title: CC bond formation using ThDP-dependent lyases.
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.
authors.affiliation: Institute of Pharmaceutical Sciences, Albert-Ludwigs-Universität Freiburg, Albertstr. 25, 79104 Freiburg, Germany. michael.mueller@pharmazie.uni-freiburg.de
authors.forename: Michael
authors.initials: M
authors.lastname: Müller
authors.forename: Georg A
authors.initials: GA
authors.lastname: Sprenger
authors.forename: Martina
authors.initials: M
authors.lastname: Pohl
mesh_terms: D000446:Aldehyde-Lyases / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism; D013831:Thiamine / Q000378:metabolism*; D013835:Thiamine Pyrophosphate / Q000378:metabolism*; D014174:Transketolase / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D014174:Transketolase; D000446:Aldehyde-Lyases; D013835:Thiamine Pyrophosphate; D013831:Thiamine