e. DLG1/SAP97, is involved in the development and regulation of neuronal and immunological synapses. DLG1 is a member of the membrane associated guanylate kinase (MAGUK) family of proteins, which function as molecular scaffolds. The C-terminal guanylate kinase (GK) domain of DLG1 binds peptides with a phosphorylated serine residue. The GK domains of the MAGUK family proteins are catalytically inactive, and instead are involved in protein-protein interactions
physiological function
-
membrane-associated guanylate kinases (MAGUKs) play an essential role localizing alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs) in adult rats
physiological function
-
the enzyme plays important roles in asexual/sexual development, conidial septation, and pathogenicity. Isoenzyme MoGuk1 likely is essential for Magnaporthe oryzae, and MoGuk2 is involved in the de novo GTP biosynthesis pathway and is important for development and virulence in the rice blast fungus
physiological function
-
guanylate kinase is a key enzyme in guanine nucleotide biosynthesis that catalyzes the conversion of GMP to GDP, is a target of regulation by guanosine 3',5'-bisdiphosphate in chloroplasts. Plants have two distinct types of GK that are localized to organelles (GKpm) or to the cytosol (GKc) and both are essential for growth and development. guanosine 3',5'-bisdiphosphate plays a pivotal role in the regulation of GTP biosynthesis in chloroplasts through specific inhibition ofGKpmactivity, with the regulation of GTP biosynthesis in chloroplasts thus being independent of that in the cytosol
-
additional information
free Mg+2 (not complexed to ATP) and GTP play a regulatory role in catalysis of BmGK. The enzyme shows a higher catalytic efficiency compared to the human enzyme and shows ternary complex (BmGK-GMP-ATP) formation with sequential substrate binding. Homology modelling and docking study with GMP using the crystal structure of the yeast enzyme, PDB ID 1EX7
additional information
-
free Mg+2 (not complexed to ATP) and GTP play a regulatory role in catalysis of BmGK. The enzyme shows a higher catalytic efficiency compared to the human enzyme and shows ternary complex (BmGK-GMP-ATP) formation with sequential substrate binding. Homology modelling and docking study with GMP using the crystal structure of the yeast enzyme, PDB ID 1EX7
additional information
size and shape of open and closed enzyme GMPK are tracked by SAXS. The binding of substrates GMP and AMPPNP, or Ap5G, or GMP and ADP, results in the compaction of size and shape of human enzyme GMPK. Determination of structural changes between open and completely closed hGMPK conformation, overview. Homology modelling of hGMPK by using the crystal structure of mGMPK's closed conformation, residues 5-194 of 197, as template, PDB ID 1LVG
additional information
-
size and shape of open and closed enzyme GMPK are tracked by SAXS. The binding of substrates GMP and AMPPNP, or Ap5G, or GMP and ADP, results in the compaction of size and shape of human enzyme GMPK. Determination of structural changes between open and completely closed hGMPK conformation, overview. Homology modelling of hGMPK by using the crystal structure of mGMPK's closed conformation, residues 5-194 of 197, as template, PDB ID 1LVG
additional information
the DLG1 GK structure adopts an open conformation. Structural comparisons of the MAGUK guanylate kinase domains and the guanylate kinase enzyme, overview
additional information
-
the DLG1 GK structure adopts an open conformation. Structural comparisons of the MAGUK guanylate kinase domains and the guanylate kinase enzyme, overview
additional information
the open-closed conformational transition in the wild-type enzyme is positive correlated with the process of GMP binding, indicating a GMP-induced closing motion of the enzyme. The GMP-bound enzyme maintains the fully closed state, in the presence of GMP, the inter-domain motions of GK enzyme are significantly restricted. Three residues Ser35, Glu70, and Asp101 more closely coordinate to the guanine ring of GMP. Structure modelling using structure PDB ID 1ex7 as a template
additional information
-
activity remains essentially unchanged with change in the growth condition (maltose + peptides, maltose, maltose + peptides + sulfur S(0), maltose + sulfur S(0), peptides + sulfur S(0))
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Hall, S.W.; Khn, H.
Purification and properties of guanylate kinase from bovine retinas and rod outer segments
Eur. J. Biochem.
161
551-556
1986
Bos taurus
brenda
Griffith, T.J.; Helleiner, C.W.
The partial purification of deoxynucleoside monophosphate kinases from L cells
Biochim. Biophys. Acta
108
114-124
1965
Mus musculus
brenda
Shimono, H.; Sugino, Y.
Metabolism of deoxyribonucleotides. Purification and properties of deoxyguanosine monophosphokinase of calf thymus
Eur. J. Biochem.
19
256-263
1971
Bos taurus, Rattus norvegicus
brenda
Buccino, R.J.; Roth, J.S.
Partial purification and properties of ATP:GMP phosphransferase from rat liver
Arch. Biochem. Biophys.
132
49-61
1969
Rattus norvegicus
brenda
Oeschger, M.
Guanylate kinase from Escherichia coli B
Methods Enzymol.
51
473-482
1978
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Agarwal, K.C.; Miech, R.P.; Parks, R.E.
Guanylate kinases from human erythrocytes, hog brain, and rat liver
Methods Enzymol.
51
483-490
1978
Homo sapiens, Rattus norvegicus, Sus scrofa
brenda
Moriguchi, M.; Kohno, H.; Kamei, M.; Tochikura, T.
Purification and properties of guanylate kinase from bakers yeast
Biochim. Biophys. Acta
662
165-167
1981
Saccharomyces cerevisiae
brenda
Berger, A.; Schiltz, E.; Schultz, G.E.
Guanylate kinase from Saccharomyces cerevisiae. Isolation and characterization, crystallization and preliminary X-ray analysis, amino acid sequence and comparison with adenylate kinases
Eur. J. Biochem.
184
433-443
1989
Saccharomyces cerevisiae
brenda
Stehle, T.; Schultz, G.E.
Temperature-dependent space-group transitions in crystals of guanylate kinase from yeast
Acta Crystallogr. Sect. B Struct. Sci.
B48
546-548
1992
Saccharomyces cerevisiae
-
brenda
Stehle, T.; Schultz, G.E.
Three-dimensional structure of the complex of guanylate kinase from yeast with its substrate GMP
J. Mol. Biol.
211
249-254
1990
Saccharomyces cerevisiae
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