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Benzoylformate decarboxylase (BFDC) from Pseudomonas putida and pyruvate decarboxylase (PDC) from Zymomonas mobilis are thiamin diphosphate (ThDP)-dependent enzymes that carry out the non-oxidative decarboxylation of aromatic and aliphatic 2-keto carboxylic acids,respectively.Both enzymes also catalyze stereospecific carboligation reactions that are of commercial interest,again with a different range of substrates.In order to identify similarities and differences on a molecular level,and to reveal factors responsible for substrate specificity and enantioselectivity,the X-ray structures BFDC and PDC were compared.Residues identified in this process were subjected to site-directed mutagenesis.