Evidence map›Paper›PMID 25931126›Full record

ArticleThe Journal of biological chemistry2015

Reconstitution of Formylglycine-generating Enzyme with Copper(II) for Aldehyde Tag Conversion.

Patrick G Holder, Lesley C Jones, Penelope M Drake, Robyn M Barfield, Stefanie Bañas, Gregory W de Hart, Jeanne Baker, David Rabuka

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed, 1 pooled it
4.1field-weighted citation impact, top 6% 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, 1 synthesis or guideline pooled it, 65 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Mechanism of OACS central science · 2025
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  7. DNA-Encoded Peptide Library Synthesis and Applications, a Mini-Review.Methods in molecular biology (Clifton, N.J.) · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Bivalent EGFR-Targeting DARPin-MMAE Conjugates.International journal of molecular sciences · 2022
    Article
  12. Article
  13. Article
  14. Bifunctional Reagents for Formylglycine Conjugation: Pitfalls and Breakthroughs.Chembiochem : a European journal of chemical biology · 2020
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Formylglycine-generating enzyme binds substrate directly at a mononuclear Cu(I) center to initiate OProceedings of the National Academy of Sciences of the United States of America · 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

8 authors at 1 institution in 1 country.

Patrick G HolderFrom Catalent Pharma Solutions, Emeryville, California 94608.
Lesley C JonesFrom Catalent Pharma Solutions, Emeryville, California 94608.
Penelope M DrakeFrom Catalent Pharma Solutions, Emeryville, California 94608.
Robyn M BarfieldFrom Catalent Pharma Solutions, Emeryville, California 94608.
Stefanie BañasFrom Catalent Pharma Solutions, Emeryville, California 94608.
Gregory W de HartFrom Catalent Pharma Solutions, Emeryville, California 94608.
Jeanne BakerFrom Catalent Pharma Solutions, Emeryville, California 94608.
David RabukaFrom Catalent Pharma Solutions, Emeryville, California 94608. Electronic address: david.rabuka@catalent.com.
Catalent (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To further our aim of synthesizing aldehyde-tagged proteins for research and biotechnology applications, we developed methods for recombinant production of aerobic formylglycine-generating enzyme (FGE) in good yield. We then optimized the FGE biocatalytic reaction conditions for conversion of cysteine to formylglycine in aldehyde tags on intact monoclonal antibodies. During the development of these conditions, we discovered that pretreating FGE with copper(II) is required for high turnover rates and yields. After further investigation, we confirmed that both aerobic prokaryotic (Streptomyces coelicolor) and eukaryotic (Homo sapiens) FGEs contain a copper cofactor. The complete kinetic parameters for both forms of FGE are described, along with a proposed mechanism for FGE catalysis that accounts for the copper-dependent activity.

Indexed as

Bacterial ProteinsCoenzymesCopperCysteineHumansOxidoreductases Acting on Sulfur Group DonorsStreptomyces coelicolorSulfatasesBacterial ProteinsCoenzymesCopperCysteineOxidoreductases Acting on Sulfur Group DonorsSulfatasesSUMF1 protein, humanaldehyde tagantibody drug conjugationcatalysisenzyme kineticsmetalloenzymemonoclonal antibodypost-translational modification (PTM)

Identifiers

PMID25931126
PMCPMC4505483
OpenAlexW2022897757

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.