Evidence map›Paper›PMID 34250527›Full record

ArticleOrganic & biomolecular chemistry2021

Characterisation of a hyperthermophilic transketolase from

Max Cárdenas-Fernández, Fabiana Subrizi, Dragana Dobrijevic, Helen C Hailes, John M Ward

Open access · hybridAbstract read
In one paragraph

Article in Organic & biomolecular chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

4 citing papers in PubMed, 13 citations in OpenAlex.

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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.

Max Cárdenas-FernándezDepartment of Biochemical Engineering, University College London, Gower Street, London WC1E 6BT, UK. m.cardenas-fernandez@kent.ac.uk j.ward@ucl.ac.uk and School of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, UK.ORCID 0000-0003-1422-5369
Fabiana SubriziDepartment of Chemistry, University College London, 20 Gordon Street, London WC1H 0AJ, UK.
Dragana DobrijevicDepartment of Biochemical Engineering, University College London, Gower Street, London WC1E 6BT, UK. m.cardenas-fernandez@kent.ac.uk j.ward@ucl.ac.uk.
Helen C HailesDepartment of Chemistry, University College London, 20 Gordon Street, London WC1H 0AJ, UK.ORCID 0000-0001-5574-4742
John M WardDepartment of Biochemical Engineering, University College London, Gower Street, London WC1E 6BT, UK. m.cardenas-fernandez@kent.ac.uk j.ward@ucl.ac.uk.ORCID 0000-0002-4415-5544
University College London · GBUniversity of Kent · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transketolase (TK) is a fundamentally important enzyme in industrial biocatalysis which carries out a stereospecific carbon-carbon bond formation, and is widely used in the synthesis of prochiral ketones. This study describes the biochemical and molecular characterisation of a novel and unusual hyperthermophilic TK from Thermotoga maritima DSM3109 (TKtmar). TKtmar has a low protein sequence homology compared to the already described TKs, with key amino acid residues in the active site highly conserved. TKtmar has a very high optimum temperature (>90 °C) and shows pronounced stability at high temperature (e.g. t1/2 99 and 9.3 h at 50 and 80 °C, respectively) and in presence of organic solvents commonly used in industry (DMSO, acetonitrile and methanol). Substrate screening showed activity towards several monosaccharides and aliphatic aldehydes. In addition, for the first time, TK specificity towards uronic acids was achieved with TKtmar catalysing the efficient conversion of d-galacturonic acid and lithium hydroxypyruvate into 7-keto-octuronic acid, a very rare C8 uronic acid, in high yields (98%, 49 mM).

Indexed as

BiocatalysisThermotoga maritimaTransketolaseEnzyme StabilitySubstrate SpecificityTransketolase

Identifiers

PMID34250527
PMCPMC8317047
OpenAlexW3179947311

What OpenQuestion holds

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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.