Evidence map›Paper›PMID 32637664›Full record

ReviewSynthetic and systems biotechnology2020

Site directed mutagenesis as a precision tool to enable synthetic biology with engineered modular polyketide synthases.

Erin E Drufva, Elijah G Hix, Constance B Bailey

Erratum issuedAbstract readReview
In one paragraph

Review in Synthetic and systems biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
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  12. Natural products research in the modern age.Synthetic and systems biotechnology · 2020
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Erin E DrufvaDepartment of Chemistry, University of Tennessee-Knoxville, Knoxville, TN, 37996, USA.
Elijah G HixDepartment of Chemistry, University of Tennessee-Knoxville, Knoxville, TN, 37996, USA.
Constance B BaileyDepartment of Chemistry, University of Tennessee-Knoxville, Knoxville, TN, 37996, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Modular polyketide synthases (PKSs) are a multidomain megasynthase class of biosynthetic enzymes that have great promise for the development of new compounds, from new pharmaceuticals to high value commodity and specialty chemicals. Their colinear biosynthetic logic has been viewed as a promising platform for synthetic biology for decades. Due to this colinearity, domain swapping has long been used as a strategy to introduce molecular diversity. However, domain swapping often fails because it perturbs critical protein-protein interactions within the PKS. With our increased level of structural elucidation of PKSs, using judicious targeted mutations of individual residues is a more precise way to introduce molecular diversity with less potential for global disruption of the protein architecture. Here we review examples of targeted point mutagenesis to one or a few residues harbored within the PKS that alter domain specificity or selectivity, affect protein stability and interdomain communication, and promote more complex catalytic reactivity.

Indexed as

ACP, acyl carrier proteinAT, acyltransferaseDEBS, 6-deoxyerthronolide B synthaseDH, dehydrataseEI, enoylisomeraseER, enoylreductaseKR, ketoreductaseKS, ketosynthaseLM, loading moduleMod, moduleMT, methyltransferasePKS, polyketide synthasePolyketide synthaseProtein engineeringPS, pyran synthaseRational designSaturation mutagenesisSite directed mutagenesisSNAC, N-acetyl cysteamineSynthetic biology

Identifiers

PMID32637664
PMCPMC7327777

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.