This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Cantoni, R.
Right arrow Articles by Riccardi, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cantoni, R.
Right arrow Articles by Riccardi, G.

 Previous Article  |  Next Article 

J Bacteriol, June 1998, p. 3218-3221, Vol. 180, No. 12
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

The MTCY428.08 Gene of Mycobacterium tuberculosis Codes for NAD+ Synthetase

Rita Cantoni,1 Manuela Branzoni,1 Monica Labò,1 Menico Rizzi,1,2 and Giovanna Riccardi1,*

Dipartimento di Genetica e Microbiologia, Università di Pavia, 27100 Pavia,1 and Dipartimento di Scienza e Tecnologia del Farmaco, Università di Torino, 10125 Torino,2 Italy

Received 23 February 1998/Accepted 10 April 1998

The product of the MTCY428.08 gene of Mycobacterium tuberculosis shows sequence homology with several NAD+ synthetases. The MTCY428.08 gene was cloned into the expression vectors pGEX-4T-1 and pET-15b. Expression in Escherichia coli led to overproduction of glutathione S-transferase fused and His6-tagged gene products, which were enzymatically assayed for NAD synthetase activity. Our results demonstrate that the MTCY428.08 gene of M. tuberculosis is the structural gene for NAD+ synthetase.

* Corresponding author. Mailing address: Dipartimento di Genetica e Microbiologia, Università di Pavia, via Abbiategrasso 207, 27100 Pavia, Italy. Phone: (39) 382 505 574. Fax: (39) 382 52 84 96. E-mail: Riccardi{at}ipvgen.unipv.it.

J Bacteriol, June 1998, p. 3218-3221, Vol. 180, No. 12
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Gazzaniga, F., Stebbins, R., Chang, S. Z., McPeek, M. A., Brenner, C. (2009). Microbial NAD Metabolism: Lessons from Comparative Genomics. Microbiol. Mol. Biol. Rev. 73: 529-541 [Abstract] [Full Text]  
  • Sorci, L., Martynowski, D., Rodionov, D. A., Eyobo, Y., Zogaj, X., Klose, K. E., Nikolaev, E. V., Magni, G., Zhang, H., Osterman, A. L. (2009). Nicotinamide mononucleotide synthetase is the key enzyme for an alternative route of NAD biosynthesis in Francisella tularensis. Proc. Natl. Acad. Sci. USA 106: 3083-3088 [Abstract] [Full Text]  
  • Wojcik, M., Seidle, H. F., Bieganowski, P., Brenner, C. (2006). Glutamine-dependent NAD+ Synthetase: HOW A TWO-DOMAIN, THREE-SUBSTRATE ENZYME AVOIDS WASTE. J. Biol. Chem. 281: 33395-33402 [Abstract] [Full Text]  
  • Jauch, R., Humm, A., Huber, R., Wahl, M. C. (2005). Structures of Escherichia coli NAD Synthetase with Substrates and Products Reveal Mechanistic Rearrangements. J. Biol. Chem. 280: 15131-15140 [Abstract] [Full Text]  
  • Veiga-Malta, I., Duarte, M., Dinis, M., Madureira, P., Ferreira, P., Videira, A. (2004). Identification of NAD+ Synthetase from Streptococcus sobrinus as a B-Cell-Stimulatory Protein. J. Bacteriol. 186: 419-426 [Abstract] [Full Text]  
  • Bieganowski, P., Pace, H. C., Brenner, C. (2003). Eukaryotic NAD+ Synthetase Qns1 Contains an Essential, Obligate Intramolecular Thiol Glutamine Amidotransferase Domain Related to Nitrilase. J. Biol. Chem. 278: 33049-33055 [Abstract] [Full Text]  
  • Bieganowski, P., Brenner, C. (2003). The Reported Human NADsyn2 Is Ammonia-dependent NAD Synthetase from a Pseudomonad. J. Biol. Chem. 278: 33056-33059 [Abstract] [Full Text]  
  • Hara, N., Yamada, K., Terashima, M., Osago, H., Shimoyama, M., Tsuchiya, M. (2003). Molecular Identification of Human Glutamine- and Ammonia-dependent NAD Synthetases. CARBON-NITROGEN HYDROLASE DOMAIN CONFERS GLUTAMINE DEPENDENCY. J. Biol. Chem. 278: 10914-10921 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»