Switching on a Nontraditional Enzymatic Base—Deprotonation by Serine in the ent-Kaurene Synthase from Bradyrhizobium japonicum

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dc.contributor.author Jia, Meirong
dc.contributor.author Zhang, Yue
dc.contributor.author Peters, Reuben
dc.contributor.author Siegel, Justin
dc.contributor.author Tantillo, Dean
dc.contributor.author Peters, Reuben
dc.contributor.department Biochemistry, Biophysics and Molecular Biology
dc.date 2019-09-22T06:10:57.000
dc.date.accessioned 2020-06-29T23:46:49Z
dc.date.available 2020-06-29T23:46:49Z
dc.date.copyright Tue Jan 01 00:00:00 UTC 2019
dc.date.issued 2019-01-01
dc.description.abstract <p>Terpene synthases often catalyze complex carbocation cascade reactions. It has been previously shown that single-residue switches involving replacement of a key aliphatic residue with serine or threonine can “short-circuit” such reactions that are presumed to act indirectly via dipole stabilization of intermediate carbocations. Here a similar switch was found in the structurally characterized <em>ent</em>-kaurene synthase from <em>Bradyrhizobium japonicum</em>. Application of a recently developed computational approach to terpene synthases, <em>TerDockin</em>, surprisingly indicates direct action of the introduced serine hydroxyl as a catalytic base. Notably, this model suggests an alternative interpretation of previous results and potential routes toward reengineering terpene synthase activity more generally.</p>
dc.description.comments <p>This is a manuscript of an article published as Jia, Meirong, Yue Zhang, Justin B. Siegel, Dean J. Tantillo, and Reuben J. Peters. "Switching on a Nontraditional Enzymatic Base–Deprotonation by Serine in the ent-Kaurene Synthase from Bradyrhizobium japonicum." <em>ACS Catalysis</em> (2019). doi: <a href="https://doi.org/10.1021/acscatal.9b02783" title="DOI URL">10.1021/acscatal.9b02783</a>. Posted with permission.</p>
dc.format.mimetype application/pdf
dc.identifier archive/lib.dr.iastate.edu/bbmb_ag_pubs/256/
dc.identifier.articleid 1264
dc.identifier.contextkey 15323141
dc.identifier.s3bucket isulib-bepress-aws-west
dc.identifier.submissionpath bbmb_ag_pubs/256
dc.identifier.uri https://dr.lib.iastate.edu/handle/20.500.12876/10728
dc.language.iso en
dc.source.bitstream archive/lib.dr.iastate.edu/bbmb_ag_pubs/256/0-Supporting_Information.pdf|||Fri Jan 14 22:58:59 UTC 2022
dc.source.bitstream archive/lib.dr.iastate.edu/bbmb_ag_pubs/256/2019_Peters_SwitchingNontraditionalManuscript.pdf|||Fri Jan 14 22:59:00 UTC 2022
dc.source.uri 10.1021/acscatal.9b02783
dc.subject.disciplines Biochemistry
dc.subject.disciplines Biophysics
dc.subject.disciplines Molecular Biology
dc.subject.disciplines Structural Biology
dc.subject.keywords biosynthesis
dc.subject.keywords terpene synthases
dc.subject.keywords enzymology
dc.subject.keywords natural products
dc.subject.keywords acid-base catalysis
dc.supplemental.bitstream Supporting_Information.pdf
dc.title Switching on a Nontraditional Enzymatic Base—Deprotonation by Serine in the ent-Kaurene Synthase from Bradyrhizobium japonicum
dc.type article
dc.type.genre article
dspace.entity.type Publication
relation.isAuthorOfPublication 498a24ec-81d7-4bee-b145-323d38e7a392
relation.isOrgUnitOfPublication c70f85ae-e0cd-4dce-96b5-4388aac08b3f
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