Evidence map›Paper›PMID 29589959›Full record

ReviewAnnual review of biochemistry2018

Understanding and Improving the Activity of Flavin-Dependent Halogenases via Random and Targeted Mutagenesis.

Mary C Andorfer, Jared C Lewis

Open access · greenAbstract readReview
In one paragraph

Review in Annual review of biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.9field-weighted citation impact, top 5% 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

32 citing papers in PubMed, 98 citations in OpenAlex.

  1. Article
  2. Peptidic Tryptophan Halogenation by a Promiscuous Flavin-Dependent Enzyme.Angewandte Chemie (International ed. in English) · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Unlocking the catalytic precision of ligand-controlled enzymatic halogenation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Spin Dynamics of Flavoproteins.International journal of molecular sciences · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

2 authors at 2 institutions in 1 country.

Mary C AndorferDepartment of Biology and Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA; email: mandorfe@mit.edu.
Jared C LewisDepartment of Chemistry, University of Chicago, Chicago, Illinois 60637, USA; email: jaredlewis@uchicago.edu.
Howard Hughes Medical Institute · USUniversity of Chicago · US

Funding

Predoctoral Training Program in Chemistry & BiologyT32GM008720 · NIGMS · UNIVERSITY OF CHICAGO · PI PICCIRILLI, JOSEPH ANTHONY · 1999 to 2020
$4.7M
Directed Evolution of Halogenases For Small Molecule FunctionalizationR01GM115665 · NIGMS · UNIVERSITY OF CHICAGO · PI LEWIS, JARED C · 2015 to 2022
$2.5M
NIGMS NIH HHS R01 GM115665NIGMS NIH HHS T32 GM008720
6 · The paper itself

Abstract

Flavin-dependent halogenases (FDHs) catalyze the halogenation of organic substrates by coordinating reactions of reduced flavin, molecular oxygen, and chloride. Targeted and random mutagenesis of these enzymes have been used to both understand and alter their reactivity. These studies have led to insights into residues essential for catalysis and FDH variants with improved stability, expanded substrate scope, and altered site selectivity. Mutations throughout FDH structures have contributed to all of these advances. More recent studies have sought to rationalize the impact of these mutations on FDH function and to identify new FDHs to deepen our understanding of this enzyme class and to expand their utility for biocatalytic applications.

Indexed as

BiocatalysisCatalytic DomainDirected Molecular EvolutionDrug DesignEnzyme StabilityFlavinsHalogenationHydrocarbons, HalogenatedMetabolic Networks and PathwaysModels, MolecularMutagenesisOxidoreductasesSubstrate SpecificityFlavinsHydrocarbons, HalogenatedOxidoreductasesC–H functionalizationdirected evolutionflavinhalogenasemutagenesis

Identifiers

PMID29589959
PMCPMC6013374
OpenAlexW2794819581

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.