Information on EC 2.7.1.173 - nicotinate riboside kinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.1.173
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RECOMMENDED NAME
GeneOntology No.
nicotinate riboside kinase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + beta-D-ribosylnicotinate = ADP + nicotinate beta-D-ribonucleotide
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
pyridine nucleotide cycling (plants)
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Nicotinate and nicotinamide metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
ATP:beta-D-ribosylnicotinate 5-phosphotransferase
The enzyme from yeast and human also has the activity of EC 2.7.1.22 (ribosylnicotinamide kinase).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme is structurally similar to Rossmann fold metabolite kinases; the enzyme is structurally similar to Rossmann fold metabolite kinases
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + beta-D-ribosylnicotinamide
ADP + nicotinamide beta-D-ribonucleotide
show the reaction diagram
ATP + beta-D-ribosylnicotinate
ADP + nicotinate beta-D-ribonucleotide
show the reaction diagram
ATP + cytidine
ADP + CMP
show the reaction diagram
ATP + nicotinamide mononucleotide
ADP + nicotinamide mononucleotide phosphate
show the reaction diagram
ATP + tiazofurin
ADP + ?
show the reaction diagram
ATP + uridine
ADP + UMP
show the reaction diagram
GTP + beta-D-ribosylnicotinate
GDP + nicotinate beta-D-ribonucleotide
show the reaction diagram
nicotinic acid riboside is a specific substrate of human Nrk enzymes
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-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + beta-D-ribosylnicotinamide
ADP + nicotinamide beta-D-ribonucleotide
show the reaction diagram
ATP + beta-D-ribosylnicotinate
ADP + nicotinate beta-D-ribonucleotide
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GTP
active with Nrk1
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.051 - 0.063
beta-D-ribosylnicotinamide
0.068 - 30
beta-D-ribosylnicotinate
15 - 30
cytidine
0.11 - 0.27
tiazofurin
1.3 - 17
uridine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21 - 0.34
beta-D-ribosylnicotinamide
0.34 - 1.7
beta-D-ribosylnicotinate
0.48 - 0.82
cytidine
0.35 - 0.49
tiazofurin
0.21 - 1.1
uridine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.1 - 5.4
beta-D-ribosylnicotinamide
19568
0.057 - 6.8
beta-D-ribosylnicotinate
7056
0.016 - 0.055
cytidine
372
1.3 - 4.5
tiazofurin
1893
0.012 - 0.85
uridine
261
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000009
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enzyme in cotyledons, pH 7.6, 27C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at; assay at
7.9
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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of germinating mungbean seedlings
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Nrk1 bound to nucleoside and nucleotide substrates and products, i.e. nicotinamide mononucleotide, ADP, tiazofurin, beta-D-ribosylnicotinate with AppNHp, and beta-D-ribosylnicotinate alone, addition of 10 mM ligand and 20 mM MgCl2, overview. Usage of different crystallization solutions depending on the ligand, containing PEG 2000 mono-methylether or PEG 3350 or PEG 4000 at 15-35%, at pH 5.0-8.0, with 0.2 M NaH2PO4, and different buffers, X-ray diffraction structure determination and analysis at 1.32-1.95 A resolution, molecular replacement
NRK1 in complex with the reaction product nicotinamide mononucleotide, and NRK1 in a ternary complex with ADP and the anticancer drug tiazofurin, sitting-drop vapor-diffusion method, 22C, mixing of protein solution containing 20 mg/ml protein, 2 mM ligand, 20 mM Tris, pH 7.5-7.8, 200 mM NaCl, 5 mM DTT, with reservoir solution containing 28% w/v PEG 3350, 200 mM NH4Cl, 5 mM DTT, and 5 mM Na2HPO4, X-ray diffraction structure determination and analysis at 1.5 A and 2.7 A resolution, respectively, modeling
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme partially by ammonium sulfate fractionation
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recombinant His-tagged NRK1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant Nrk1 and Nrk2 from Escherichia coli by metal chelate affinity chromatography; recombinant Nrk2 from Escherichia coli by metal chelate affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His-tagged wild-type Nrk1 expression in Escherichia coli, expression of wild-type and mutant Nrk1 from the GAL1 promoter on a LEU2 plasmid in Saccharomyces cerevisiae strain BY278; His-tagged wild-type Nrk2 expression in Escherichia coli, expression of wild-type and mutant Nrk2 from the GAL1 promoter on a LEU2 plasmid in Saccharomyces cerevisiae strain BY278
overexpression of His-tagged NRK1 in Escherichia coli strain BL21(DE3)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D35A
site-directed mutagenesis of Nrk2
D36A
site-directed mutagenesis of Nrk1
E100A
site-directed mutagenesis of Nrk2, mutant activity in ATP-dependent phosphorylation is below the level of detection
E174R
site-directed mutagenesis of Nrk2
E98A
site-directed mutagenesis of Nrk1, mutant activity in ATP-dependent phosphorylation is below the level of detection