Optically active &amp / #945 / -hydroxy ketones are important subunits of many biologically active compounds and indispensable synthons for asymmetric synthesis. Benzaldehyde Lyase from Pseudomonas fluorescens Biovar I is a novel ThDP-dependent enzyme that catalyzes the synthesis of benzoin type chiral &amp / #945 / -hydroxy ketones starting from both benzaldehyde and racemic benzoin derivatives. Benzaldehyde Lyase is the first example of enzymes in the literature which leads to a chemical resolution of enantiomers of benzoin derivatives through a C-C bond cleavage reaction. Chiral 2-hydroxypropiophenone derivatives are formed by benzaldehyde lyase (BAL), catalyzing C-C bond formation after a selective C-C bond cleavage of a benzoin derivative accepted as a substrate. The enzyme uses only the (R)-benzoin derivatives as substrate for the formation of (R)-HPP derivatives and it is highly stereoselective. Thus, in the presence of the acetaldehyde as the acceptor aldehyde, the C-C bond cleavage of the benzoin molecule followed by the carboligation of the acetaldehyde to yield chiral 2-hydroxy propiophenone derivatives. Given the racemic benzoin to the enzyme as the substrate in the presence of acetaldehyde, both the racemic resolution of the substrate, revealing the unreacted (S)-Benzoin and the formation of the corresponding R-HPP occur.