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Structure and mechanism of HpcH : a metal ion dependent class II aldolase from the homoprotocatechuate degradation pathway of Escherichia coli
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Rea, Dean, Fülöp, Vilmos, Bugg, Tim and Roper, David I. (2007) Structure and mechanism of HpcH : a metal ion dependent class II aldolase from the homoprotocatechuate degradation pathway of Escherichia coli. Journal of Molecular Biology, Vol.373 (No.4). pp. 866-876. doi:10.1016/j.jmb.2007.06.048 ISSN 0022-2836.
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Official URL: http://dx.doi.org/10.1016/j.jmb.2007.06.048
Abstract
Microorganisms are adept at degrading chemically resistant aromatic compounds. One of the longest and most well characterized aromatic catabolic pathways is the 4-hydroxyphenylacetic acid degradation pathway of Escherichia coli. The final step involves the conversion of 4-hydroxy-2-oxoheptane-1,7-dioate into pyruvate and succinic semialdehyde. This reaction is catalyzed by 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (HpcH), a member of the divalent metal ion dependent class 11 aldolase enzymes that have great biosynthetic potential. We have solved the crystal structure of HpcH in the apo form, and with magnesium and the substrate analogue oxamate bound, to 1.6 angstrom and 2.0 angstrom, respectively. Comparison with similar structures of the homologous 2-dehydro-3-deoxygalactarate aldolase, coupled with site-directed mutagenesis data, implicate histidine 45 and arginine 70 as key catalytic residues.
Item Type: | Journal Article | ||||
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Subjects: | Q Science > QD Chemistry | ||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) |
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Journal or Publication Title: | Journal of Molecular Biology | ||||
Publisher: | Academic Press | ||||
ISSN: | 0022-2836 | ||||
Official Date: | 2 November 2007 | ||||
Dates: |
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Volume: | Vol.373 | ||||
Number: | No.4 | ||||
Number of Pages: | 11 | ||||
Page Range: | pp. 866-876 | ||||
DOI: | 10.1016/j.jmb.2007.06.048 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access |
Data sourced from Thomson Reuters' Web of Knowledge
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