Evidence map›Paper›PMID 31807686›Full record

ArticleACS central science2019

Site-Selective C-H Halogenation Using Flavin-Dependent Halogenases Identified via Family-Wide Activity Profiling.

Brian F Fisher, Harrison M Snodgrass, Krysten A Jones, Mary C Andorfer, Jared C Lewis

Open access · diamondAbstract read
In one paragraph

Article in ACS central science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

60 citing papers in PubMed, 114 citations in OpenAlex.

  1. Predicting Functional Diversity Within Enzyme Families: A Practical Perspective.Chembiochem : a European journal of chemical biology · 2026
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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

5 authors at 3 institutions in 1 country.

Brian F FisherDepartment of Chemistry, Indiana University, Bloomington, Indiana 47405, United States.
Harrison M SnodgrassDepartment of Chemistry, Indiana University, Bloomington, Indiana 47405, United States.
Krysten A JonesDepartment of Chemistry, University of Chicago, Chicago, Illinois 60637, United States.
Mary C AndorferDepartment of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.
Jared C LewisDepartment of Chemistry, Indiana University, Bloomington, Indiana 47405, United States.
Indiana University Bloomington · USMassachusetts Institute of Technology · USUniversity of Chicago · US

Funding

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 GM115665
6 · The paper itself

Abstract

Enzymes are powerful catalysts for site-selective C-H bond functionalization. Identifying suitable enzymes for this task and for biocatalysis in general remains challenging, however, due to the fundamental difficulty of predicting catalytic activity from sequence information. In this study, family-wide activity profiling was used to obtain sequence-function information on flavin-dependent halogenases (FDHs). This broad survey provided a number of insights into FDH activity, including halide specificity and substrate preference, that were not apparent from the more focused studies reported to date. Regions of FDH sequence space that are most likely to contain enzymes suitable for halogenating small-molecule substrates were also identified. FDHs with novel substrate scope and complementary regioselectivity on large, three-dimensionally complex compounds were characterized and used for preparative-scale late-stage C-H functionalization. In many cases, these enzymes provide activities that required several rounds of directed evolution to accomplish in previous efforts, highlighting that this approach can achieve significant time savings for biocatalyst identification and provide advanced starting points for further evolution.

Identifiers

PMID31807686
PMCPMC6891866
OpenAlexW2981561997

What OpenQuestion holds

Textmetadata
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.