Investigating the conservation pattern of a putative second terpene synthase divalent metal binding motif in plants Zhou, Ke Peters, Reuben Peters, Reuben
dc.contributor.department Biochemistry, Biophysics and Molecular Biology 2020-04-02T17:50:34.000 2020-06-29T23:45:48Z 2020-06-29T23:45:48Z Thu Jan 01 00:00:00 UTC 2009 2009-02-01
dc.description.abstract <p>Terpene synthases (TPS) require divalent metal ion co-factors, typically magnesium, that are bound by a canonical DDXXD motif, as well as a putative second, seemingly less well conserved and understood (N/D)DXX(S/T)XXXE motif. Given the role of the Ser/Thr side chain hydroxyl group in ligating one of the three catalytically requisite divalent metal ions and the loss of catalytic activity upon substitution with Ala, it is surprising that Gly is frequently found in this ‘middle’ position of the putative second divalent metal binding motif in plant TPS. Here we report mutational investigation of this discrepancy in a model plant diterpene cyclase, abietadiene synthase from Abies grandis (AgAS). Substitution of the corresponding Thr in AgAS with Ser or Gly decreased catalytic activity much less than substitution with Ala. We speculate that the ability of Gly to partially restore activity relative to Ala substitution for Ser/Thr stems from the associated reduction in steric volume enabling a water molecule to substitute for the hydroxyl group from Ser/Thr, potentially in a divalent metal ion coordination sphere. In any case, our results are consistent with the observed conservation pattern for this putative second divalent metal ion binding motif in plant TPS.</p>
dc.description.comments <p>NOTICE: this is the author’s version of a work that was accepted for publication in Phytochemistry. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in <em>Phytochemistry</em>, VOL 70, ISSUE 3, (2009) DOI: <a href="" target="_blank" title="Persistent link using digital object identifier">10.1016/j.phytochem.2008.12.022</a>.</p>
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dc.identifier archive/
dc.identifier.articleid 1131
dc.identifier.contextkey 10350131
dc.identifier.s3bucket isulib-bepress-aws-west
dc.identifier.submissionpath bbmb_ag_pubs/123
dc.language.iso en
dc.source.bitstream archive/|||Fri Jan 14 19:18:05 UTC 2022
dc.source.uri 10.1016/j.phytochem.2008.12.022
dc.subject.disciplines Biochemistry, Biophysics, and Structural Biology
dc.subject.disciplines Genetics and Genomics
dc.subject.disciplines Plant Sciences
dc.subject.keywords Terpene Synthase
dc.subject.keywords Enzymatic Mechanism
dc.subject.keywords Cyclization
dc.subject.keywords Metal binding motifs
dc.subject.keywords Labdane-related diterpenoids
dc.title Investigating the conservation pattern of a putative second terpene synthase divalent metal binding motif in plants
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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