Evidence map›Paper›PMID 34845903›Full record

ArticleBiochemistry2021

Second-Shell Amino Acid R266 Helps Determine

Dat P Truong, Simon Rousseau, Benjamin W Machala, Jamison P Huddleston, Mingzhao Zhu, Kenneth G Hull, Daniel Romo, Frank M Raushel, James C Sacchettini, Margaret E Glasner

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 53% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
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

10 authors at 2 institutions in 1 country.

Dat P TruongDepartment of Biochemistry and Biophysics, Texas A&M University, 2128 TAMU, College Station, Texas 77843-2128, United States.
Simon RousseauDepartment of Biochemistry and Biophysics, Texas A&M University, 2128 TAMU, College Station, Texas 77843-2128, United States.
Benjamin W MachalaDepartment of Biochemistry and Biophysics, Texas A&M University, 2128 TAMU, College Station, Texas 77843-2128, United States.
Jamison P HuddlestonDepartment of Chemistry, Texas A&M University, 3255 TAMU, College Station, Texas 77843-3255, United States.
Mingzhao ZhuBaylor Synthesis and Drug-Lead Discovery Laboratory, Department of Chemistry and Biochemistry, Baylor University, One Bear Place, Waco, Texas 76798-7348, United States.
Kenneth G HullBaylor Synthesis and Drug-Lead Discovery Laboratory, Department of Chemistry and Biochemistry, Baylor University, One Bear Place, Waco, Texas 76798-7348, United States.ORCID 0000-0002-3697-9551
Daniel RomoBaylor Synthesis and Drug-Lead Discovery Laboratory, Department of Chemistry and Biochemistry, Baylor University, One Bear Place, Waco, Texas 76798-7348, United States.ORCID 0000-0003-3805-092X
Frank M RaushelDepartment of Biochemistry and Biophysics, Texas A&M University, 2128 TAMU, College Station, Texas 77843-2128, United States.
James C SacchettiniDepartment of Chemistry, Texas A&M University, 3255 TAMU, College Station, Texas 77843-3255, United States.ORCID 0000-0001-5767-2367
Margaret E GlasnerDepartment of Biochemistry and Biophysics, Texas A&M University, 2128 TAMU, College Station, Texas 77843-2128, United States.ORCID 0000-0003-1818-1965
Texas A&M University · USBaylor University · US

Funding

Biophysical constraints on evolution of enzyme specificityR01GM124409 · NIGMS · TEXAS A&M AGRILIFE RESEARCH · PI GLASNER, MARGARET E · 2018 to 2021
$1.2M
NIGMS NIH HHS R01 GM124409
6 · The paper itself

Abstract

Catalytic promiscuity is the coincidental ability to catalyze nonbiological reactions in the same active site as the native biological reaction. Several lines of evidence show that catalytic promiscuity plays a role in the evolution of new enzyme functions. Thus, studying catalytic promiscuity can help identify structural features that predispose an enzyme to evolve new functions. This study identifies a potentially preadaptive residue in a promiscuous

Indexed as

Amino Acid IsomerasesAmino Acid SequenceAmino Acid SubstitutionAmycolatopsisBacterial ProteinsBiocatalysisCarbon-Carbon LyasesCatalytic DomainConserved SequenceCrystallography, X-RayEnzyme StabilityEvolution, MolecularKineticsModels, MolecularMutagenesis, Site-DirectedRecombinant ProteinsAmino Acid IsomerasesBacterial ProteinsCarbon-Carbon Lyaseso-succinylbenzoic acid synthaseRecombinant Proteins

Identifiers

PMID34845903
PMCPMC8939854
OpenAlexW3215328034

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.