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2uz1

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{{STRUCTURE_2uz1| PDB=2uz1 | SCENE= }}
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'''1.65 ANGSTROM STRUCTURE OF BENZALDEHYDE LYASE COMPLEXED WITH 2-METHYL-2,4-PENTANEDIOL'''
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===1.65 ANGSTROM STRUCTURE OF BENZALDEHYDE LYASE COMPLEXED WITH 2-METHYL-2,4-PENTANEDIOL===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_17620706}}
==About this Structure==
==About this Structure==
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[[Category: Thiamine diphosphate]]
[[Category: Thiamine diphosphate]]
[[Category: Thiamine pyrophosphate]]
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Revision as of 01:03, 29 July 2008

Image:2uz1.png

Template:STRUCTURE 2uz1

1.65 ANGSTROM STRUCTURE OF BENZALDEHYDE LYASE COMPLEXED WITH 2-METHYL-2,4-PENTANEDIOL

Template:ABSTRACT PUBMED 17620706

About this Structure

2UZ1 is a Single protein structure of sequence from Pseudomonas fluorescens. Full crystallographic information is available from OCA.

Reference

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 Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jul 1;63(Pt, 7):546-8. Epub 2007 Jun 15. PMID:17620706

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