CC bond formation using ThDP-dependent lyases

Curr Opin Chem Biol. 2013 Apr;17(2):261-70. doi: 10.1016/j.cbpa.2013.02.017. Epub 2013 Mar 20.

Abstract

The present review summarizes recent achievements in enzymatic thiamine catalysis during the past three years. With well-established enzymes such as BAL, PDC and TK new reactions have been identified and respective variants were prepared, which enable access to stereoisomeric products. Further we highlight recent progress with 'new' ThDP-dependent enzymes like MenD and PigD, which catalyze the Stetter-like 1,4 addition of aldehydes and YerE, which is the first known ThDP-dependent enzyme accepting ketones as acceptors.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Aldehyde-Lyases / metabolism*
  • Bacterial Proteins / metabolism
  • Thiamine / metabolism*
  • Thiamine Pyrophosphate / metabolism*
  • Transketolase / metabolism

Substances

  • Bacterial Proteins
  • Transketolase
  • Aldehyde-Lyases
  • Thiamine Pyrophosphate
  • Thiamine