ArticleScientific reports2014
Structure, function and inhibition of ent-kaurene synthase from Bradyrhizobium japonicum.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 51 citations in OpenAlex.
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- Changing Face: A Key Residue for the Addition of Water by Sclareol Synthase.ACS catalysis · 2018Article
- Insights Into the Bifunctional Aphidicolan-16-ß-ol Synthase Through Rapid Biomolecular Modeling Approaches.Frontiers in chemistry · 2018Article
- Structural and Chemical Biology of Terpenoid Cyclases.Chemical reviews · 2017Review
- Elucidation of gibberellin biosynthesis in bacteria reveals convergent evolution.Nature chemical biology · 2017Article
- Biosynthetic Origin of the Ether Ring in Platensimycin.Journal of the American Chemical Society · 2016Article
- Multi-domain terpenoid cyclase architecture and prospects for proximity in bifunctional catalysis.Current opinion in structural biology · 2016Review
- Structure of the ent-Copalyl Diphosphate Synthase PtmT2 from Streptomyces platensis CB00739, a Bacterial Type II Diterpene Synthase.Journal of the American Chemical Society · 2016Article
- Structure and Function of Fusicoccadiene Synthase, a Hexameric Bifunctional Diterpene Synthase.ACS chemical biology · 2016Article
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Authors and funding
15 authors at 4 institutions in 3 countries.
Funding
Abstract
We report the first X-ray crystal structure of ent-kaur-16-ene synthase from Bradyrhizobium japonicum, together with the results of a site-directed mutagenesis investigation into catalytic activity. The structure is very similar to that of the α domains of modern plant terpene cyclases, a result that is of interest since it has been proposed that many plant terpene cyclases may have arisen from bacterial diterpene cyclases. The ent-copalyl diphosphate substrate binds to a hydrophobic pocket near a cluster of Asp and Arg residues that are essential for catalysis, with the carbocations formed on ionization being protected by Leu, Tyr and Phe residues. A bisphosphonate inhibitor binds to the same site. In the kaurene synthase from the moss Physcomitrella patens, 16-α-hydroxy-ent-kaurane as well as kaurene are produced since Leu and Tyr in the P. patens kaurene synthase active site are replaced by smaller residues enabling carbocation quenching by water. Overall, the results represent the first structure determination of a bacterial diterpene cyclase, providing insights into catalytic activity, as well as structural comparisons with diverse terpene synthases and cyclases which clearly separate the terpene cyclases from other terpene synthases having highly α-helical structures.
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