Comparative characterisation of thiamin diphosphate-dependent decarboxylases

Dörte Gocke, Thorsten Graf, Helen Brosi, Ilona Frindi-Wosch, Lydia Walter, Michael Müller, Martina Pohl*

*Corresponding author for this work

Research output: Contribution to journalArticleResearchpeer-review

40 Citations (Scopus)


Several 2-keto acid decarboxylases catalyse an acyloin condensation-like carboligase reaction beside their physiological decarboxylase activity. Although many data concerning stability and catalytic potential of these enzymes are available, a standard evaluation under similar reaction conditions is lacking. In this comprehensive survey we assemble already published data combined with new studies of three bacterial pyruvate decarboxylases, yeast pyruvate decarboxylase, benzoylformate decarboxylase from Pseudomonas putida (BFD) and the branched-chain 2-keto acid decarboxylase from Lactococcus lactis (KdcA). The obtained results proof that the optima for activity and stability are rather similar if comparable reaction conditions are used. Although the substrate ranges of the decarboxylase reaction of the various pyruvate decarboxylases are similar as well, they differ remarkably from those of BFD and KdcA. We further show that the range of acceptable donor aldehydes for the carboligase reaction of a respective enzyme can be reliably predicted from the substrate range of decarboxylase reaction.

Original languageEnglish
Pages (from-to)30-35
Number of pages6
JournalJournal of Molecular Catalysis - B Enzymatic
Issue number1-2
Publication statusPublished - Nov 2009
Externally publishedYes


  • 2-Hydroxy ketones
  • Acetoin
  • Enzymatic carboligation
  • Enzymatic decarboxylation
  • Phenylacetylcarbinol


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