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Information on EC 2.7.4.8 - guanylate kinase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P15454
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2.7.4.8 guanylate kinaseIUBMB Comments
dGMP can also act as acceptor, and dATP can act as donor.
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Word Map
- 2.7.4.8
- junction
- synapses
- drosophila
- nmda
-
cell-cell
- src
-
excitatory
-
synapse-associated
- hippocampal
-
domain-containing
-
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
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
maguk, guanylate kinase, membrane-associated guanylate kinase, maguks, membrane-associated guanylate kinases, guanylate kinase (gk), gmp kinase, membrane associated guanylate kinase, gmpk, cavbeta2a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-GMP kinase
-
-
-
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ATP:GMP phosphotransferase
-
-
-
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deoxyguanylate kinase
-
-
-
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GMP kinase
-
-
-
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guanosine monophosphate kinase
-
-
-
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kinase, guanylate (phosphorylating)
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:(d)GMP phosphotransferase
dGMP can also act as acceptor, and dATP can act as donor.
CAS REGISTRY NUMBER
COMMENTARY
9026-59-9
-
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
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
-
-
?
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
-
-
?
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
-
regulation of cellular adhesion and signal transduction at sites of cell-cell contact
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
GMP
-
non competitive with respect to MgATP2- because of the formation of an abortive complex guanylate kinase-MgATP2-GMP
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
RCSB Protein Data Bank: 1EX6, enzyme with a non-acetylated N terminus in its unligated form
Uniprot
RCSB Protein Data Bank: 1EX7, enzyme with a non-acetylated N terminus in a complex with GMP
Uniprot
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
guanylate kinase is a key enzyme in guanine nucleotide biosynthesis, purine biosynthetic pathways in plant cells and bacteria, overview
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
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Y78F
-
affinity for MgATP2- similar to wild type but affinity for GMP decreases by a factor of 12
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography
method that includes DEAE-cellulose, hydroxyapatite and Sephadex-75 chromatography
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method that includes DEAE-Sephacel, Cibacron-blue Sepharose and two Sephadex-75 chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
-
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
Stehle, T.; Schultz, G.E.
Refined structure of the complex between guanylate kinase and its substrate GMP at 2.0 A resolution
J. Mol. Biol.
224
1127-1141
1992
Saccharomyces cerevisiae
Li, Y.; Zhang, Y.; Yan, H.
Kinetic and thermodynamic characterizations of yeast guanylate kinase
J. Biol. Chem.
271
28038-28044
1996
Saccharomyces cerevisiae
Zhang, Y.; Li, Y.; Wu, Y.; Yan, H.
Structural and functional roles of tyrosine 78 of yeast guanylate kinase
J. Biol. Chem.
272
19343-19350
1997
Saccharomyces cerevisiae
Blaszczyk, J.; Li, Y.; Yan, H.; Ji, X.
Crystal structure of unligated guanylate kinase from yeast reveals GMP-induced conformational changes
J. Mol. Biol.
307
247-257
2001
Saccharomyces cerevisiae (P15454), Saccharomyces cerevisiae
Olsen, O.; Bredt, D.S.
Functional analysis of the nucleotide binding domain of membrane-associated guanylate kinases
J. Biol. Chem.
278
6873-6878
2003
Saccharomyces cerevisiae, Rattus norvegicus
Nomura, Y.; Izumi, A.; Fukunaga, Y.; Kusumi, K.; Iba, K.; Watanabe, S.; Nakahira, Y.; Weber, A.P.; Nozawa, A.; Tozawa, Y.
Diversity in guanosine 3,5-bisdiphosphate (ppGpp) sensitivity among guanylate kinases of bacteria and plants
J. Biol. Chem.
289
15631-15641
2014
Arabidopsis thaliana (Q94JM2), Bacillus subtilis, Escherichia coli, Oryza sativa Japonica Group (Q10M74), Oryza sativa Japonica Group (Q2QPW1), Oryza sativa Japonica Group Nipponbare (Q10M74), Oryza sativa Japonica Group Nipponbare (Q2QPW1), Pisum sativum (W8VNI6), Pisum sativum (W8VZ39), Pisum sativum, Saccharomyces cerevisiae (P15454), Saccharomyces cerevisiae, Synechococcus elongatus, Synechococcus elongatus PCC 7942
EXTERNAL LINKS (specific for EC-Number 2.7.4.8)
Transporter Classification Database (TCDB): 8.A.24.1.8
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