TAILIEUCHUNG - Báo cáo khoa học: Structure and mechanism of the ThDP-dependent benzaldehyde lyase from Pseudomonas fluorescens

Pseudomonas fluorescensis able to grow on R-benzoin as the sole carbon and energy source because it harbours the enzyme benzaldehyde lyase that cleaves the acyloin linkage using thiamine diphosphate (ThDP) as a cofac-tor. In the reverse reaction, this lyase catalyses the carboligation of two aldehydes with high substrate and stereospecificity. | ềFEBS Journal Structure and mechanism of the ThDP-dependent benzaldehyde lyase from Pseudomonas fluorescens Tanja G. Mosbacher1 Michael Mueller2 and Georg E. Schulz1 1 Institut fur Organische Chemie und Biochemie Albert-Ludwigs-Universitat Freiburg im Breisgau Germany 2 Institut fur Pharmazeutische Wissenschaften Albert-Ludwigs-Universitat Freiburg im Breisgau Germany Keywords acyloin condensation carbon-carbon ligation crystal structure seleno-methionine MAD Correspondence G. E. Schulz Institut for Organische Chemie und Biochemie Albertstr. 21 Freiburg im Breisgau Germany 79104 Tel 49 761 203 6058 Fax 49 761 203 6161 Email Note After submission of this manuscript we received a preprint of the following paper reporting that the mutation of His29 to alanine reduces the BAL activity to 5 . Kneen MM Pogozheva ID Kenyon GL McLeish MJ 2005 Exploring the active site of benzaldehyde lyase by modeling and mutagenesis. Biochim Biophys Acta Proteins and Proteomics doi . Received 5 August 2005 revised 22 September 2005 accepted 29 September 2005 doi Pseudomonas fluorescens is able to grow on R-benzoin as the sole carbon and energy source because it harbours the enzyme benzaldehyde lyase that cleaves the acyloin linkage using thiamine diphosphate ThDP as a cofactor. In the reverse reaction this lyase catalyses the carboligation of two aldehydes with high substrate and stereospecificity. The enzyme structure was determined by X-ray diffraction at A resolution. A structure-based comparison with other proteins showed that benzaldehyde lyase belongs to a group of closely related ThDP-dependent enzymes. The ThDP cofactors of these enzymes are fixed at their two ends in separate domains suspending a comparatively mobile thiazolium ring between them. While the residues binding the two ends of ThDP are well conserved the lining of the active centre pocket around the thiazolium moiety .

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