Evidence map›Paper›PMID 28620813›Full record

ArticleJournal of molecular modeling2017

An in-silico insight into the substrate binding characteristics of the active site of amorpha-4, 11-diene synthase, a key enzyme in artemisinin biosynthesis.

Habib Eslami, Seyed Kaveh Mohtashami, Maryam Taghavi Basmanj, Maryam Rahati, Hamzeh Rahimi

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Article in Journal of molecular modeling, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 50% of its field
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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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

5 authors at 4 institutions in 1 country.

Habib EslamiDepartment of Pharmacology, Molecular Medicine Research Center, Hormozgan Health Institute, School of Pharmacy, Hormozgan University of Medical Sciences, Bandar Abbas, Iran.
Seyed Kaveh MohtashamiCrop Genetic Engineering Group- Biofuel Research Team (BRT), Agricultural Biotechnology Research Institute of Iran (ABRII), Karaj, Iran.
Maryam Taghavi BasmanjBiotechnology Research Center, Molecular Medicine Department, Pasteur Institute of Iran, Tehran, Iran.
Maryam RahatiCrop Genetic Engineering Group- Biofuel Research Team (BRT), Agricultural Biotechnology Research Institute of Iran (ABRII), Karaj, Iran.
Hamzeh RahimiBiotechnology Research Center, Molecular Medicine Department, Pasteur Institute of Iran, Tehran, Iran. buksanbio@gmail.com.
Agricultural Biotechnology Research Institute of Iran · IRBiotechnology Research Center · IRHormozgan University of Medical Sciences · IRPasteur Institute of Iran · IR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The enzyme amorphadiene synthase (ADS) conducts the first committed step in the biosynthetic conversion of the substrate farnesyl pyrophosphate (FPP) to artemisinin, which is a highly effective natural product against multidrug-resistant strains of malaria. Due to the either low abundance or low turn-over rate of the enzyme, obtaining artemisinin from both natural and synthetic sources is costly and laborious. In this in silico study, we strived to elucidate the substrate binding site specificities of the ADS, with the rational that unraveling enzyme features paves the way for enzyme engineering to increase synthesis rate. A homology model of the ADS from Artemisia annua L. was constructed based on the available crystal structure of the 5-epiaristolochene synthase (TEAS) and further analyzed with molecular dynamic simulations to determine residues forming the substrate recognition pocket. We also investigated the structural aspects of Mg

Indexed as

Computer SimulationModels, MolecularAlkyl and Aryl TransferasesArtemisia annuaArtemisininsLactonesPlant ProteinsSequence AlignmentStructural Homology, ProteinAlkyl and Aryl Transferasesamorpha-4,11-diene synthaseartemisinArtemisininsLactonesPlant ProteinsAmorpha-4, 11-diene synthaseArtemisininHomology modelingMolecular dynamicsSubstrate binding site

Identifiers

PMID28620813
OpenAlexW2625583428

What OpenQuestion holds

Textmetadata
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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.