Evidence map›Paper›PMID 32557118›Full record

ArticleBiotechnology letters2020

Engineered formate dehydrogenase from Chaetomium thermophilum, a promising enzymatic solution for biotechnical CO

Mehmet M Çakar, Jouni Ruupunen, Juan Mangas-Sanchez, William R Birmingham, Deniz Yildirim, Ossi Turunen, Nicholas J Turner, Jarkko Valjakka, Barış Binay

Abstract read
PubMed Publisher
In one paragraph

Article in Biotechnology letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

9 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Direct Biocatalytic Processes for COMolecules (Basel, Switzerland) · 2023
    Review
  4. Review
  5. Article
  6. Real flue gas COFrontiers in bioengineering and biotechnology · 2023
    Article
  7. Article
  8. Review
  9. 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

9 authors at 5 institutions in 3 countries.

Mehmet M ÇakarDepartment of Molecular Biology and Genetics, Gebze Technical University, 41400, Gebze, Kocaeli, Turkey.
Jouni RuupunenFaculty of Medicine and Health Technology, Tampere University, 33014, Tampereen yliopisto, Finland.
Juan Mangas-SanchezManchester Institute of Biotechnology, School of Chemistry, University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
William R BirminghamManchester Institute of Biotechnology, School of Chemistry, University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
Deniz YildirimDepartment of Chemistry, Cukurova University, 01330, Adana, Turkey.
Ossi TurunenSchool of Forest Sciences, University of Eastern Finland, 80101, Joensuu, Finland.
Nicholas J TurnerManchester Institute of Biotechnology, School of Chemistry, University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK. nicholas.turner@manchester.ac.uk.ORCID http://orcid.org/0000-0002-8708-0781
Jarkko ValjakkaFaculty of Medicine and Health Technology, Tampere University, 33014, Tampereen yliopisto, Finland.
Barış BinayDepartment of Bioengineering, Gebze Technical University, 41400, Gebze, Kocaeli, Turkey. binay@gtu.edu.tr.ORCID http://orcid.org/0000-0002-6190-6549
University of Manchester · GBGebze Technical University · TRTampere University · FICukurova University · TRUniversity of Eastern Finland · FI

Funding

TUBITAK 214Z292
6 · The paper itself

Abstract

objectivesFormate dehydrogenases (FDHs) are NAD(P)H-dependent enzymes that catalyse the reversible oxidation of formate to CO

resultsFour libraries were constructed targeting five residues in the active site. We identified two variants (G93H/I94Y and R259C) with enhanced reduction activity which were characterised in the presence of both aqueous CO

conclusionsTwo variants presenting up to five-fold increase in catalytic efficiency and k

Indexed as

MutationAlcohol DehydrogenaseBiocatalysisCarbon DioxideCatalytic DomainChaetomiumDirected Molecular EvolutionFormate DehydrogenasesFormatesFungal ProteinsOxidation-ReductionPropanolsProtein EngineeringStreptomyces coelicolor1-phenylpropanolAlcohol DehydrogenaseCarbon DioxideFormate DehydrogenasesFormatesformic acidFungal ProteinsPropanolsBiotransformationCO2 reductionEnzyme engineeringMolecular dynamicsNAD+-dependent FDH

Identifiers

PMID32557118
OpenAlexW3036284899

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.