Evidence map›Paper›PMID 34721367›Full record

ReviewFrontiers in microbiology2021

Mini Review: Advances in 2-Haloacid Dehalogenases.

Yayue Wang, Qiao Xiang, Qingfeng Zhou, Jingliang Xu, Dongli Pei

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

11 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Computational Studies of Enzymes for C-F Bond Degradation and Functionalization.Chemphyschem : a European journal of chemical physics and physical chemistry · 2025
    Review
  8. Article
  9. Article
  10. Review
  11. 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

5 authors at 2 institutions in 1 country.

Yayue WangCollege of Biology and Food, Shangqiu Normal University, Shangqiu, China.
Qiao XiangCollege of Biology and Food, Shangqiu Normal University, Shangqiu, China.
Qingfeng ZhouCollege of Biology and Food, Shangqiu Normal University, Shangqiu, China.
Jingliang XuSchool of Chemical Engineering, Zhengzhou University, Zhengzhou, China.
Dongli PeiCollege of Biology and Food, Shangqiu Normal University, Shangqiu, China.
Shangqiu Normal University · CNZhengzhou University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The 2-haloacid dehalogenases (EC 3.8.1.X) are industrially important enzymes that catalyze the cleavage of carbon-halogen bonds in 2-haloalkanoic acids, releasing halogen ions and producing corresponding 2-hydroxyl acids. These enzymes are of particular interest in environmental remediation and environmentally friendly synthesis of optically pure chiral compounds due to their ability to degrade a wide range of halogenated compounds with astonishing efficiency for enantiomer resolution. The 2-haloacid dehalogenases have been extensively studied with regard to their biochemical characterization, protein crystal structures, and catalytic mechanisms. This paper comprehensively reviews the source of isolation, classification, protein structures, reaction mechanisms, biochemical properties, and application of 2-haloacid dehalogenases; current trends and avenues for further development have also been included.

Indexed as

2-haloacid dehalogenasesapplicationbiochemical propertiescatalytic mechanismprotein structure

Identifiers

PMID34721367
PMCPMC8554231
OpenAlexW3205838659

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.