Assimilation of nicotinamide mononucleotide requires periplasmic AphA phosphatase in Salmonella enterica

Julianne H. Grose, Ulfar Bergthorsson, Yaping Xu, Jared Sterneckert, Behzad Khodaverdian, John R. Roth

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21 Scopus citations

Abstract

Salmonella enterica can obtain pyridine from exogenous nicotinamide mononucleotide (NMN) by three routes. In route 1, nicotinamide is removed from NMN in the periplasm and enters the cell as the free base. In route 2, described here, phosphate is removed from NMN in the periplasm by acid phosphatase (AphA), and the produced nicotinamide ribonucleoside (NmR) enters the cell via the PnuC* transporter. Internal NmR is then converted back to NMN by the NmR kinase activity of NadR. Route 3 is seen only in pnuC* transporter mutants, which import NMN intact and can therefore grow on lower levels of NMN. Internal NMN produced by either route 2 or route 3 is deamidated to nicotinic acid mononucleotide and converted to NAD by the biosynthetic enzymes NadD and NadE.

Original languageEnglish (US)
Pages (from-to)4521-4530
Number of pages10
JournalJournal of Bacteriology
Volume187
Issue number13
DOIs
StatePublished - Jul 2005

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ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

Grose, J. H., Bergthorsson, U., Xu, Y., Sterneckert, J., Khodaverdian, B., & Roth, J. R. (2005). Assimilation of nicotinamide mononucleotide requires periplasmic AphA phosphatase in Salmonella enterica. Journal of Bacteriology, 187(13), 4521-4530. https://doi.org/10.1128/JB.187.13.4521-4530.2005