Reshaping the active pocket of promiscuous lactonases for degrading bulky organophosphate flame retardants

Chem Commun (Camb). 2021 Jul 1;57(53):6475-6478. doi: 10.1039/d1cc02657g.

Abstract

Engineering of a promiscuous lactonase via semi-rational evolution gave a 1007-fold improvement in its catalytic activity in the degradation of triphenyl phosphate (TPHP). TPHP is a typical bulky organophosphate flame retardant (OPFR) and is widely used in industry. To the best of our knowledge, this is the first artificial enzyme capable of degrading OPFRs.

MeSH terms

  • Carboxylic Ester Hydrolases / chemistry*
  • Carboxylic Ester Hydrolases / genetics
  • Carboxylic Ester Hydrolases / metabolism*
  • Catalytic Domain*
  • Flame Retardants / metabolism*
  • Organophosphates / metabolism*
  • Protein Engineering
  • Substrate Specificity

Substances

  • Flame Retardants
  • Organophosphates
  • Carboxylic Ester Hydrolases