2uz1: Difference between revisions
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==Overview== | ==Overview== | ||
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, | 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. | ||
==About this Structure== | ==About this Structure== | ||
2UZ1 is a | 2UZ1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens] with TPP and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Benzoin_aldolase Benzoin aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.38 4.1.2.38] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2UZ1 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: thiamine pyrophosphate]] | [[Category: thiamine pyrophosphate]] | ||
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Revision as of 14:06, 5 November 2007
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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, 2-methyl-2,4-pentanediol (MPD) at hydrophobic patches of the enzyme, surface.
About this StructureAbout this Structure
2UZ1 is a Single protein structure of sequence from Pseudomonas fluorescens with TPP and MPD as ligands. Active as Benzoin aldolase, with EC number 4.1.2.38 Structure known Active Site: AC1. 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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