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Publication Abstract from PubMed
Benzoylformate decarboxylase (BFD) from Pseudomonas putida is an exceptional thiamin diphosphate-dependent enzyme, as it catalyzes the formation of (S)-2-hydroxy-1-phenylpropan-1-one from benzaldehyde and acetaldehyde. This is the only currently known S-selective reaction (92 % ee) catalyzed by this otherwise R-selective class of enzymes. Here we describe the molecular basis of the introduction of S selectivity into ThDP-dependent decarboxylases. By shaping the active site of BFD through the use of rational protein design, structural analysis, and molecular modeling, optimal steric stabilization of the acceptor aldehyde in a structural element called the S pocket was identified as the predominant interaction for adjusting stereoselectivity. Our studies revealed Leu461 as a hot spot for stereoselectivity in BFD. Exchange to alanine and glycine resulted in variants that catalyze the S-stereoselective addition of larger acceptor aldehydes, such as propanal with benzaldehyde and its derivatives-a reaction not catalyzed by the wild-type enzyme. Crystal structure analysis of the variant BFDL461A supports the modeling studies.
Rational protein design of ThDP-dependent enzymes-engineering stereoselectivity.,Gocke D, Walter L, Gauchenova E, Kolter G, Knoll M, Berthold CL, Schneider G, Pleiss J, Muller M, Pohl M Chembiochem. 2008 Feb 15;9(3):406-12. PMID:18224647[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑Gocke D, Walter L, Gauchenova E, Kolter G, Knoll M, Berthold CL, Schneider G, Pleiss J, Muller M, Pohl M. Rational protein design of ThDP-dependent enzymes-engineering stereoselectivity. Chembiochem. 2008 Feb 15;9(3):406-12. PMID:18224647 doi:https://dx.doi.org/10.1002/cbic.200700598
