Structural and functional characterization of sulfurtransferase from Frondihabitans sp. PAMC28461

PLoS One. 2024 Mar 25;19(3):e0298999. doi: 10.1371/journal.pone.0298999. eCollection 2024.

Abstract

Sulfurtransferases transfer of sulfur atoms from thiols to acceptors like cyanide. They are categorized as thiosulfate sulfurtransferases (TSTs) and 3-mercaptopyruvate sulfurtransferases (MSTs). TSTs transfer sulfur from thiosulfate to cyanide, producing thiocyanate. MSTs transfer sulfur from 3-mercaptopyruvate to cyanide, yielding pyruvate and thiocyanate. The present study aimed to isolate and characterize the sulfurtransferase FrST from Frondihabitans sp. PAMC28461 using biochemical and structural analyses. FrST exists as a dimer and can be classified as a TST rather than an MST according to sequence-based clustering and enzyme activity. Furthermore, the discovery of activity over a wide temperature range and the broad substrate specificity exhibited by FrST suggest promising prospects for its utilization in industrial applications, such as the detoxification of cyanide.

MeSH terms

  • Cyanides
  • Cysteine / analogs & derivatives*
  • Pyruvic Acid
  • Sulfur
  • Sulfurtransferases / chemistry
  • Thiocyanates*
  • Thiosulfate Sulfurtransferase
  • Thiosulfates*

Substances

  • thiocyanate
  • Thiocyanates
  • 3-mercaptopyruvic acid
  • Thiosulfates
  • Sulfurtransferases
  • Thiosulfate Sulfurtransferase
  • Pyruvic Acid
  • Cyanides
  • Sulfur
  • Cysteine

Grants and funding

This research was part of the project titled “Development of potential antibiotic compounds using polar organism resources (20200610)” funded by the Ministry of Oceans and Fisheries, Korea. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.