Open AccessStructure of the ThDP‐dependent enzyme benzaldehyde lyase refined to 1.65 Å resolution
Author(s) -
Maraite Andy,
Schmidt Thomas,
AnsörgeSchumacher Marion B.,
Brzozowski A. Marek,
Grogan Gideon
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107028576
Subject(s) - benzaldehyde , benzoin , chemistry , active site , stereochemistry , thiamine , enzyme , lyase , derivative (finance) , molecule , resolution (logic) , organic chemistry , catalysis , artificial intelligence , computer science , financial economics , economics
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 Å 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 ( P 2 1 2 1 2 1 ) and its structure refined to a resolution of 1.65 Å, 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.