2uz1
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1.65 ANGSTROM STRUCTURE OF BENZALDEHYDE LYASE COMPLEXED WITH 2-METHYL-2,4-PENTANEDIOL
OverviewOverview
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, ... [(full description)]
About this StructureAbout this Structure
2UZ1 is a [Single protein] structure of sequence from [Pseudomonas fluorescens] with TPP and MPD as [ligands]. Active as [[1]], with EC number [4.1.2.38]. Full crystallographic information is available from [OCA].
ReferenceReference
Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to 1.65 A resolution., Maraite A, Schmidt T, Ansorge-Schumacher MB, Brzozowski AM, Grogan G, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2007 Jul 1;63(Pt, 7):546-8. Epub 2007 Jun 15. PMID:17620706
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