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Title: Structural and Biochemical Characterization of Gentisate 1,2-Dioxygenase from Escherichia coli O157:H7.

Abstract

Gentisic acid (2,5-dihydroxybenzoic acid) is a key intermediate in aerobic bacterial pathways that are responsible for the metabolism of a large number of aromatic compounds. The critical step of these pathways is the oxygen-dependent reaction catalysed by gentisate 1,2-dioxygenase which opens the aromatic ring of gentisate to form maleylpyruvate. From gentisic acid, the cell derives carbon and energy through the conversion of maleylpyruvate to central metabolites. We have confirmed the annotation of a gentisate 1,2-dioygenase from the pathogenic O157:H7 Escherichia coli strain and present the first structural characterization of this family of enzymes. The identity of the reaction product was revealed using tandem mass spectroscopy. The operon responsible for the degradation of gentisate in this organism exhibits a high degree of conservation with the gentisate-degrading operons of other pathogenic bacteria, including the Shiga toxin-producing E. coli O103:H2, but does not appear to be present in non-pathogenic strains. The acquisition of the gentisate operon may represent a special adaptation to meet carbon source requirements under conditions of environmental stress and may provide a selective advantage for enterohaemorrhagic E. coli relative to their non-pathogenic counterparts.

Authors:
; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
929818
Report Number(s):
BNL-80373-2008-JA
TRN: US200822%%897
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Journal Name:
Molecular Microbiology
Additional Journal Information:
Journal Volume: 61
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; ESCHERICHIA COLI; OXYGENASES; MORPHOLOGY; BIOCHEMISTRY; BACTERIA; BIOLOGICAL PATHWAYS; METABOLISM; AROMATICS; national synchrotron light source

Citation Formats

Adams, M, Singh, V, Keller, B, and Jia, Z. Structural and Biochemical Characterization of Gentisate 1,2-Dioxygenase from Escherichia coli O157:H7.. United States: N. p., 2006. Web. doi:10.1111/j.1365-2958.2006.05334.x.
Adams, M, Singh, V, Keller, B, & Jia, Z. Structural and Biochemical Characterization of Gentisate 1,2-Dioxygenase from Escherichia coli O157:H7.. United States. doi:10.1111/j.1365-2958.2006.05334.x.
Adams, M, Singh, V, Keller, B, and Jia, Z. Sun . "Structural and Biochemical Characterization of Gentisate 1,2-Dioxygenase from Escherichia coli O157:H7.". United States. doi:10.1111/j.1365-2958.2006.05334.x.
@article{osti_929818,
title = {Structural and Biochemical Characterization of Gentisate 1,2-Dioxygenase from Escherichia coli O157:H7.},
author = {Adams, M and Singh, V and Keller, B and Jia, Z},
abstractNote = {Gentisic acid (2,5-dihydroxybenzoic acid) is a key intermediate in aerobic bacterial pathways that are responsible for the metabolism of a large number of aromatic compounds. The critical step of these pathways is the oxygen-dependent reaction catalysed by gentisate 1,2-dioxygenase which opens the aromatic ring of gentisate to form maleylpyruvate. From gentisic acid, the cell derives carbon and energy through the conversion of maleylpyruvate to central metabolites. We have confirmed the annotation of a gentisate 1,2-dioygenase from the pathogenic O157:H7 Escherichia coli strain and present the first structural characterization of this family of enzymes. The identity of the reaction product was revealed using tandem mass spectroscopy. The operon responsible for the degradation of gentisate in this organism exhibits a high degree of conservation with the gentisate-degrading operons of other pathogenic bacteria, including the Shiga toxin-producing E. coli O103:H2, but does not appear to be present in non-pathogenic strains. The acquisition of the gentisate operon may represent a special adaptation to meet carbon source requirements under conditions of environmental stress and may provide a selective advantage for enterohaemorrhagic E. coli relative to their non-pathogenic counterparts.},
doi = {10.1111/j.1365-2958.2006.05334.x},
journal = {Molecular Microbiology},
number = ,
volume = 61,
place = {United States},
year = {2006},
month = {1}
}