Assimilation of nicotinamide mononucleotide requires periplasmic AphA phosphatase in Salmonella enterica

Research output: Contribution to journalResearch articleContributedpeer-review

Contributors

  • Julianne H. Grose - , University of Utah (Author)
  • Ulfar Bergthorsson - , University of Utah, University of New Mexico (Author)
  • Yaping Xu - , University of Utah (Author)
  • Behzad Khodaverdian - , University of Utah (Author)
  • John R. Roth - , University of Utah, University of California at Davis (Author)
  • Jared Lynn Sterneckert - , University of Utah (Author)

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.

Details

Original languageEnglish
Pages (from-to)4521-4530
Number of pages10
JournalJournal of bacteriology
Volume187
Issue number13
Publication statusPublished - Jul 2005
Peer-reviewedYes
Externally publishedYes

External IDs

PubMed 15968063
ORCID /0000-0002-7688-3124/work/142250049

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