Enzymes
| UniProtKB help_outline | 8 proteins |
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- Name help_outline β-D-ribosylnicotinate Identifier CHEBI:58527 (Beilstein: 4154357) help_outline Charge 0 Formula C11H13NO6 InChIKeyhelp_outline PUEDDPCUCPRQNY-ZYUZMQFOSA-N SMILEShelp_outline OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)[n+]1cccc(c1)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ATP Identifier CHEBI:30616 (Beilstein: 3581767) help_outline Charge -4 Formula C10H12N5O13P3 InChIKeyhelp_outline ZKHQWZAMYRWXGA-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,284 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline nicotinate β-D-ribonucleotide Identifier CHEBI:57502 Charge -2 Formula C11H12NO9P InChIKeyhelp_outline JOUIQRNQJGXQDC-ZYUZMQFOSA-L SMILEShelp_outline O[C@H]1[C@@H](O)[C@@H](O[C@@H]1COP([O-])([O-])=O)[n+]1cccc(c1)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ADP Identifier CHEBI:456216 (Beilstein: 3783669) help_outline Charge -3 Formula C10H12N5O10P2 InChIKeyhelp_outline XTWYTFMLZFPYCI-KQYNXXCUSA-K SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 841 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:25568 | RHEA:25569 | RHEA:25570 | RHEA:25571 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Nicotinate riboside salvage in plants: presence of nicotinate riboside kinase in mungbean seedlings.
Matsui A., Ashihara H.
Salvage of nicotinate riboside for NAD synthesis was investigated in mungbean seedlings. Nicotinate riboside kinase activity was detected in extracts from cotyledons. Exogenously supplied [carboxyl-(14)C]nicotinate riboside was readily converted into pyridine nucleotides in cotyledons of mungbean ... >> More
Salvage of nicotinate riboside for NAD synthesis was investigated in mungbean seedlings. Nicotinate riboside kinase activity was detected in extracts from cotyledons. Exogenously supplied [carboxyl-(14)C]nicotinate riboside was readily converted into pyridine nucleotides in cotyledons of mungbean seedlings. This conversion was also found in embryonic axes, but the rate was lower than in cotyledons. These results suggest that, in addition to the seven-component pyridine nucleotide cycle (PNC VII), an eight-component cycle (PNC VIII) involving nicotinate riboside kinase operates in plants. << Less
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Nicotinamide riboside kinase structures reveal new pathways to NAD+.
Tempel W., Rabeh W.M., Bogan K.L., Belenky P., Wojcik M., Seidle H.F., Nedyalkova L., Yang T., Sauve A.A., Park H.-W., Brenner C.
The eukaryotic nicotinamide riboside kinase (Nrk) pathway, which is induced in response to nerve damage and promotes replicative life span in yeast, converts nicotinamide riboside to nicotinamide adenine dinucleotide (NAD+) by phosphorylation and adenylylation. Crystal structures of human Nrk1 bou ... >> More
The eukaryotic nicotinamide riboside kinase (Nrk) pathway, which is induced in response to nerve damage and promotes replicative life span in yeast, converts nicotinamide riboside to nicotinamide adenine dinucleotide (NAD+) by phosphorylation and adenylylation. Crystal structures of human Nrk1 bound to nucleoside and nucleotide substrates and products revealed an enzyme structurally similar to Rossmann fold metabolite kinases and allowed the identification of active site residues, which were shown to be essential for human Nrk1 and Nrk2 activity in vivo. Although the structures account for the 500-fold discrimination between nicotinamide riboside and pyrimidine nucleosides, no enzyme feature was identified to recognize the distinctive carboxamide group of nicotinamide riboside. Indeed, nicotinic acid riboside is a specific substrate of human Nrk enzymes and is utilized in yeast in a novel biosynthetic pathway that depends on Nrk and NAD+ synthetase. Additionally, nicotinic acid riboside is utilized in vivo by Urh1, Pnp1, and Preiss-Handler salvage. Thus, crystal structures of Nrk1 led to the identification of new pathways to NAD+. << Less
PLoS Biol. 5:2220-2230(2007) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Purification and properties of a human nicotinamide ribonucleoside kinase.
Sasiak K., Saunders P.P.
Nicotinamide ribonucleoside kinase (NRK) phosphorylates at least two nucleoside analogs of potential clinical interest, tiazofurin and 3-deazaguanosine. In this study NRK has been purified to near homogeneity from human placenta. The purification procedure consists of several chromatographic steps ... >> More
Nicotinamide ribonucleoside kinase (NRK) phosphorylates at least two nucleoside analogs of potential clinical interest, tiazofurin and 3-deazaguanosine. In this study NRK has been purified to near homogeneity from human placenta. The purification procedure consists of several chromatographic steps including salt precipitation, DE-52 chromatography, sucrose density gradient fractionation, hydroxylapatite chromatography, and anion exchange FPLC. The final enzyme preparation is homogeneous as judged by a single silver-stainable band on both nondenaturing and denaturing polyacrylamide gels. The molecular weight of the enzyme, as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration on Superdex 75 HR 10/30, is approximately 29 and 32 kDa, respectively. The isoelectric pH for NRK is 5.6. The reaction requires ATP. The pH optimum is in the region 6.5-9.0. NRK in the purified preparations, with added bovine serum albumin, was stable for days at 4 degrees C and for months at -70 degrees C. The enzyme is very unstable at low protein concentration. NRK phosphorylated several substrates including nicotinamide ribonucleoside, guanosine, tiazofurin, and 3-deazaguanosine with apparent Km values of 9.6, 115, 90, and 16.5 microM, respectively. << Less
Arch. Biochem. Biophys. 333:414-418(1996) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.