Enzymes
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- Name help_outline β-nicotinamide D-riboside Identifier CHEBI:15927 (Beilstein: 3912857; CAS: 1341-23-7) help_outline Charge 1 Formula C11H15N2O5 InChIKeyhelp_outline JLEBZPBDRKPWTD-TURQNECASA-O SMILEShelp_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:33163 | RHEA:33164 | RHEA:33165 | RHEA:33166 | |
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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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Assimilation of nicotinamide mononucleotide requires periplasmic AphA phosphatase in Salmonella enterica.
Grose J.H., Bergthorsson U., Xu Y., Sterneckert J., Khodaverdian B., Roth J.R.
Salmonella enterica can obtain pyridine from exogenous nicotinamide mononucleotide (NMN) by three routes. In route 1, nicotinamide is removed from NMN in the periplasm and enters the cell as the free base. In route 2, described here, phosphate is removed from NMN in the periplasm by acid phosphata ... >> More
Salmonella enterica can obtain pyridine from exogenous nicotinamide mononucleotide (NMN) by three routes. In route 1, nicotinamide is removed from NMN in the periplasm and enters the cell as the free base. In route 2, described here, phosphate is removed from NMN in the periplasm by acid phosphatase (AphA), and the produced nicotinamide ribonucleoside (NmR) enters the cell via the PnuC transporter. Internal NmR is then converted back to NMN by the NmR kinase activity of NadR. Route 3 is seen only in pnuC* transporter mutants, which import NMN intact and can therefore grow on lower levels of NMN. Internal NMN produced by either route 2 or route 3 is deamidated to nicotinic acid mononucleotide and converted to NAD by the biosynthetic enzymes NadD and NadE. << Less
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Crystal structure of the vitamin B3 transporter PnuC, a full-length SWEET homolog.
Jaehme M., Guskov A., Slotboom D.J.
PnuC transporters catalyze cellular uptake of the NAD+ precursor nicotinamide riboside (NR) and belong to a large superfamily that includes the SWEET sugar transporters. We present a crystal structure of Neisseria mucosa PnuC, which adopts a highly symmetrical fold with 3+1+3 membrane topology not ... >> More
PnuC transporters catalyze cellular uptake of the NAD+ precursor nicotinamide riboside (NR) and belong to a large superfamily that includes the SWEET sugar transporters. We present a crystal structure of Neisseria mucosa PnuC, which adopts a highly symmetrical fold with 3+1+3 membrane topology not previously observed in any protein. The high symmetry of PnuC with a single NR bound in the center suggests a simple alternating-access translocation mechanism. << Less
Nat. Struct. Mol. Biol. 21:1013-1015(2014) [PubMed] [EuropePMC]