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Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to 1.65 A resolution.

ABSTRACT: 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.

SUBMITTER: Maraite A

PROVIDER: S-EPMC2335142 | biostudies-literature | 2007 Jul

REPOSITORIES: biostudies-literature

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Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to 1.65 A resolution.

Maraite Andy A Schmidt Thomas T Ansörge-Schumacher Marion B MB Brzozowski A Marek AM Grogan Gideon G

Acta crystallographica. Section F, Structural biology and crystallization communications 20070615 Pt 7

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 com ...[more]

PMID: 17620706

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