Evidence map›Paper›PMID 22528483›Full record

ArticleThe Journal of biological chemistry2012

Identification of a human trans-3-hydroxy-L-proline dehydratase, the first characterized member of a novel family of proline racemase-like enzymes.

Wouter F Visser, Nanda M Verhoeven-Duif, Tom J de Koning

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

20 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. The integration of AlphaFold-predicted and crystal structures of humanComputational and structural biotechnology journal · 2022
    Article
  7. L-Arginine Nutrition and Metabolism in Ruminants.Advances in experimental medicine and biology · 2022
    Article
  8. Article
  9. Review
  10. Characterization of a NovelJournal of bacteriology · 2017
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

3 authors at 2 institutions in 1 country.

Wouter F VisserDepartment of Metabolic Diseases, University Medical Center Utrecht/Wilhelmina Children's Hospital Utrecht, 3508 AB Utrecht, The Netherlands. w.visser-2@umcutrecht.nl
Nanda M Verhoeven-Duif
Tom J de Koning
University Medical Center Utrecht · NLWilhelmina Children's Hospital · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A family of eukaryotic proline racemase-like genes has recently been identified. Several members of this family have been well characterized and are known to catalyze the racemization of free proline or trans-4-hydroxyproline. However, the majority of eukaryotic proline racemase-like proteins, including a human protein called C14orf149, lack a specific cysteine residue that is known to be critical for racemase activity. Instead, these proteins invariably contain a threonine residue at this position. The function of these enzymes has remained unresolved until now. In this study, we demonstrate that three enzymes of this type, including human C14orf149, catalyze the dehydration of trans-3-hydroxy-L-proline to Δ(1)-pyrroline-2-carboxylate (Pyr2C). These are the first enzymes of this subclass of proline racemase-like genes for which the enzymatic activity has been resolved. C14orf149 is also the first human enzyme that acts on trans-3-hydroxy-L-proline. Interestingly, a mutant enzyme in which the threonine in the active site is mutated back into cysteine regained 3-hydroxyproline epimerase activity. This result suggests that the enzymatic activity of these enzymes is dictated by a single residue. Presumably, human C14orf149 serves to degrade trans-3-hydroxy-L-proline from the diet and originating from the degradation of proteins that contain this amino acid, such as collagen IV, which is an important structural component of basement membrane.

Indexed as

Gene Expression Regulation, EnzymologicAmino Acid IsomerasesAnimalsBasement MembraneCarbon-Oxygen LyasesCatalysisCatalytic DomainCloning, MolecularCysteineGlutathione TransferaseHumansHydroxyprolineModels, BiologicalMutationOpen Reading FramesPhylogenyAmino Acid IsomerasesCarbon-Oxygen LyasesCysteineGlutathione TransferaseHydroxyprolineL3HYPDH protein, humanproline racemase

Identifiers

PMID22528483
PMCPMC3381129
OpenAlexW1975905428

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.