Mechanistic Insights into the Formation of the 6,10‐Bicyclic Eunicellane Skeleton by the Bacterial Diterpene Synthase Bnd4

2021 ◽  
Author(s):  
Baofu Xu ◽  
Dean Tantillo ◽  
Jeffrey Rudolf
Keyword(s):  
Diterpene Synthase

scholarly journals Transcriptomic Insight into Terpenoid Biosynthesis and Functional Characterization of Three Diterpene Synthases in Scutellaria barbata

Molecules ◽  
2018 ◽  
Vol 23 (11) ◽  
pp. 2952 ◽  
Author(s):  
Huabei Zhang ◽  
Baolong Jin ◽  
Junling Bu ◽  
Juan Guo ◽  
Tong Chen ◽  
...  
Keyword(s):  
Average Length ◽  
Functional Characterization ◽  
Terpene Synthase ◽  
Terpenoid Biosynthesis ◽  
Vitro Assay ◽  
Scutellaria Barbata ◽  
Aerial Parts ◽  
Diterpene Synthase ◽  
Clerodane Diterpenoids

Scutellaria barbata (Lamiaceae) is an important medicinal herb widely used in China, Korea, India, and other Asian countries. Neo-clerodane diterpenoids are the largest known group of Scutellaria diterpenoids and show promising cytotoxic activity against several cancer cell lines. Here, Illumina-based deep transcriptome analysis of flowers, the aerial parts (leaf and stem), and roots of S. barbata was used to explore terpenoid-related genes. In total, 121,958,564 clean RNA-sequence reads were assembled into 88,980 transcripts, with an average length of 1370 nt and N50 length of 2144 nt, indicating high assembly quality. We identified nearly all known terpenoid-related genes (33 genes) involved in biosynthesis of the terpenoid backbone and 14 terpene synthase genes which generate skeletons for different terpenoids. Three full length diterpene synthase genes were functionally identified using an in vitro assay. SbTPS8 and SbTPS9 were identified as normal-CPP and ent-CPP synthase, respectively. SbTPS12 reacts with SbTPS8 to produce miltiradiene. Furthermore, SbTPS12 was proven to be a less promiscuous class I diterpene synthase. These results give a comprehensive understanding of the terpenoid biosynthesis in S. barbata and provide useful information for enhancing the production of bioactive neo-clerodane diterpenoids through genetic engineering.

A diterpene synthase from the clary sage Salvia sclarea catalyzes the cyclization of geranylgeranyl diphosphate to (8R)-hydroxy-copalyl diphosphate

2013 ◽  
Vol 91 ◽  
pp. 93-99 ◽  
Author(s):  
Nils Günnewich ◽  
Yasuhiro Higashi ◽  
Xiaohong Feng ◽  
Kum-Boo Choi ◽  
Jürgen Schmidt ◽  
...  
Keyword(s):  
Geranylgeranyl Diphosphate ◽  
Salvia Sclarea ◽  
Diterpene Synthase

scholarly journals The terpene synthase gene family inTripterygium wilfordiiharbors a labdane-type diterpene synthase among the monoterpene synthase TPS-b subfamily

2017 ◽  
Vol 89 (3) ◽  
pp. 429-441 ◽  
Author(s):  
Nikolaj L. Hansen ◽  
Allison M. Heskes ◽  
Britta Hamberger ◽  
Carl E. Olsen ◽  
Björn M. Hallström ◽  
...  
Keyword(s):  
Gene Family ◽  
Terpene Synthase ◽  
Monoterpene Synthase ◽  
Diterpene Synthase

scholarly journals A Fungal Diterpene Synthase Is Responsible for Sterol Biosynthesis for Growth

2020 ◽  
Vol 11 ◽  
Author(s):  
Yanjie Liu ◽  
Anqing Duan ◽  
Longfei Chen ◽  
Dan Wang ◽  
Qiaohong Xie ◽  
...  
Keyword(s):  
Sterol Biosynthesis ◽  
Diterpene Synthase

Substitution of Two Active-Site Residues Alters C9-Hydroxylation in a Class II Diterpene Synthase

ChemBioChem ◽  
2016 ◽  
Vol 17 (24) ◽  
pp. 2304-2307 ◽  
Author(s):  
Sibongile Mafu ◽  
Emil Fischer ◽  
J. Bennett Addison ◽  
Isabel Riberio Barbosana ◽  
Philipp Zerbe
Keyword(s):  
Active Site ◽  
Class Ii ◽  
Active Site Residues ◽  
Diterpene Synthase

scholarly journals Following evolution's lead to a single residue switch for diterpene synthase product outcome

2007 ◽  
Vol 104 (18) ◽  
pp. 7397-7401 ◽  
Author(s):  
Meimei Xu ◽  
P. Ross Wilderman ◽  
Reuben J. Peters
Keyword(s):  
Natural Products ◽  
Higher Plants ◽  
Primary Metabolism ◽  
Terpene Synthases ◽  
Natural Product Biosynthesis ◽  
Widespread Occurrence ◽  
Gibberellin Metabolism ◽  
Diterpene Synthase ◽  
Short Circuits ◽  
Product Outcome

There have been few insights into the biochemical origins of natural product biosynthesis from primary metabolism. Of particular interest are terpene synthases, which often mediate the committed step in particular biosynthetic pathways so that alteration of their product outcome is a key step in the derivation of novel natural products. These enzymes also catalyze complex reactions of significant mechanistic interest. Following an evolutionary lead from two recently diverged, functionally distinct diterpene synthase orthologs from different subspecies of rice, we have identified a single residue that can switch product outcome. Specifically, the mutation of a conserved isoleucine to threonine that acts to convert not only the originally targeted isokaurene synthase into a specific pimaradiene synthase but also has a much broader effect, which includes conversion of the ent-kaurene synthases found in all higher plants for gibberellin phytohormone biosynthesis to the production of pimaradiene. This surprisingly facile switch for diterpene synthase catalytic specificity indicates the ease with which primary (gibberellin) metabolism can be subverted to secondary biosynthesis and may underlie the widespread occurrence of pimaradiene-derived natural products. In addition, because this isoleucine is required for the mechanistically more complex cyclization to tetracyclic kaurene, whereas substitution with threonine “short-circuits” this mechanism to produce the “simpler” tricyclic pimaradiene, our results have some implications regarding the means by which terpene synthases specify product outcome.

scholarly journals Molecular and functional evolution of the fungal diterpene synthase genes

2015 ◽  
Vol 15 (1) ◽  
Author(s):  
Marc JC Fischer ◽  
Camille Rustenhloz ◽  
Véronique Leh-Louis ◽  
Guy Perrière
Keyword(s):  
Functional Evolution ◽  
Diterpene Synthase
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