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

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
File
Original bundle
Now showing 1 - 2 of 2
Name:
2019_Peters_SwitchingNontraditionalManuscript.pdf
Size:
2.22 MB
Format:
Adobe Portable Document Format
Description:
Name:
0-Supporting_Information.pdf
Size:
6.19 MB
Format:
Adobe Portable Document Format
Description:
Collections