Evidence map›Paper›PMID 27935677›Full record

ArticleBiochemistry2016

Tryptophan Synthase Uses an Atypical Mechanism To Achieve Substrate Specificity.

Andrew R Buller, Paul van Roye, Javier Murciano-Calles, Frances H Arnold

Abstract read
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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.2field-weighted citation impact, top 19% 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

22 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Promiscuity-Guided Enzyme Evolution via Substrate Multiplexed Screening.Angewandte Chemie (International ed. in English) · 2026
    Review
  3. Solution-state nuclear magnetic resonance studies of theBiochemistry and biophysics reports · 2026
    Article
  4. Review
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  6. Article
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  12. Review
  13. Article
  14. Article
  15. ACS catalysis · 2021
    Article
  16. Article
  17. Article
  18. Tryptophan Synthase: Biocatalyst Extraordinaire.Chembiochem : a European journal of chemical biology · 2021
    Review
  19. Article
  20. Facile in Vitro Biocatalytic Production of Diverse Tryptamines.Chembiochem : a European journal of chemical biology · 2019
    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

4 authors at 1 institution in 1 country.

Andrew R BullerDivision of Chemistry and Chemical Engineering 210-41, California Institute of Technology , 1200 East California Boulevard, Pasadena, California 91125, United States.
Paul van RoyeDivision of Chemistry and Chemical Engineering 210-41, California Institute of Technology , 1200 East California Boulevard, Pasadena, California 91125, United States.
Javier Murciano-CallesDivision of Chemistry and Chemical Engineering 210-41, California Institute of Technology , 1200 East California Boulevard, Pasadena, California 91125, United States.
Frances H ArnoldDivision of Chemistry and Chemical Engineering 210-41, California Institute of Technology , 1200 East California Boulevard, Pasadena, California 91125, United States.ORCID http://orcid.org/0000-0002-4027-364X
California Institute of Technology · US

Funding

Radical SAM enzyme engineering to produce improved thiopeptide antibioticsF32GM110851 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI BULLER, ANDREW · 2015 to 2016
$109k
NIGMS NIH HHS F32 GM110851
6 · The paper itself

Abstract

Tryptophan synthase (TrpS) catalyzes the final steps in the biosynthesis of l-tryptophan from l-serine (Ser) and indole-3-glycerol phosphate (IGP). We report that native TrpS can also catalyze a productive reaction with l-threonine (Thr), leading to (2S,3S)-β-methyltryptophan. Surprisingly, β-substitution occurs in vitro with a 3.4-fold higher catalytic efficiency for Ser over Thr using saturating indole, despite a >82000-fold preference for Ser in direct competition using IGP. Structural data identify a novel product binding site, and kinetic experiments clarify the atypical mechanism of specificity: Thr binds efficiently but decreases the affinity for indole and disrupts the allosteric signaling that regulates the catalytic cycle.

Indexed as

Biosynthetic PathwaysAllosteric RegulationArchaeal ProteinsBinding SitesBiocatalysisCrystallography, X-RayGlycerophosphatesIndolesKineticsModels, MolecularMolecular StructureProtein BindingProtein DomainsProtein SubunitsPyrococcus furiosusSerineArchaeal Proteinsbeta-methyltryptophanGlycerophosphatesindoleindoleglycerol phosphateIndolesProtein SubunitsSerineThreonineTryptophanTryptophan Synthase

Identifiers

PMID27935677
PMCPMC5207025
OpenAlexW2560179290

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.