Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to 1.65 A resolution.
Benzaldehyde lyase (BAL; EC 4.1.2.38) is a thiamine diphosphate (ThDP) dependent enzyme that catalyses the enantioselective carboligation of two molecules of benzaldehyde to form (R)-benzoin. BAL has hence aroused interest for its potential in the industrial synthesis of optically active benzoins and derivatives. The structure of BAL was previously solved to a resolution of 2.6 A using MAD experiments on a selenomethionine derivative [Mosbacher et al. (2005), FEBS J. 272, 6067-6076]. In this communication of parallel studies, BAL was crystallized in an alternative space group (P2(1)2(1)2(1)) and its structure refined to a resolution of 1.65 A, allowing detailed observation of the water structure, active-site interactions with ThDP and also the electron density for the co-solvent 2-methyl-2,4-pentanediol (MPD) at hydrophobic patches of the enzyme surface.
Maraite
Andy
A
Department of Biotechnology, Faculty of Natural Sciences, RWTH Aachen University, Worringerweg 1, 52074 Aachen, Germany.
Schmidt
Thomas
T
Ansörge-Schumacher
Marion B
MB
Brzozowski
A Marek
AM
Grogan
Gideon
G
D000446:Aldehyde-Lyases / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013835:Thiamine Pyrophosphate / Q000737:chemistry* / Q000378:metabolism
D000446:Aldehyde-Lyases; C059416:benzaldehyde lyase; D013835:Thiamine Pyrophosphate