Evidence map›Paper›PMID 32624849›Full record

ArticleEngineering in life sciences2017

Engineering bi-functional enzyme complex of formate dehydrogenase and leucine dehydrogenase by peptide linker mediated fusion for accelerating cofactor regeneration.

Yonghui Zhang, Yali Wang, Shizhen Wang, Baishan Fang

Open access · bronzeAbstract read
In one paragraph

Article in Engineering in life sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-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

14 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Protein scaffolds: A tool for multi-enzyme assembly.Biotechnology reports (Amsterdam, Netherlands) · 2021
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Metabolic Engineering ofFrontiers in bioengineering and biotechnology · 2020
    Article
  13. EnhancingEngineering in life sciences · 2019
    Article
  14. Enzyme Fusions in Biocatalysis: Coupling Reactions by Pairing Enzymes.Chembiochem : a European journal of chemical biology · 2019
    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

4 authors at 1 institution in 1 country.

Yonghui ZhangDepartment of Chemical and Biochemical Engineering College of Chemistry and Chemical Engineering Xiamen University Xiamen P. R. China.ORCID 0000-0002-7313-4259
Yali WangDepartment of Chemical and Biochemical Engineering College of Chemistry and Chemical Engineering Xiamen University Xiamen P. R. China.
Shizhen WangDepartment of Chemical and Biochemical Engineering College of Chemistry and Chemical Engineering Xiamen University Xiamen P. R. China.
Baishan FangDepartment of Chemical and Biochemical Engineering College of Chemistry and Chemical Engineering Xiamen University Xiamen P. R. China.
Xiamen University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study reports the application of peptide linker in the construction of bi-functional formate dehydrogenase (FDH) and leucine dehydrogenase (LeuDH) enzymatic complex for efficient cofactor regeneration and L-tert leucine (L-tle) biotransformation. Seven FDH-LeuDH fusion enzymes with different peptide linker were successfully developed and displayed both parental enzyme activities. The incorporation order of FDH and LeuDH was investigated by predicting three-dimensional structures of LeuDH-FDH and FDH-LeuDH models using the I-TASSER server. The enzymatic characterization showed that insertion of rigid peptide linker obtained better activity and thermal stability in comparison with flexible peptide linker. The production rate of fusion enzymatic complex with suitable flexible peptide linker was increased by 1.2 times compared with free enzyme mixture. Moreover, structural analysis of FDH and LeuDH suggested the secondary structure of the N-, C-terminal domain and their relative positions to functional domains was also greatly relevant to the catalytic properties of the fusion enzymatic complex. The results show that rigid peptide linker could ensure the independent folding of moieties and stabilized enzyme structure, while the flexible peptide linker was likely to bring enzyme moieties in close proximity for superior cofactor channeling.

Indexed as

Bi‐functional enzymeFormate dehydrogenaseLeucine dehydrogenaseL‐tert leucinePeptide linker

Identifiers

PMID32624849
PMCPMC6999412
OpenAlexW2600831950

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.