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Biochemical and structural investigations on phosphoribosylpyrophosphate synthetase from Mycobacterium smegmatis.

Abstract Mycobacterium smegmatis represents one model for studying the biology of its pathogenic relative Mycobacterium tuberculosis. The structural characterization of a M. tuberculosis ortholog protein can serve as a valid tool for the development of molecules active against the M. tuberculosis target. In this context, we report the biochemical and structural characterization of M. smegmatis phosphoribosylpyrophosphate synthetase (PrsA), the ortholog of M. tuberculosis PrsA, the unique enzyme responsible for the synthesis of phosphoribosylpyrophosphate (PRPP). PRPP is a key metabolite involved in several biosynthetic pathways including those for histidine, tryptophan, nucleotides and decaprenylphosphoryl-arabinose, an essential precursor for the mycobacterial cell wall biosynthesis. Since M. tuberculosis PrsA has been validated as a drug target for the development of antitubercular agents, the data presented here will add to the knowledge of the mycobacterial enzyme and could contribute to the development of M. tuberculosis PrsA inhibitors of potential pharmacological interest.
PMID
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Authors

Mayor MeshTerms
Keywords
Journal Title plos one
Publication Year Start




PMID- 28419153
OWN - NLM
STAT- In-Process
DA  - 20170418
LR  - 20170418
IS  - 1932-6203 (Electronic)
IS  - 1932-6203 (Linking)
VI  - 12
IP  - 4
DP  - 2017
TI  - Biochemical and structural investigations on phosphoribosylpyrophosphate
      synthetase from Mycobacterium smegmatis.
PG  - e0175815
LID - 10.1371/journal.pone.0175815 [doi]
AB  - Mycobacterium smegmatis represents one model for studying the biology of its
      pathogenic relative Mycobacterium tuberculosis. The structural characterization
      of a M. tuberculosis ortholog protein can serve as a valid tool for the
      development of molecules active against the M. tuberculosis target. In this
      context, we report the biochemical and structural characterization of M.
      smegmatis phosphoribosylpyrophosphate synthetase (PrsA), the ortholog of M.
      tuberculosis PrsA, the unique enzyme responsible for the synthesis of
      phosphoribosylpyrophosphate (PRPP). PRPP is a key metabolite involved in several 
      biosynthetic pathways including those for histidine, tryptophan, nucleotides and 
      decaprenylphosphoryl-arabinose, an essential precursor for the mycobacterial cell
      wall biosynthesis. Since M. tuberculosis PrsA has been validated as a drug target
      for the development of antitubercular agents, the data presented here will add to
      the knowledge of the mycobacterial enzyme and could contribute to the development
      of M. tuberculosis PrsA inhibitors of potential pharmacological interest.
FAU - Donini, Stefano
AU  - Donini S
AD  - Department of Pharmaceutical Sciences, Universita del Piemonte Orientale "A.
      Avogadro", Largo Donegani 2, Novara, Italy.
FAU - Garavaglia, Silvia
AU  - Garavaglia S
AD  - Department of Pharmaceutical Sciences, Universita del Piemonte Orientale "A.
      Avogadro", Largo Donegani 2, Novara, Italy.
FAU - Ferraris, Davide M
AU  - Ferraris DM
AD  - Department of Pharmaceutical Sciences, Universita del Piemonte Orientale "A.
      Avogadro", Largo Donegani 2, Novara, Italy.
FAU - Miggiano, Riccardo
AU  - Miggiano R
AD  - Department of Pharmaceutical Sciences, Universita del Piemonte Orientale "A.
      Avogadro", Largo Donegani 2, Novara, Italy.
FAU - Mori, Shigetarou
AU  - Mori S
AD  - Department of Bacteriology II, National Institute of Infectious Diseases, Gakuen 
      4-7-1, Musashimurayama-shi, Tokyo, Japan.
FAU - Shibayama, Keigo
AU  - Shibayama K
AD  - Department of Bacteriology II, National Institute of Infectious Diseases, Gakuen 
      4-7-1, Musashimurayama-shi, Tokyo, Japan.
FAU - Rizzi, Menico
AU  - Rizzi M
AUID- ORCID: http://orcid.org/0000-0002-7930-399X
AD  - Department of Pharmaceutical Sciences, Universita del Piemonte Orientale "A.
      Avogadro", Largo Donegani 2, Novara, Italy.
LA  - eng
PT  - Journal Article
DEP - 20170418
PL  - United States
TA  - PLoS One
JT  - PloS one
JID - 101285081
EDAT- 2017/04/19 06:00
MHDA- 2017/04/19 06:00
CRDT- 2017/04/19 06:00
PHST- 2017/01/13 [received]
PHST- 2017/03/31 [accepted]
AID - 10.1371/journal.pone.0175815 [doi]
AID - PONE-D-17-01688 [pii]
PST - epublish
SO  - PLoS One. 2017 Apr 18;12(4):e0175815. doi: 10.1371/journal.pone.0175815.
      eCollection 2017.

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