Ribosylnicotinamide kinase

Part of the Springer Handbook of Enzymes book series (HDBKENZYMES, volume 35)


EC number

Systematic name

ATP:N-ribosylnicotinamide 5′-phosphotransferase

Recommended name

ribosylnicotinamide kinase


NadR <3, 4, 5> [3]

kinase, ribosylnicotinamide (phosphorylating)

CAS registry number



Escherichia Coli Molecular Weight Crystal Structure Kinase Activity Veterinary Medicine 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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  1. [1]
    Rowen, J.W.; Kornberg, A.: The phosphorolysis of nicotinamide riboside. J. Biol. Chem., 193, 497–507 (1951)PubMedGoogle Scholar
  2. [2]
    Singh, S.K.; Kurnasov, O.V.; Chen, B.; Robinson, H.; Grishin, N.V.; Osterman, A.L.; Zhang, H.: Crystal structure of Haemophilus influenzae NadR protein. A bifunctional enzyme endowed with NMN adenyltransferase and ribosylnicotinimide kinase activities. J. Biol. Chem., 277, 33291–33299 (2002)PubMedCrossRefGoogle Scholar
  3. [3]
    Kurnasov, O.V.; Polanuyer, B.M.; Ananta, S.; Sloutsky, R.; Tam, A.; Gerdes, S.Y.; Osterman, A.L.: Ribosylnicotinamide kinase domain of NadR protein: identification and implications in NAD biosynthesis. J. Bacteriol., 184, 6906–6917 (2002)PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2007

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