Evidence map›Paper›PMID 23352143›Full record

ArticleChemistry & biology2013

Engineering the substrate specificity of the DhbE adenylation domain by yeast cell surface display.

Keya Zhang, Kathryn M Nelson, Karan Bhuripanyo, Kimberly D Grimes, Bo Zhao, Courtney C Aldrich, Jun Yin

Open access · greenAbstract read
In one paragraph

Article in Chemistry & biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
7.8field-weighted citation impact, top 3% 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

33 citing papers in PubMed, 92 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Keya ZhangDepartment of Chemistry, University of Chicago, Chicago, IL 60637, USA.
Kathryn M Nelson
Karan Bhuripanyo
Kimberly D Grimes
Bo Zhao
Courtney C Aldrich
Jun Yin
University of Chicago · USUniversity of Minnesota · US

Funding

Design of Antituberculosis Agents that Target Siderophore BiosynthesisR01AI070219 · NIAID · UNIVERSITY OF MINNESOTA · PI ALDRICH, COURTNEY C · 2006 to 2013
$2.2M
NIAID NIH HHS AI070219NIAID NIH HHS R01 AI070219
6 · The paper itself

Abstract

The adenylation (A) domains of nonribosomal peptide synthetases (NRPSs) activate aryl acids or amino acids to launch their transfer through the NRPS assembly line for the biosynthesis of many medicinally important natural products. In order to expand the substrate pool of NRPSs, we developed a method based on yeast cell surface display to engineer the substrate specificities of the A-domains. We acquired A-domain mutants of DhbE that have 11- and 6-fold increases in k(cat)/K(m) with nonnative substrates 3-hydroxybenzoic acid and 2-aminobenzoic acid, respectively and corresponding 3- and 33-fold decreases in k(cat)/K(m) values with the native substrate 2,3-dihydroxybenzoic acid, resulting in a dramatic switch in substrate specificity of up to 200-fold. Our study demonstrates that yeast display can be used as a high throughput selection platform to reprogram the "nonribosomal code" of A-domains.

Indexed as

Bacillus subtilisCatalytic DomainCell Surface Display TechniquesHydroxybenzoatesMutationortho-AminobenzoatesPeptide SynthasesSubstrate SpecificityYeasts2,3-dihydroxybenzoic acid3-hydroxybenzoic acidanthranilic acidHydroxybenzoatesortho-AminobenzoatesPeptide Synthases

Identifiers

PMID23352143
PMCPMC3807743
OpenAlexW2045400012

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.