Evidence map›Paper›PMID 30320324›Full record

ArticleOrganic & biomolecular chemistry2019

Identification of a lysine 4-hydroxylase from the glidobactin biosynthesis and evaluation of its biocatalytic potential.

Alexander Amatuni, Hans Renata

Abstract read
In one paragraph

Article in Organic & biomolecular chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Sequential oxidation of L-lysine by a non-heme iron hydroxylase.bioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. New Trends and Future Opportunities in the Enzymatic Formation of C-C, C-N, and C-O bonds.Chembiochem : a European journal of chemical biology · 2022
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Exploration of Iron- and a-Ketoglutarate-Dependent Dioxygenases as Practical Biocatalysts in Natural Product Synthesis.Synlett : accounts and rapid communications in synthetic organic chemistry · 2021
    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

2 authors.

Alexander AmatuniThe Scripps Research Institute, 130 Scripps Way, Jupiter, FL 33458, USA. hrenata@scripps.edu.
Hans Renata

Funding

Biocatalytic C-H Functionalization Logic in the Chemoenzymatic Synthesis of Therapeutic Natural ProductsR35GM128895 · NIGMS · UNIVERSITY OF FLORIDA · PI Hans Renata · 2018 to 2026
$3.7M
NIGMS NIH HHS R35 GM128895
6 · The paper itself

Abstract

We present the functional characterization of GlbB, a lysine 4-hydroxylase from the glidobactin biosynthetic gene cluster. Despite its narrow substrate specificity, GlbB is able to catalyze the hydroxylation of l-lysine with excellent total turnover number and complete regio- and diastereoselectivity. The synthetic utility of GlbB is illustrated by its use in the efficient preparation of a key dipeptide fragment of glidobactin.

Indexed as

BiocatalysisModels, MolecularPeptidesProcollagen-Lysine, 2-Oxoglutarate 5-DioxygenaseProtein ConformationStereoisomerismPeptidesProcollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase

Identifiers

PMID30320324
PMCPMC6374188

What OpenQuestion holds

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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.