2.7.1.173: nicotinate riboside kinase
This is an abbreviated version!
For detailed information about nicotinate riboside kinase, go to the full flat file.
Reaction
Synonyms
More, NaR kinase, nicotinamide riboside kinase, nicotinamide riboside kinase 1, nicotinamide riboside kinase 2, nicotinic acid riboside kinase, nicotinic acid riboside kinase 1, NMRK1, NMRK2, NR kinase, Nrk, NRK1, Nrk2, ribosylnicotinic acid kinase
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Substrates Products
Substrates Products on EC 2.7.1.173 - nicotinate riboside kinase
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REACTION DIAGRAM
GTP + beta-D-ribosylnicotinate
GDP + nicotinate beta-D-ribonucleotide
nicotinic acid riboside is a specific substrate of human Nrk enzymes
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ADP + nicotinamide beta-D-ribonucleotide
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ATP + beta-D-ribosylnicotinamide
ADP + nicotinamide beta-D-ribonucleotide
beta-D-ribosylnicotinamide is an NAD+ precursor utilized via the Nrk and Preiss-Hander pathways
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ATP + beta-D-ribosylnicotinamide
ADP + nicotinamide beta-D-ribonucleotide
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ATP + beta-D-ribosylnicotinamide
ADP + nicotinamide beta-D-ribonucleotide
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ATP + beta-D-ribosylnicotinate
ADP + nicotinate beta-D-ribonucleotide
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ATP + beta-D-ribosylnicotinate
ADP + nicotinate beta-D-ribonucleotide
nicotinic acid riboside is a specific substrate of human Nrk enzymes
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ATP + beta-D-ribosylnicotinate
ADP + nicotinate beta-D-ribonucleotide
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ATP + beta-D-ribosylnicotinate
ADP + nicotinate beta-D-ribonucleotide
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conversion of beta-D-ribosylnicotinate into nicotinate mononucleotide by NaR kinase in cotyledons of mungbean seedlings
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ADP + nicotinamide mononucleotide phosphate
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ATP + nicotinamide mononucleotide
ADP + nicotinamide mononucleotide phosphate
binding mode of the substrate, overview
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Asp35 and Glu100 in Nrk2 are essential residues for function in vivo
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additional information
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Asp35 and Glu100 in Nrk2 are essential residues for function in vivo
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additional information
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Asp36 and Glu98 in Nrk1 are essential residues for function in vivo
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additional information
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Asp36 and Glu98 in Nrk1 are essential residues for function in vivo
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additional information
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substrate specificity of recombinant Nrk1 and Nrk2, overview. Classification of Nrk1 as an nicotinic acid riboside and tiazofurin:ATP or GTP kinase, Nrk1 displays a 340fold preference for nicotinic acid riboside over cytidine in the KM term and a 500fold preference over either cytidine or uridine in the kcat/KM term. Poor cytidine monophosphate-forming activity of the enzyme. Structural basis of substrate specificity, overview. Base recognition in the Nrk1 nucleoside-binding site excludes uridine but supports beta-D-ribosylnicotinamide phosphorylation
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additional information
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substrate specificity of recombinant Nrk1 and Nrk2, overview. Classification of Nrk1 as an nicotinic acid riboside and tiazofurin:ATP or GTP kinase, Nrk1 displays a 340fold preference for nicotinic acid riboside over cytidine in the KM term and a 500fold preference over either cytidine or uridine in the kcat/KM term. Poor cytidine monophosphate-forming activity of the enzyme. Structural basis of substrate specificity, overview. Base recognition in the Nrk1 nucleoside-binding site excludes uridine but supports beta-D-ribosylnicotinamide phosphorylation
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additional information
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substrate specificity of recombinant Nrk2, overview. Classification of Nrk2 as an ATP-specific nicotinic acid riboside, tiazofurin, and uridine kinase. Poor cytidine monophosphate-forming activity of the enzyme. Structural basis of substrate specificity, overview
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additional information
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substrate specificity of recombinant Nrk2, overview. Classification of Nrk2 as an ATP-specific nicotinic acid riboside, tiazofurin, and uridine kinase. Poor cytidine monophosphate-forming activity of the enzyme. Structural basis of substrate specificity, overview
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additional information
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the main NRK activity in human OVCAR-3 cells is due to the expression of enzyme NRK1
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additional information
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development of a highly sensitive, rapid and specific coupled enzymatic assay that allows simultaneous determination of NRK activitiy, as well as of nicotinic acid phosphoribosyltransferase, quinolinic acid phosphoribosyltransferase, and nicotinamide phosphoribosyltransferase activities, in various biological samples of various origins, evaluation and optimization using liver extracts, overview
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