Synthesis of a heterogeneous artificial metallolipase with chimeric catalytic activity

Chem Commun (Camb). 2015 Jun 7;51(45):9324-7. doi: 10.1039/c5cc02450a.

Abstract

A solid-phase strategy using lipase as a biomolecular scaffold to produce a large amount of Cu(2+)-metalloenzyme is proposed here. The application of this protocol on different 3D cavities of the enzyme allows creating a heterogeneous artificial metallolipase showing chimeric catalytic activity. The artificial catalyst was assessed in Diels-Alder cycloaddition reactions and cascade reactions showing excellent catalytic properties.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalysis
  • Catalytic Domain
  • Lipase / chemical synthesis*
  • Lipase / chemistry
  • Metalloproteins / chemical synthesis*
  • Metalloproteins / chemistry
  • Models, Molecular

Substances

  • Metalloproteins
  • Lipase