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Structure and mechanism of HpcG, a hydratase in the homoprotocatechuate degradation pathway of Escherichia coli
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Izumi, Atsushi, Rea, Dean, Adachi, Tomoko, Unzai, Satoru, Park, Sam-Yong, Roper, David I. and Tame, Jeremy R. H. (2007) Structure and mechanism of HpcG, a hydratase in the homoprotocatechuate degradation pathway of Escherichia coli. Journal of Molecular Biology, Vol.370 (No.5). pp. 899-911. doi:10.1016/j.jmb.2007.05.006 ISSN 0022-2836.
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Official URL: http://dx.doi.org/10.1016/j.jmb.2007.05.006
Abstract
HpcG catalyses the hydration of a carbon-carbon double bond without the aid of any cofactor other than a simple divalent metal ion such as Mg2+. Since the substrate has a nearby carbonyl group, it is believed that it first isomerises to form a pair of conjugated double bonds in the enol tautomer before Michael addition of water. Previous chemical studies of the reaction, of the mechanism. The substrate itself is unstable, preventing co-crystallisation or soaking of crystals, but oxalate is a strong competitive inhibitor. We have solved the crystal structure of the protein in the apo form, and with magnesium and oxalate bound. Modelling substrate into the active site suggests the attacking water molecule is not part of the metal coordination shell, in contrast to a previous proposal. Our model suggests that geometrically strained cis isomer intermediates do not lie on the reaction pathway, and that separate groups are involved in the isomerisation and hydration steps. (c) 2007 Elsevier Ltd. All rights reserved.
| Item Type: | Journal Article | ||||
|---|---|---|---|---|---|
| Subjects: | Q Science > QD Chemistry | ||||
| Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) > Biological Sciences ( -2010) | ||||
| Journal or Publication Title: | Journal of Molecular Biology | ||||
| Publisher: | Academic Press | ||||
| ISSN: | 0022-2836 | ||||
| Official Date: | 27 July 2007 | ||||
| Dates: |
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| Volume: | Vol.370 | ||||
| Number: | No.5 | ||||
| Number of Pages: | 13 | ||||
| Page Range: | pp. 899-911 | ||||
| DOI: | 10.1016/j.jmb.2007.05.006 | ||||
| Status: | Peer Reviewed | ||||
| Publication Status: | Published | ||||
| Access rights to Published version: | Restricted or Subscription Access |
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