Structure of the Thdp-dependent Enzyme Benzaldehyde Lyase Refined to 1.65 A Resolution.
From: Department of Biotechnology, Faculty of Natural Sciences, RWTH Aachen University, Worringerweg 1, 52074 Aachen, Germany.
Acta crystallographica. Section F, Structural biology and crystallization communications
- Publish Date: Jul 2007
- ISSN: 1744-3091
- Volume: 63
- Issue: Pt 7
- Pages: 546-8
- Medium: Internet
- Language: English
- Citation (JAMA): Maraite Andy, Schmidt Thomas, Ansörge-Schumacher Marion B, et al. Structure of the Thdp-dependent Enzyme Benzaldehyde Lyase Refined to 1.65 A Resolution.. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. Jul 2007;63:546-8
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.
Mesh Headings (Keywords): Aldehyde-Lyases, Binding Sites, Crystallography, X-Ray, Protein Conformation, Protein Structure, Secondary, Thiamine Pyrophosphate
Check for Full Text / PubMed Unique Identifier (PMID): 17620706
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