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Information on EC 2.7.1.73 - inosine kinase
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2.7.1.73 inosine kinaseSpecify your search results
Word Map
- 2.7.1.73
- purine
-
salvage
- nucleoside
- guanine
- hypoxanthine
-
2.7.1.20
- acetylicum
-
2.4.2.7
-
phosphoribosylation
-
3.5.4.3
- ppgpp
-
brevibacterium
- xanthosine
- deoxyadenosine
-
exiguobacterium
- deoxyguanosine
- ribokinase
- synthesis
- nutrition
The enzyme appears in viruses and cellular organisms
Synonyms
inosine kinase, inosine-guanosine kinase, guanosine-inosine kinase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
guanosine-inosine kinase
inosine-guanosine kinase
-
-
-
-
kinase, inosine (phosphorylating)
-
-
-
-
guanosine-inosine kinase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + inosine = ADP + IMP
ordered bi bi mechanism in which guanosine is the first substrate to bind and GMP is the last product to be released
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ATP + inosine = ADP + IMP
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP:inosine 5'-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY
37237-46-0
-
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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
UTP + guanosine
UDP + GMP
UTP shows 20% of the activity with ATP
-
-
?
ATP + inosine
ADP + 5'-IMP
about 60% of the activity with guanosine
-
?
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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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120
50
-
substrate inosine, crude cell extract, pH 7.5, temperature not specified in the publication
60
-
substrate guanosine, crude cell extract, pH 7.5, temperature not specified in the publication
120
-
substrate guanosine, crude cell extract, pH 7.5, temperature not specified in the publication
120
-
substrate inosine, crude cell extract, pH 7.5, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10.5
-
pH 6.0: about 40% of maximal activity, pH 10.5: about 85% of maximal activity
6.5 - 8.2
-
pH 6.5: about 60% of maximal activity, pH 8.2: about 70% of maximal activity, Tris-maleate buffer
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
-
in the salvage pathway, guanosine and inosine are directly phosphorylated to GMP and IMP, respectively, by guanosine-inosine kinase, or guanosine is indirectly converted to GMP through serial phosphorolysis and phosphorylation catalyzed by purine nucleoside phosphorylase and guanine phosphoribosyltransferase, respectively, pathway, overview
metabolism
-
comparison of growth characteristics including intracellular protein levels, RNA content, and nucleotide pool sizes between the extreme halophile Halobacterium halobium and the moderate halophile Haloferax volcanii. The differences in the metabolism of purine bases and nucleosides and the sensitivity to purine analogs between the two halobacteria are reflected in differences in purine enzyme levels
metabolism
-
comparison of growth characteristics including intracellular protein levels, RNA content, and nucleotide pool sizes between the extreme halophile Halobacterium halobium and the moderate halophile Haloferax volcanii. The differences in the metabolism of purine bases and nucleosides and the sensitivity to purine analogs between the two halobacteria are reflected in differences in purine enzyme levels
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
overexpression of Gsk in the fed-batch fermentation in recombinant Escherichia coli strain BL21star(DE3) with glucose as the sole carbon source, leads to a significant improvement of GDP-L-fucose production, profiles of cell growth and GDP-L-fucose production, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene gsk, recombinant expression in Corynebacterium ammoniagenes ATP-regenerating strain ATCC 21477, the Escherichia coli trp promoter proves to be most efficient with regard to inducing the expression of gsk, as compared to tac promoter
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gene gsk, several metabolic enzymes such as GMP synthetase and IMP dehydrogenase, GMP reductase, and guanosine-inosine kinase, all involved in the biosynthesis of GMP, are co-overexpressed in recombinant Escherichia coli TOP10 and BL21star(DE3) cells becoming able to produce GDP-L-fucose, pH-stat fed-batch fermentations quantification and optimization, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nutrition
-
practical possibility of producing 5'-GMP by phosphorylation of guanosine using a guanosine-inosine kinase coupled with ATP regeneration
synthesis
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the recombinant strain, which expresses gene gsk and has both inosine kinase activity and ATP-regenerating activity, is used to induce the phosphorylation of inosine to produce inosine 5'-monophosphate, which is widely used as a flavor enhancer
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pierre, K.J.; LePage, G.A.
Formation of inosine-5-monophosphate by a kinase in cell-free extracts of Ehrlich ascites cells in vitro
Proc. Soc. Exp. Biol. Med.
127
432-440
1968
Mus musculus
brenda
Combes, A.; Lefleuriel, J.; Le Floc'h, F.
the inosine-guanosine kinase activity of mitochondria in tubers of Jerusalem artichoke
Plant Physiol. Biochem.
27
729-736
1989
Helianthus tuberosus
-
brenda
Ipata, P.L.; Gualerzi, C.; Scolozzi, C.; Tozzi, M.G.; Trinei, M.; Barsacchi, D.
Occurrence of inosine kinase as a distinct enzyme in Spirulina platensis
Biochem. Biophys. Res. Commun.
209
547-553
1995
Arthrospira platensis
brenda
Mori, H.; Iida, A.; Teshiba, S.; Fujio, T.
Cloning of a guanosine-inosine kinase gene of Escherichia coli and characterization of the purified gene product
J. Bacteriol.
177
4921-4926
1995
Escherichia coli (P0AEW6), Escherichia coli
brenda
Kawasaki, H.; Usuda, Y.; Shimaoka, M.; Utagawa, T.
Development of an improved assay for purine nucleoside kinase activity in cell extracts and detection of inosine kinase activity in Brevibacterium acetylicum ATCC 953, related species, and Corynebacterium flaccumfaciens ATCC 6887
Biosci. Biotechnol. Biochem.
64
761-766
2000
Exiguobacterium acetylicum, Curtobacterium flaccumfaciens
brenda
Kawasaki, H.; Usuda, Y.; Shimaoka, M.; Utagawa, T.
Phosphorylation of guanosine using guanosine-inosine kinase from Exiguobacterium acetylicum coupled with ATP regeneration
Biosci. Biotechnol. Biochem.
64
2259-2261
2000
Exiguobacterium acetylicum
brenda
Kawasaki, H.; Shimaoka, M.; Usuda, Y.; Utagawa, T.
End-product regulation and kinetic mechanism of guanosine-inosine kinase from Escherichia coli
Biosci. Biotechnol. Biochem.
64
972-979
2000
Escherichia coli
brenda
Lee, W.H.; Shin, S.Y.; Kim, M.D.; Han, N.S.; Seo, J.H.
Modulation of guanosine nucleotides biosynthetic pathways enhanced GDP-L-fucose production in recombinant Escherichia coli
Appl. Microbiol. Biotechnol.
93
2327-2334
2012
Escherichia coli
brenda
Usuda, Y.; Shimaoka, M.; Kawasaki, H.; Utagawa, T.
Expression of the guanosine-inosine kinase gene from Exiguobacterium acetylicum in Corynebacterium ammoniagenes and phosphorylation of inosine to produce inosine 5'-monophosphate
World J. Microbiol. Biotechnol.
27
709-712
2011
Exiguobacterium acetylicum
brenda
Stuer-Lauridsen, B.; Nygaard, P.
Purine salvage in two halophilic archaea: characterization of salvage pathways and isolation of mutants resistant to purine analogs
J. Bacteriol.
180
457-463
1998
Halobacterium salinarum, Haloferax volcanii
brenda
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