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Information on EC 2.7.4.8 - guanylate kinase

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EC Tree
IUBMB Comments
dGMP can also act as acceptor, and dATP can act as donor.
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This record set is specific for:
UNIPROT: Q12959
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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=
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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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
phospho group transfer
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
ATP:(d)GMP phosphotransferase
dGMP can also act as acceptor, and dATP can act as donor.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-59-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DLG1_HUMAN
904
0
100455
Swiss-Prot
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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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of His-tagged GK domain fragment of human DLG1 in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mori, S.; Tezuka, Y.; Arakawa, A.; Handa, N.; Shirouzu, M.; Akiyama, T.; Yokoyama, S.
Crystal structure of the guanylate kinase domain from discs large homolog 1 (DLG1/SAP97)
Biochem. Biophys. Res. Commun.
435
334-338
2013
Homo sapiens (Q12959), Homo sapiens
Manually annotated by BRENDA team