Structural and functional study of SaAcP, an acylphosphatase from Staphylococcus aureus

Kyu Yeon Lee, Dong Gyun Kim, Ki Young Lee, Chinar Pathak, Ji Sung Koo, Hee Chul Ahn, Bong Jin Lee

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

Acylphosphatase is the smallest enzyme that is widely distributed in many diverse organisms ranging from archaebacteria to higher-eukaryotes including the humans. The enzyme hydrolyzes the carboxyl-phosphate bonds of the acyl phosphates which are important intermediates in glycolysis, membrane pumps, tricarboxylic acid cycle, and urea biosynthesis. Despite its biological importance in critical cellular functions, very limited structural investigations have been conducted on bacterial acylphosphatases. Here, we first unveiled the crystal structure of SaAcP, an acylphosphatase from gram-positive S. aureus at the atomic level. Structural insights on the active site together with mutation study provided greater understanding of the catalytic mechanism of SaAcP as a bacterial acylphosphatase and as a putative apyrase. Furthermore, through NMR titration experiment of SaAcP in its solution state, the dynamics and the alterations of residues affected by the phosphate ion were validated. Our findings elucidate the structure-function relationship of acylphosphatases in gram-positive bacteria and will provide a valuable basis for researchers in the field related to bacterial acylphosphatases.

Original languageEnglish
Pages (from-to)173-178
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume532
Issue number2
DOIs
StatePublished - 5 Nov 2020

Keywords

  • Acylphosphatase
  • NMR spectroscopy
  • Staphylococcus aureus
  • X-ray crystallography

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