ATTENTION: The software behind KU ScholarWorks is being upgraded to a new version. Starting July 15th, users will not be able to log in to the system, add items, nor make any changes until the new version is in place at the end of July. Searching for articles and opening files will continue to work while the system is being updated. If you have any questions, please contact Marianne Reed at mreed@ku.edu .

Show simple item record

dc.contributor.authorLuo, Qianyi
dc.contributor.authorMeneely, Kathleen M.
dc.contributor.authorLamb, Audrey L.
dc.date.accessioned2017-06-05T20:11:07Z
dc.date.available2017-06-05T20:11:07Z
dc.date.issued2011-05-11
dc.identifier.citationLuo, Q., Meneely, K. M., & Lamb, A. L. (2011). Entropic and enthalpic components of catalysis in the mutase and lyase activities of Pseudomonas aeruginosa PchB. Journal of the American Chemical Society, 133(18), 7229–7233. http://doi.org/10.1021/ja202091aen_US
dc.identifier.urihttp://hdl.handle.net/1808/24376
dc.descriptionThis document is the Accepted Manuscript version of a Published Work that appeared in final form in the Journal of the American Chemical Society, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://doi.org/10.1021/ja202091a.en_US
dc.description.abstractThe isochorismate-pyruvate lyase from Pseudomonas aeruginosa (PchB) catalyzes two pericyclic reactions, demonstrating the eponymous activity and also chorismate mutase activity. The thermodynamic parameters for these enzyme-catalyzed activities, as well as the uncatalyzed isochorismate decomposition, are reported from temperature dependence of kcat and kuncat data. The entropic effects do not contribute to enzyme catalysis as expected from previously reported chorismate mutase data. Indeed, an entropic penalty for the enzyme-catalyzed mutase reaction (ΔS‡ = -12.1 ± 0.6 cal/molK) is comparable to that of the previously reported uncatalyzed reaction, whereas that of the enzyme-catalyzed lyase reaction (ΔS‡ = -24.3 ± 0.6 cal/molK) is larger than that of the uncatalyzed lyase reaction (-15.77 ± 0.02 cal/molK) documented here. With the assumption that chemistry is rate-limiting, we propose that a reactive substrate conformation is formed upon loop closure of the active site and that ordering of the loop contributes to the entropic penalty for converting the enzyme substrate complex to the transition state.en_US
dc.publisherAmerican Chemical Societyen_US
dc.titleEntropic and enthalpic components of catalysis in the mutase and lyase activities of Pseudomonas aeruginosa PchBen_US
dc.typeArticleen_US
kusw.kuauthorLuo, Qianyi
kusw.kuauthorMeneely, Kathleen M.
kusw.kuauthorLamb, Audrey L.
kusw.kudepartmentMolecular Biosciencesen_US
dc.identifier.doi10.1021/ja202091aen_US
kusw.oaversionScholarly/refereed, publisher versionen_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US
dc.identifier.pmidPMC3163167en_US
dc.rights.accessrightsopenAccess


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record