Ribosylnicotinamide kinase

Ribosylnicotinamide kinase
Identifiers
EC no.2.7.1.22
CAS no.9030-61-9
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Ribosylnicotinamide kinase (EC 2.7.1.22) is an enzyme that catalyzes the chemical reaction

The enzyme characterised from liver converts the riboside, nicotinamide riboside, to the ribonucleotide, nicotinamide mononucleotide, by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP).[1] The reaction is part of the biosynthetic pathway to the coenzyme, nicotinamide adenine dinucleotide.[2]

This enzyme is a transferase, specifically one transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:N-ribosylnicotinamide 5'-phosphotransferase. This enzyme is also called ribosylnicotinamide kinase (phosphorylating).[3]

Food

The enzyme can be found in milk[4] and beer. Since the molecules are difficult to detect, it is expected that there are a lot more food products containing ribosylnicotinamide kinase.

References

  1. ↑ Rowen, John W.; Kornberg, Arthur (1951). "The Phosphorolysis of Nicotinamide Riboside". Journal of Biological Chemistry. 193 (2): 497–507. doi:10.1016/S0021-9258(18)50905-4. PMID 14907738.
  2. ↑ Campbell, Michael T.D.; Jones, David S.; Andrews, Gavin P.; Li, Shu (2019). "Understanding the physicochemical properties and degradation kinetics of nicotinamide riboside, a promising vitamin B3nutritional supplement". Food & Nutrition Research. 63. doi:10.29219/fnr.v63.3419. PMC 6878970. PMID 31807125.
  3. ↑ Enzyme 2.7.1.22 at KEGG Pathway Database.
  4. ↑ Bieganowski, Pawel; Brenner, Charles (2004). "Discoveries of Nicotinamide Riboside as a Nutrient and Conserved NRK Genes Establish a Preiss-Handler Independent Route to NAD+ in Fungi and Humans". Cell. 117 (4): 495–502. doi:10.1016/S0092-8674(04)00416-7. PMID 15137942.