# Structural and functional characterization of sulfurtransferase from Frondihabitans sp. PAMC28461

## TL;DR

This study identifies and characterizes a sulfurtransferase from Frondihabitans sp. PAMC28461, showing it functions as a TST with potential industrial uses.

## Contribution

The novel contribution is the structural and functional characterization of FrST as a TST with broad substrate specificity and thermal stability.

## Key findings

- FrST is a dimeric TST, not an MST, based on sequence clustering and enzyme activity.
- FrST exhibits activity across a wide temperature range and broad substrate specificity.
- FrST shows potential for industrial applications, such as cyanide detoxification.

## 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.