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

ECTree

     2 Transferases

         2.7 Transferring phosphorus-containing groups

             2.7.1 Phosphotransferases with an alcohol group as acceptor

                2.7.1.173 nicotinate riboside kinase

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Results	in table
12	AA Sequence
1	Application
6	Cloned(Commentary)
8	Cofactor
2	Crystallization (Commentary)
1	Expression
16	General Information
14	kcat/KM [mM/s]
14	KM Value [mM]
5	Metals/Ions
9	Natural Substrates/ Products (Substrates)
9	Organism
3	Pathway
1	PDB ID
3	pH Optimum
6	Protein Variants
4	Purification (Commentary)
2	Reaction
8	Reference
13	Source Tissue
1	Specific Activity [micromol/min/mg]
26	Substrates and Products (Substrate)
2	Subunits
27	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
14	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.7.1.173 - nicotinate riboside kinase

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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

Homo sapiens

Q9NPI5, Q9NWW6

718250

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, 22°C, 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

Homo sapiens

Q9NWW6

682879