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Gene Review:

nadE - NAD synthetase, NH3/glutamine-dependent

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK1738, JW1729, efg, ntrL

Willison, J.C. et al., Yamaguchi, F. et al., Tesmer, J.J. et al., Gerdes, S.Y. et al., Nessi, C. et al., et al.

Yamaguchi, Koga, Yoshioka, Takahashi, Sakuraba, Ohshima,

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Disease relevance of nadE

This gene, designated nadE, is located between gdh and nit at 27 min on the Salmonella typhimurium chromosome [1].
Structures of Escherichia coli NAD synthetase with substrates and products reveal mechanistic rearrangements [2].
The Escherichia coli efg gene and the Rhodobacter capsulatus adgA gene code for NH3-dependent NAD synthetase [3].
The outB gene of Bacillus subtilis codes for NAD synthetase [4].
Stable ammonia-specific NAD synthetase from Bacillus stearothermophilus: purification, characterization, gene cloning, and applications [5].

High impact information on nadE

The structure and conserved sequence fingerprint of the nucleotide-binding site in a second domain of GMP synthetase are common to a family of ATP pyrophosphatases, including NAD synthetase, asparagine synthetase and argininosuccinate synthetase [6].
Here we report experiments showing that OutB is a NH3-dependent NAD synthetase, the enzyme that catalyzes the final reaction in the biosynthesis of NAD [4].
(i) The product of the slr1691 gene, a homolog of Escherichia coli gene nadE containing an additional nitrilase-like N-terminal domain, is a NAD synthetase capable of utilizing glutamine as an amide donor in vitro [7].
The essential gene efg, which complements ammonia-dependent growth (adgA) mutations in Rhodobacter capsulatus and is located at 38.1 min on the Escherichia coli chromosome, was found to code for NH3-dependent NAD synthetase [3].
Bacillus stearothermophilus H-804 isolated from a hot spring in Beppu, Japan, produced an ammonia-specific NAD synthetase (EC 6.3.1.5) [5].

Chemical compound and disease context of nadE

Glutamine-dependent NAD synthetase activity was found in crude extracts of E. coli but not in the purified enzyme, suggesting that it may be catalyzed by an additional subunit [3].

Analytical, diagnostic and therapeutic context of nadE

Structural study of Escherichia coli NAD synthetase: overexpression, purification, crystallization, and preliminary crystallographic analysis [8].

References

Structural gene for NAD synthetase in Salmonella typhimurium. Hughes, K.T., Olivera, B.M., Roth, J.R. J. Bacteriol. (1988) [Pubmed]
Structures of Escherichia coli NAD synthetase with substrates and products reveal mechanistic rearrangements. Jauch, R., Humm, A., Huber, R., Wahl, M.C. J. Biol. Chem. (2005) [Pubmed]
The Escherichia coli efg gene and the Rhodobacter capsulatus adgA gene code for NH3-dependent NAD synthetase. Willison, J.C., Tissot, G. J. Bacteriol. (1994) [Pubmed]
The outB gene of Bacillus subtilis codes for NAD synthetase. Nessi, C., Albertini, A.M., Speranza, M.L., Galizzi, A. J. Biol. Chem. (1995) [Pubmed]
Stable ammonia-specific NAD synthetase from Bacillus stearothermophilus: purification, characterization, gene cloning, and applications. Yamaguchi, F., Koga, S., Yoshioka, I., Takahashi, M., Sakuraba, H., Ohshima, T. Biosci. Biotechnol. Biochem. (2002) [Pubmed]
The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. Tesmer, J.J., Klem, T.J., Deras, M.L., Davisson, V.J., Smith, J.L. Nat. Struct. Biol. (1996) [Pubmed]
Comparative genomics of NAD biosynthesis in cyanobacteria. Gerdes, S.Y., Kurnasov, O.V., Shatalin, K., Polanuyer, B., Sloutsky, R., Vonstein, V., Overbeek, R., Osterman, A.L. J. Bacteriol. (2006) [Pubmed]
Structural study of Escherichia coli NAD synthetase: overexpression, purification, crystallization, and preliminary crystallographic analysis. Ozment, C., Barchue, J., DeLucas, L.J., Chattopadhyay, D. J. Struct. Biol. (1999) [Pubmed]

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