Evidence map›Paper›PMID 31650156›Full record

ReviewNatural product reports2020

Terpene synthases in disguise: enzymology, structure, and opportunities of non-canonical terpene synthases.

Jeffrey D Rudolf, Chin-Yuan Chang

Abstract readReview
In one paragraph

Review in Natural product reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

72 citing papers in PubMed.

  1. Article
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  10. Structural Revision of the CAngewandte Chemie (International ed. in English) · 2026
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  13. Review
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12 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Jeffrey D RudolfDepartment of Chemistry, University of Florida, Gainesville, Florida 32611, USA. jrudolf@chem.ufl.edu.ORCID 0000-0003-2718-9651
Chin-Yuan ChangDepartment of Biological Science and Technology, National Chiao Tung University, Hsin-Chu, Taiwan, Republic of China.ORCID 0000-0001-7314-3967

Funding

Cytochrome P450 Enzymes from Streptomyces: Diverse Biocatalysts in Natural Products BiosynthesisR00GM124461 · NIGMS · UNIVERSITY OF FLORIDA · PI RUDOLF, JEFFREY DANIEL · 2019 to 2021
$747k
Cytochrome P450 Enzymes from Streptomyces: Diverse Biocatalysts in Natural Products BiosynthesisK99GM124461 · NIGMS · SCRIPPS FLORIDA · PI RUDOLF, JEFFREY DANIEL · 2017 to 2017
$90k
NIGMS NIH HHS K99 GM124461NIGMS NIH HHS R00 GM124461
6 · The paper itself

Abstract

Covering: up to July 2019 Terpene synthases (TSs) are responsible for generating much of the structural diversity found in the superfamily of terpenoid natural products. These elegant enzymes mediate complex carbocation-based cyclization and rearrangement cascades with a variety of electron-rich linear and cyclic substrates. For decades, two main classes of TSs, divided by how they generate the reaction-triggering initial carbocation, have dominated the field of terpene enzymology. Recently, several novel and unconventional TSs that perform TS-like reactions but do not resemble canonical TSs in sequence or structure have been discovered. In this review, we identify 12 families of non-canonical TSs and examine their sequences, structures, functions, and proposed mechanisms. Nature provides a wide diversity of enzymes, including prenyltransferases, methyltransferases, P450s, and NAD+-dependent dehydrogenases, as well as completely new enzymes, that utilize distinctive reaction mechanisms for TS chemistry. These unique non-canonical TSs provide immense opportunities to understand how nature evolved different tools for terpene biosynthesis by structural and mechanistic characterization while affording new probes for the discovery of novel terpenoid natural products and gene clusters via genome mining. With every new discovery, the dualistic paradigm of TSs is contradicted and the field of terpene chemistry and enzymology continues to expand.

Indexed as

Alkyl and Aryl TransferasesAminophenolsCannabinoidsCyclizationCytochrome P-450 Enzyme SystemDimethylallyltranstransferaseIridoidsLyngbya ToxinsMolecular StructurePhenazinesPolycyclic CompoundsProtein ConformationTerpenesAlkyl and Aryl TransferasesAminophenolsCannabinoidsCytochrome P-450 Enzyme SystemDimethylallyltranstransferaseIridoidslavanducyaninLyngbya ToxinsPhenazinesplatencinPolycyclic CompoundsteleocidinsTerpenesterpene synthase

Identifiers

PMID31650156
PMCPMC7101268

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.