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Information on EC 2.7.4.8 - guanylate kinase
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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
- hippocampal
-
excitatory
-
domain-containing
-
synapse-associated
- n-methyl-d-aspartate
-
spine
-
magi-1
- adaptor
-
adherens
-
palmitoylated
-
zonula
-
glutamatergic
-
kinase-like
-
pdz-binding
- carma1
- bcl10
-
discs-large
-
crumbs
-
septate
-
occludens
- dgmp
-
kinase-associated
-
tcr-induced
-
card-containing
-
ampars
-
mucosa-associated
-
junction-associated
-
neuroligins
-
neurexins
-
shank
- drug development
- medicine
The enzyme appears in viruses and cellular organisms
Synonyms
5'-GMP kinase, apo-EcGMPK, ATP: GMP phosphotransferase, ATP:GMP phosphotransferase, BmGK, CASK polypeptide, Cavbeta1b, Cavbeta2a, deoxyguanylate kinase, DLG1/SAP97, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ATP: GMP phosphotransferase
ATP:GMP phosphotransferase
CASK polypeptide
cf. EC 2.7.11.1, the protein contains a guanylate kinase domain
DLG1/SAP97
GKpm
GMK
GMP kinase
GMPK
guanosine monophosphate kinase
guanylate kinase
GUK
MAGUK
membrane associated guanylate kinase protein
membrane-associated guanylate kinase
additional information
-
the enzyme belongs to the post-synaptic density-95 membrane associated guanylate kinase, MAGUK, family of scaffolding proteins,
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + GMP = ADP + GDP
-
-
-
-
ATP + GMP = ADP + GDP
conformational changes and induced-fit reaction mechanism of the allosteric enzyme, overview
ATP + GMP = ADP + GDP
conformational changes and induced-fit reaction mechanism of the allosteric enzyme, overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
Phosphorylation
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
ATP:(d)GMP phosphotransferase
dGMP can also act as acceptor, and dATP can act as donor.
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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
ATP + (R)-3-((2-amino-1,6-dihydro-6-oxo-9H-purin-9-yl)methoxy)-4-hydroxybutylphosphonic acid
(R)-ganciclovir phosphonate monophosphate
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
-
-
?
guanosine monophosphate + adenosine triphosphate
guanosine diphosphate + adenosine diphosphate
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
-
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 + GMP
ADP + GDP
-
first step in 'cGMP-cycle' toward re-synthesis of cGMP
-
-
?
ATP + GMP
ADP + GDP
GMP and ATP served as the most effective phosphate acceptor and donor, respectively
-
-
r
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
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
-
nucleoside monophosphate binding site is highly specific for guanine moiety
-
-
?
ATP + GMP
ADP + GDP
-
deoxyguanosine, guanosine are no acceptor substrates
-
-
?
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
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
-
regulation of cellular adhesion and signal transduction at sites of cell-cell contact
-
-
?
ATP + GMP
ADP + GDP
-
nucleoside monophosphate binding site is highly specific for guanine moiety
-
-
?
ATP + GMP
ADP + GDP
-
key enzyme of biosynthetic pathway of GTP or dGTP
-
r
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
-
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
-
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
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
-
-
?
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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
ATP + GMP
ADP + GDP
-
first step in 'cGMP-cycle' toward re-synthesis of cGMP
-
-
?
ATP + GMP
ADP + GDP
guanylate kinase is an essential enzyme
-
-
?
ATP + GMP
ADP + GDP
guanylate kinase is an essential enzyme
-
-
?
ATP + GMP
ADP + GDP
-
regulation of cellular adhesion and signal transduction at sites of cell-cell contact
-
-
?
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
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.
-
-
r
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Fe2+
Fe3+
K+
Mg2+
Mn2+
Na+
NH4+
Rb+
Zn2+
additional information
K+
-
activity of dGMP kinase progressively enhanced as the concentration of KCl is increased to 250 mM, GMP phosphorylation unaffected
additional information
-
GMP-kinase activity is less sensitive to metal ions than dGMP-kinase activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6-Selenoguanosine 5'-phosphate
-
GMP-phosphorylation, pI 4.9-isozyme, competitive with respect to GMP
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
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.
P1 -(5'-adenosyl)-P5 -(5'-guanosyl)pentaphosphate
a non-hydrolysable bi-substrate analogue
6-Thioguanosine 5'-phosphate
-
dGMP-phosphorylation; not thiodeoxyguanosine derivative
6-Thioguanosine 5'-phosphate
-
GMP-phosphorylation, pI 4.9-isozyme, competitive with respect to GMP
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 organellar isozyme
guanosine 3',5'-bisdiphosphate
specific inhibition of the organellar isozyme
additional information
no or poor inhibition by sulfydryl group inhibitors p-chloromercuribenzoate and N-ethylmaleimide, reducing agents (DTT and BME) and His modification by diethyl dicarbonate. No or poor inhbition by DEC, ivermectin and levamisole
-
additional information
-
no or poor inhibition by sulfydryl group inhibitors p-chloromercuribenzoate and N-ethylmaleimide, reducing agents (DTT and BME) and His modification by diethyl dicarbonate. No or poor inhbition 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
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no activation by 1,4-dithiothreitol or 2-mercaptoethanol
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.015
GMP
-
wild type enzyme, in 100 mM Tris–HCl buffer pH 7.5, 4 mM ATP, 10 mM MgCl2, 1 mM dithiothreitol, 100 mM KCl, at 30°C
0.073
GMP
recombinant chloroplast isozyme, pH 7.5, 30°C
0.202
GMP
recombinant cytosolic isozyme, pH 7.5, 30°C
0.27
GMP
-
mutant S35N/V168F, in 100 mM Tris–HCl buffer pH 7.5, 4 mM ATP, 10 mM MgCl2, 1 mM dithiothreitol, 100 mM KCl, at 30°C
additional information
additional information
-
kinetic parameters of several substrates for 4 isoenzymes
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
detailed reaction kinetics, overview
-
additional information
additional information
detailed reaction kinetics, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
23
GMP
recombinant chloroplast isozyme, pH 7.5, 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
317
GMP
recombinant chloroplast isozyme, pH 7.5, 30°C
344
GMP
recombinant cytosolic isozyme, pH 7.5, 30°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.14
9-(6,6-difluoro-6-phosphonohexyl)guanine
-
pH 7.5, 30ºC, higher affinity than 9-(6-phosphonohexyl)guanine for guanylate kinases al pH values below 7.5
0.0028
guanosine 3',5'-bisdiphosphate
versus GMP, pH 7.5, 30°C
0.043
9-(1,3-dihydroxy-2-propylmethyl)guanine 5'-monophosphate
-
pH 7.5, isoenzyme 4
0.052
9-(1,3-dihydroxy-2-propylmethyl)guanine 5'-monophosphate
-
pH 7.5, isoenzyme 4
0.06
9-(1,3-dihydroxy-2-propylmethyl)guanine 5'-monophosphate
-
pH 7.5, isoenzyme 1
0.067
9-(1,3-dihydroxy-2-propylmethyl)guanine 5'-monophosphate
-
pH 7.5, isoenzyme 2
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0005
Ap5G
Escherichia coli
The crystal structure of EcGMPK in complex with Ap5G solved at 2.5 Å resolution.
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5
999
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10.9
-
about half-maximal activity at pH 5 and maximal activity at pH 10.9, GMP-phosphorylation, calf thymus
5.7 - 10.9
-
about half-maximal activity at pH 5.7 and 10.9, dGMP-phosphorylation, calf thymus
6.8 - 8.6
-
about 80% of maximal activity at pH 6.8 and 8.6, about 95% of maximal activity at pH 7.3 and 8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.7 - 4.8
4.9
-
4 isoelectric variants, agarose gel electrophoresis and isoelectric focusing
4.7 - 4.8
-
3 isoelectric variants, predominant form: pI 4.9, agarose gel electrophoresis and isoelectric focusing
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
derived from W3110, uninfected or infected with RNA-phage MS2
-
-
brenda
RCSB Protein Data Bank: 1EX6, enzyme with a non-acetylated N terminus in its unligated form
Uniprot
brenda
RCSB Protein Data Bank: 1EX7, enzyme with a non-acetylated N terminus in a complex with GMP
Uniprot
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
post-synaptic density-95 membrane associated, association with N-methyl-D-aspartate receptor NR2 subunits via their C-terminal glutamate serine, aspartate/glutamate, valine motifs
brenda
-
S-SCAM is associated with beta-dystroglycan 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
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
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
-
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
-
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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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20000
22000
22010
deduced from the amino acid composition and detected by mass spectrometry, adducts with sulfate and not phosphate are detected in mass spectrometry
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
24000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
homodimer
2 * 24000, SDS-PAGE, gel filtration and glutaraldehyde cross-linking
monomer
monomer or dimer
the recombinant and refolded CaVbeta1b-GK is a mixture of dimers and monomers
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
dimer
-
One of the two SaGMK dimers within the crystal asymmetric unit has two monomers in different conformations: an open form with a bound sulfate ion (mimicking the beta-phosphate of ATP) and a closed form with bound GMP and sulfate ion. Each monomer is bound through its P-loop to a sulfate ion.
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
the secondary structure of BmGK consists of 45% alpha-helices, 18% beta-sheets, by circular dichrosim analysis
additional information
-
the secondary structure of BmGK consists of 45% alpha-helices, 18% beta-sheets, by circular dichrosim analysis
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.
additional information
-
structural model of microtubule-associated protein-1a. Domain organization of neuronal MAGUKs, 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
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
additional information
phosphoprotein
-
PSD-MAGUK's major phosphorylation sites, regulation by phosphorylation through Ser/Thr protein kinases and also Tyr-dependent kinases, overview
phosphoprotein
-
PSD-MAGUK's major phosphorylation sites, regulation by phosphorylation, through Ser/Thr protein kinases and also Tyr-dependent kinases, overview
phosphoprotein
-
PSD-MAGUK's major phosphorylation sites, regulation by phosphorylation, through Ser/Thr protein kinases and also Tyr-dependent kinases, overview
additional information
-
As is evident from the structure, GK has a clamp-like cavity, where the two lobes of the protein close through an ca. 1-nm conformational change upon binding the substrates, most of the conformational motion is induced by GMP binding. The substrates GMP and ATP drive this conformational change through several direct and indirect (via water molecules) interactions that bring the LID and nucleotide-monophosphate-binding domain (herein referred to as NMP-BD) nearer and jointly toward the CORE region, the structure closing in a vise-like motion. In this configuration, the CORE is catalytically active toward phosphoryl transfer, which relies on a residue sequence (the P-loop) that is conserved in kinases.
additional information
As is evident from the structure, GK has a clamp-like cavity, where the two lobes of the protein close through an ca. 1-nm conformational change upon binding the substrates, most of the conformational motion is induced by GMP binding. The substrates GMP and ATP drive this conformational change through several direct and indirect (via water molecules) interactions that bring the LID and nucleotide-monophosphate-binding domain (herein referred to as NMP-BD) nearer and jointly toward the CORE region, the structure closing in a vise-like motion. In this configuration, the CORE is catalytically active toward phosphoryl transfer, which relies on a residue sequence (the P-loop) that is conserved in kinases.
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified the GK domain fragment of human DLG1, hanging drop vapor diffusion method, mixing of 6.5 mg/ml protein in 20 mM Tris-HCl buffer, pH 8.0, 150 mM NaCl and 2 mM dithiothreitol, with reservoir solution containing 0.2 M sodium thiocyanate and 22% PEG 3350, 20°C, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement and selenomethionine single-wavelength anomalous dispersion, using the PSD-95 GK domain, PDB ID 1JXO, as a search model
SAP97 SH3-guanylate kinase/p-LGN18 complex, hanging drop vapor diffusion method, using 0.2M ammonium nitrate, 20% (w/v) polyethylene glycol 3350
-
SAP97 SH3-guanylate kinase/p-LGN18 complex, hanging drop vapor diffusion method, using 0.2M ammonium nitrate, 20% (w/v) polyethylene glycol 3350
crystal structure of the enzyme with a non-acetylated N terminus in its unligated form as well as in complex with GMP
temperature-dependent space-group transitions between orthorhombic and tetragonal forms
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D74A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E101D
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N103D
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y76F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S35P
Y78F
-
affinity for MgATP2- similar to wild type but affinity for GMP decreases by a factor of 12
additional information
S35P
the conversed proline residue at this position among all GK domains, drastically impairs the GMP binding affinity and significantly reduces the guanylate kinase activity, functional transition of the enzyme guanylate kinase is induced by a single mutation leading to the functional transition of the enzyme from a phosphoryl transfer kinase into a phosphorprotein interaction domain, molecular dynamic and metadynamics simulations, overview. The serine to proline mutation can also lead to the misrecognition of GMP, explaining the catalytic inactivity of the mutant. The GK domain is in an open state in the S35P mutant
additional information
-
RNAi knockdown of the cytosolic enzyme, a v2 mutant is temperature-sensitive and develops chlorotic leaves at restrictive temperatures, the v2 mutation causes inhibition of chloroplast differentiation; in particular, it disrupts the chloroplast translation machinery during early leaf development
additional information
-
construction of mutant PSD-95 SH3-GK which contains a deleterious point mutation in the C-terminal SH3 domain
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
-
10 min, about 80% loss of activity, t1/2: 3 min (dGMP-phosphorylation), t1/2: 4 min (GMP-phosphorylation)
80
-
incubation for 2 min, 5 min, 10 min or 20 min leads to 43%, 67%, 89% or 97% loss of activity, respectively, 30 min: inactivation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis against water, pH 6 with several changes of outer fluid inactivates, stable to dialysis for less than 36 h without changing the outer fluid
-
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
0°C, below, in 70% saturated ammonium sulfate, several years
4°C, diluted calf thymus enzyme solution, 0.002 mg/ml, inactivation within 10 days, KCl protects
-
4°C, partially purified calf thymus enzyme preparation in the presence of 1 M KCl, 3 months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
4 isoenzymes purified by a method that includes GMP agarose chromatography and isoelectric focusing
-
method
method that includes DEAE-cellulose and Sephadex-75 chromatography
method that includes DEAE-cellulose, hydroxyapatite and Sephadex G-100 chromatography
-
method that includes DEAE-cellulose, hydroxyapatite and Sephadex-75 chromatography
-
method that includes DEAE-cellulose, Sephadex-75 chromatography and isoelectric focusing
-
method that includes DEAE-Sephacel and Blue Sepharose CL 6B chromatography
-
method that includes DEAE-Sephacel, Cibacron-blue Sepharose and two Sephadex-75 chromatography
-
partial
partial by a method that includes DEAE-cellulose, hydroxyapatite and Sephadex G-200 chromatography
-
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 BL21 (DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography, native enzyme from chloroplasts by gel filtration
recombinant His-tagged GK domain fragment of human DLG1 from Escherichia coli by anion exchange chromatography and gel filtration. The tag is cleaved by TEV protease
recombinant His6-tagged PSD-95 SH3-GK from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, recombinant GST-tagged PSD-95 SH3-GK from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography
-
recombinant N-terminally His6-tagged and SUMO-tagged enzyme from Escherichia coli strain BL21-(DE3)-pLysS by nickel affinity chromatography and gel filtration
recombinant protein
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic tree, recombinant expression of C-terminally and N-terminally His-tagged enzyme in Escherichia coli BL21 (DE3)
DNA and amino acid sequence determination and analysis, sequence comparison
-
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expression of GFP-tagged enzyme in COS cells, expression of His6-tagged and GST-tagged PSD-95 SH3-GK in Escherichia coli strain BL21(DE3)
-