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Gene Review

NADSYN1  -  NAD synthetase 1

Homo sapiens

Synonyms: FLJ10631, Glutamine-dependent NAD(+) synthetase, NAD(+) synthetase
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High impact information on NADSYN1

  • The overexpression of YK1 in both suspension-cultured cells and rice plants increased NAD(H) and NADP(H) levels by causing an increase in NAD synthetase and NAD kinase activities [1].
  • The incubation of intact red blood cells with lead followed by rigorous washing to remove lead abolished nearly all NAD synthetase activity [2].
  • The enzyme was found to be cold labile and extremely unstable in crude hemolysate, with complete loss of activity occurring after 24 hours at 4 degrees C. However, maintenance of crude hemolysate at 20 to 25 degrees C in the presence of EDTA and KCl increased NAD synthetase stability substantially (half-life = 10 days) [2].
  • Using these conditions, NAD synthetase was purified 3,100-fold with a 29% yield using DEAE-cellulose column chromatography, ammonium sulfate fractionation, and dialysis [2].
  • Our results also indicate that the carbon-nitrogen hydrolase domain is the functional domain of NAD synthetase to make use of glutamine as an amide donor in NAD synthesis [3].

Biological context of NADSYN1

  • Therefore, we conclude that humans have two types of NAD synthetase exhibiting different amide donor specificity and tissue distributions [3].

Associations of NADSYN1 with chemical compounds


Other interactions of NADSYN1

  • METHODS: We developed an ammonia assay using a system consisting of three enzymes, NAD synthetase (NADS; EC, glucose dehydrogenase (GlcDH; EC, and diaphorase (DI; EC [6].


  1. Enhanced dihydroflavonol-4-reductase activity and NAD homeostasis leading to cell death tolerance in transgenic rice. Hayashi, M., Takahashi, H., Tamura, K., Huang, J., Yu, L.H., Kawai-Yamada, M., Tezuka, T., Uchimiya, H. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  2. Partial purification and properties of nicotinamide adenine dinucleotide synthetase from human erythrocytes: evidence that enzyme activity is a sensitive indicator of lead exposure. Zerez, C.R., Wong, M.D., Tanaka, K.R. Blood (1990) [Pubmed]
  3. Molecular identification of human glutamine- and ammonia-dependent NAD synthetases. Carbon-nitrogen hydrolase domain confers glutamine dependency. Hara, N., Yamada, K., Terashima, M., Osago, H., Shimoyama, M., Tsuchiya, M. J. Biol. Chem. (2003) [Pubmed]
  4. Hypoxanthine-guanine phosphoribosyltransferase deficiency and erythrocyte synthesis of pyridine coenzymes. Micheli, V., Sestini, S., Rocchigiani, M., Jacomelli, G., Manzoni, F., Peruzzi, L., Gathof, B.S., Zammarchi, E., Pompucci, G. Life Sci. (1999) [Pubmed]
  5. A fluorescence-based coupling reaction for monitoring the activity of recombinant human NAD synthetase. Bembenek, M.E., Kuhn, E., Mallender, W.D., Pullen, L., Li, P., Parsons, T. Assay and drug development technologies. (2005) [Pubmed]
  6. A new enzymatic cycling method for ammonia assay using NAD synthetase. Yamaguchi, F., Etoh, T., Takahashi, M., Misaki, H., Sakuraba, H., Ohshima, T. Clin. Chim. Acta (2005) [Pubmed]
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