Evidence map›Paper›PMID 27933789›Full record

ArticleBiochemistry2016

The T296V Mutant of Amorpha-4,11-diene Synthase Is Defective in Allylic Diphosphate Isomerization but Retains the Ability To Cyclize the Intermediate (3R)-Nerolidyl Diphosphate to Amorpha-4,11-diene.

Zhenqiu Li, Ruiping Gao, Qinggang Hao, Huifang Zhao, Longbin Cheng, Fang He, Li Liu, Xiuhua Liu, Wayne K W Chou, Huajie Zhu and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Single Point Mutation Abolishes Water Capture in Germacradien-4-ol Synthase.Chembiochem : a European journal of chemical biology · 2024
    Article
  2. Understanding and Engineering the Stereoselectivity of Humulene Synthase.Angewandte Chemie (International ed. in English) · 2021
    Article
  3. Review
  4. Article
  5. Review
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

11 authors.

Zhenqiu Li
Ruiping Gao
Qinggang Hao
Huifang Zhao
Longbin Cheng
Fang He
Li Liu
Xiuhua Liu
Wayne K W ChouDepartment of Chemistry, Brown University , Box H, Providence, Rhode Island 02912-9108, United States.
Huajie Zhu
David E CaneDepartment of Chemistry, Brown University , Box H, Providence, Rhode Island 02912-9108, United States.

Funding

STEREOCHEMICAL STUDIES OF ISOPRENOID BIOSYNTHESISR01GM030301 · NIGMS · BROWN UNIVERSITY · PI CANE, DAVID E · 1985 to 2015
$5.4M
STEROCHEMICAL STUDIES 0F ISOPRENOID BIOSYNTHESISR37GM030301 · NIGMS · BROWN UNIVERSITY · PI CANE, DAVID E · 1994 to 2003
$1.8M
NIGMS NIH HHS R01 GM030301NIGMS NIH HHS R37 GM030301
6 · The paper itself

Abstract

The T296V mutant of amorpha-4,11-diene synthase catalyzes the abortive conversion of the natural substrate (E,E)-farnesyl diphosphate mainly into the acyclic product (E)-β-farnesene (88%) instead of the natural bicyclic sesquiterpene amorphadiene (7%). Incubation of the T296V mutant with (3R,6E)-nerolidyl diphosphate resulted in cyclization to amorphadiene. Analysis of additional mutants of amino acid residue 296 and in vitro assays with the intermediate analogue (2Z,6E)-farnesyl diphosphate as well as (3S,6E)-nerolidyl diphosphate demonstrated that the T296V mutant can no longer catalyze the allylic rearrangement of farnesyl diphosphate to the normal intermediate (3R,6E)-nerolidyl diphosphate, while retaining the ability to cyclize (3R,6E)-nerolidyl diphosphate to amorphadiene. The T296A mutant predominantly retained amorphadiene synthase activity, indicating that neither the hydroxyl nor the methyl group of the Thr296 side chain is required for cyclase activity.

Indexed as

Mutation, MissenseAlkyl and Aryl TransferasesArtemisia annuaBiocatalysisCyclizationDiphosphatesGas Chromatography-Mass SpectrometryKineticsModels, ChemicalMolecular StructurePlant ProteinsPolycyclic SesquiterpenesPolyisoprenyl PhosphatesSesquiterpenesStereoisomerismSubstrate SpecificityAlkyl and Aryl Transferasesamorpha-4,11-dieneamorpha-4,11-diene synthaseDiphosphatesfarnesyl pyrophosphatePlant ProteinsPolycyclic SesquiterpenesPolyisoprenyl PhosphatesSesquiterpenes

Identifiers

PMID27933789
PMCPMC5154624

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Registered trials

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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.