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

Andy Maraite; Thomas Schmidt; Marion B. Ansoerge-Schumacher; A. Marek Brzozowski; Gideon Grogan

doi:10.1107/S1744309107028576

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

Andy Maraite, Thomas Schmidt, Marion B. Ansoerge-Schumacher, A. Marek Brzozowski, Gideon Grogan

Chemistry

Research output: Contribution to journal › Article › peer-review

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 angstrom 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 angstrom, 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.

Original language	English
Pages (from-to)	546-548
Number of pages	3
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	63
DOIs	https://doi.org/10.1107/S1744309107028576
Publication status	Published - Jul 2007

Keywords

ALPHA-HYDROXY KETONES
C BOND FORMATION
PSEUDOMONAS-FLUORESCENS
CRYSTALLIZATION
MODE

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10.1107/S1744309107028576

Cite this

@article{ed47279d05d94c25ad5127aa12e5542c,

title = "Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to 1.65 angstrom 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 angstrom 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 angstrom, 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.",

keywords = "ALPHA-HYDROXY KETONES, C BOND FORMATION, PSEUDOMONAS-FLUORESCENS, CRYSTALLIZATION, MODE",

author = "Andy Maraite and Thomas Schmidt and Ansoerge-Schumacher, {Marion B.} and Brzozowski, {A. Marek} and Gideon Grogan",

year = "2007",

month = jul,

doi = "10.1107/S1744309107028576",

language = "English",

volume = "63",

pages = "546--548",

journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

issn = "1744-3091",

publisher = "Wiley-Blackwell",

}

TY - JOUR

T1 - Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to 1.65 angstrom resolution

AU - Maraite, Andy

AU - Schmidt, Thomas

AU - Ansoerge-Schumacher, Marion B.

AU - Brzozowski, A. Marek

AU - Grogan, Gideon

PY - 2007/7

Y1 - 2007/7

N2 - 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 angstrom 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 angstrom, 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.

AB - 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 angstrom 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 angstrom, 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.

KW - ALPHA-HYDROXY KETONES

KW - C BOND FORMATION

KW - PSEUDOMONAS-FLUORESCENS

KW - CRYSTALLIZATION

KW - MODE

U2 - 10.1107/S1744309107028576

DO - 10.1107/S1744309107028576

M3 - Article

SN - 1744-3091

VL - 63

SP - 546

EP - 548

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

ER -