Evidence map›Paper›PMID 35935533›Full record

ArticleNature catalysis2022

Biocatalytic synthesis of non-standard amino acids by a decarboxylative aldol reaction.

Jonathan M Ellis, Meghan E Campbell, Prasanth Kumar, Eric P Geunes, Craig A Bingman, Andrew R Buller

Open access · greenAbstract read
In one paragraph

Article in Nature catalysis, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.9field-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

29 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Article
  3. Promiscuity-Guided Enzyme Evolution via Substrate Multiplexed Screening.Angewandte Chemie (International ed. in English) · 2026
    Review
  4. Pyridoxal 5'-Phosphate-Dependent Enzymatic Decarboxylative Annulation.Journal of the American Chemical Society · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. An Update: Enzymatic Synthesis for Industrial Applications.Angewandte Chemie (International ed. in English) · 2025
    Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Engineered Biocatalytic Synthesis of β-N-Substituted-α-Amino Acids.Angewandte Chemie (International ed. in English) · 2023
    Article
  20. Review
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

6 authors at 1 institution in 1 country.

Jonathan M EllisDepartment of Chemistry, University of Wisconsin-Madison; Madison, Wisconsin, United States.
Meghan E CampbellDepartment of Chemistry, University of Wisconsin-Madison; Madison, Wisconsin, United States.
Prasanth KumarDepartment of Chemistry, University of Wisconsin-Madison; Madison, Wisconsin, United States.
Eric P GeunesDepartment of Chemistry, University of Wisconsin-Madison; Madison, Wisconsin, United States.
Craig A BingmanDepartment of Biochemistry, University of Wisconsin-Madison; Madison, Wisconsin, United States.
Andrew R BullerDepartment of Chemistry, University of Wisconsin-Madison; Madison, Wisconsin, United States.
University of Wisconsin–Madison · US

Funding

BIOTECHNOLOGY TRAINING PROGRAMT32GM008349 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI FOX, BRIAN G · 1989 to 2019
$22.5M
Engineering in vivo biomolecular synthesis with non-standard building blocksDP2GM137417 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BULLER, ANDREW · 2019 to 2019
$2.2M
NIGMS NIH HHS DP2 GM137417NIGMS NIH HHS T32 GM008349
6 · The paper itself

Abstract

Enzymes are renowned for their catalytic efficiency and selectivity. Despite the wealth of carbon-carbon bond forming transformations in traditional organic chemistry and nature, relatively few C-C bond forming enzymes have found their way into the biocatalysis toolbox. Here we show that the enzyme UstD performs a highly selective decarboxylative aldol addition with diverse aldehyde substrates to make non-standard, γ-hydroxy amino acids. We increased the activity of UstD through three rounds of classic directed evolution and an additional round of computationally-guided engineering. The enzyme that emerged, UstD

Identifiers

PMID35935533
PMCPMC9355265
OpenAlexW4226019975

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.