Evidence map›Paper›PMID 30646877›Full record

ArticleBMC structural biology2019

The human transketolase-like proteins TKTL1 and TKTL2 are bona fide transketolases.

Gaurang P Deshpande, Hugh-George Patterton, M Faadiel Essop

Open access · hybridAbstract read
In one paragraph

Article in BMC structural biology, 2019. 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
2.0field-weighted citation impact, top 17% 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, 27 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

3 authors at 1 institution in 1 country.

Gaurang P DeshpandeCardio-Metabolic Research Group (CMRG), Department of Physiological Sciences, Stellenbosch University, Room 2005, Mike De Vries Building, Merriman Avenue, Stellenbosch, 7600, South Africa.
Hugh-George PattertonCentre for Bioinformatics and Computational Biology, Stellenbosch University, Stellenbosch, 7600, South Africa.
M Faadiel EssopCardio-Metabolic Research Group (CMRG), Department of Physiological Sciences, Stellenbosch University, Room 2005, Mike De Vries Building, Merriman Avenue, Stellenbosch, 7600, South Africa. mfessop@sun.ac.za.ORCID 0000-0002-8434-4294
Stellenbosch University · ZA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThree transketolase genes have been identified in the human genome to date: transketolase (TKT), transketolase-like 1 (TKTL1) and transketolase-like 2 (TKTL2). Altered TKT functionality is strongly implicated in the development of diabetes and various cancers, thus offering possible therapeutic utility. It will be of great value to know whether TKTL1 and TKTL2 are, similarly, potential therapeutic targets. However, it remains unclear whether TKTL1 and TKTL2 are functional transketolases.

resultsHomology modelling of TKTL1 and TKTL2 using TKT as template, revealed that both TKTL1 and TKTL2 could assume a folded structure like TKT. TKTL1/2 presented a cleft of suitable dimensions between the homodimer surfaces that could accommodate the co-factor-substrate. An appropriate cavity and a hydrophobic nodule were also present in TKTL1/2, into which the diphosphate group fitted, and that was implicated in aminopyrimidine and thiazole ring binding in TKT, respectively. The presence of several identical residues at structurally equivalent positions in TKTL1/2 and TKT identified a network of interactions between the protein and co-factor-substrate, suggesting the functional fidelity of TKTL1/2 as transketolases.

conclusionsOur data support the hypothesis that TKTL1 and TKTL2 are functional transketolases and represent novel therapeutic targets for diabetes and cancer.

Indexed as

HumansHydrogen BondingModels, MolecularMolecular Dynamics SimulationProtein BindingProtein ConformationProtein FoldingPyrimidinesStructural Homology, ProteinThiazolesTransketolase2-aminopyrimidinePyrimidinesThiazolesTKTL1 protein, humanTransketolaseGlycolysisPentose phosphate pathwayThiamineTransketolaseTransketolase-like 1Transketolase-like 2

Identifiers

PMID30646877
PMCPMC6334435
OpenAlexW2909431770

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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.