Journal
FEBS LETTERS
Volume 579, Issue 25, Pages 5773-5780Publisher
WILEY
DOI: 10.1016/j.febslet.2005.09.066
Keywords
herbicide resistance; crystal structure; induced-fit; alternative substrate
Funding
- NCRR NIH HHS [P20 RR16443-01] Funding Source: Medline
- NIGMS NIH HHS [1R01 GM70633-01] Funding Source: Medline
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The shikimate pathway enzyme 5-enolpyruvyl shikimate-3-phosphate synthase (EPSP synthase) has received attention in the past because it is the target of the broad-spectrum herbicide glyphosate. The natural substrate of EPSP synthase is shikimate-3-phosphate. However, this enzyme can also utilize shikimate as substrate. Remarkably, this reaction is insensitive to inhibition by glyphosate. Crystallographic analysis of EPSP synthase from Escherichia coli, in complex with shikimate/glyphosate at 1.5 angstrom resolution, revealed that binding of shikimate induces changes around the backbone of the active site, which in turn impact the efficient binding of glyphosate. The implications from these findings with respect to the design of novel glyphosate-insensitive EPSP synthase enzymes are discussed. (c) 2005 Published by Elsevier B.V.
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