2.7.4.8: guanylate kinase
This is an abbreviated version!
For detailed information about guanylate kinase, go to the full flat file.
Word Map on EC 2.7.4.8
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2.7.4.8
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junction
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synapses
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drosophila
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nmda
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cell-cell
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src
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excitatory
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synapse-associated
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hippocampal
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domain-containing
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magi-1
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adaptor
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spine
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palmitoylated
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n-methyl-d-aspartate
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presynaptic
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glutamatergic
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kinase-like
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adherens
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pdz-binding
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zonula
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carma1
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crumbs
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bcl10
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neurexins
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discs-large
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dgmp
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septate
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occludens
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kinase-associated
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junction-associated
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tcr-induced
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ampars
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shank
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mucosa-associated
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card-containing
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neuroligins
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drug development
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medicine
- 2.7.4.8
- junction
- synapses
- drosophila
- nmda
-
cell-cell
- src
-
excitatory
-
synapse-associated
- hippocampal
-
domain-containing
-
magi-1
- adaptor
-
spine
-
palmitoylated
- n-methyl-d-aspartate
-
presynaptic
-
glutamatergic
-
kinase-like
-
adherens
-
pdz-binding
-
zonula
- carma1
-
crumbs
- bcl10
-
neurexins
-
discs-large
- dgmp
-
septate
-
occludens
-
kinase-associated
-
junction-associated
-
tcr-induced
-
ampars
-
shank
-
mucosa-associated
-
card-containing
-
neuroligins
- drug development
- medicine
Reaction
Synonyms
5'-GMP kinase, apo-EcGMPK, ATP: GMP phosphotransferase, ATP:GMP phosphotransferase, BmGK, CASK polypeptide, Cavbeta1b, Cavbeta2a, deoxyguanylate kinase, DLG1/SAP97, ecGMPK, GK, GK3, GKc, GKpm, GMK, GMK3, GMP kinase, GMPK, guanosine monophosphate kinase, guanosine monophosphate kinase (EcGMPK), guanylate kinase, guanylate kinase (GK), guanylate monophosphate kinase, GUK, kinase, guanylate (phosphorylating), MAGUK, MAGUK PSD-95, MAGUKs, membrane associated guanylate kinase, membrane associated guanylate kinase protein, membrane-associated guanylate kinase, membrane-associated guanylate kinases, MoGuk1, MoGuk2, More, organellar GK, post-synaptic density-95 membrane associated guanylate kinase, postsynaptic density protein-95 SH3 GK, PSD-95 GK, PSD-95 MAGUK, PSD-95alpha, PSD-95beta, Staphylococcus aureus guanylate monophosphate kinase, voltage-gated calcium channel beta1b, voltage-gated calcium channel beta2a, YGK
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2.7.4.8 guanylate kinaseAdvanced search results
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results (General Information
General Information on EC 2.7.4.8 - guanylate kinase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
drug target
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success for treatment with 5'-guanylic acid in conjunction first-line antileishmanial therapies
evolution
malfunction
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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
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
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guanylate kinase is a key enzyme in guanine nucleotide biosynthesis, purine biosynthetic pathways in plant cells and bacteria, overview
metabolism
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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
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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
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guanylate kinase is one of the key enzymes in nucleotide biosynthesis
metabolism
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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
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guanylate kinase is a key enzyme in guanine nucleotide biosynthesis, purine biosynthetic pathways in plant cells and bacteria, overview
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metabolism
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guanylate kinase is a key enzyme in guanine nucleotide biosynthesis, purine biosynthetic pathways in plant cells and bacteria, overview
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physiological function
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guanylate kinase is the sole molecular target for the development of acquired resistance to the cytotoxic nucleotide 9-[2-(phosphonomethoxyethyl)]-guanine
physiological function
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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
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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
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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
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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
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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
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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
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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
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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
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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))
