Evidence map›Paper›PMID 32980502›Full record

ArticleBiochimica et biophysica acta. General subjects2021

Comparative structural and mechanistic studies of 4-hydroxy-tetrahydrodipicolinate reductases from Mycobacterium tuberculosis and Vibrio vulnificus.

Swanandi Pote, Sangita Kachhap, Nicholas J Mank, Leily Daneshian, Vincent Klapper, Sarah Pye, Amy K Arnette, Linda S Shimizu, Tomasz Borowski, Maksymilian Chruszcz

Open access · greenAbstract readComparative Study
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochimica et biophysica acta. General subjects, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
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0citing papers in PubMed
–field-weighted citation impact, top 89% 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

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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

0 citing papers in PubMed, 3 citations in OpenAlex.

No citing paper in PubMed yet.

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

10 authors at 2 institutions in 2 countries.

Swanandi PoteDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, USA.
Sangita KachhapJerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, 30-239 Krakow, Poland.
Nicholas J MankDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, USA.
Leily DaneshianDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, USA.
Vincent KlapperDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, USA.
Sarah PyeDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, USA.
Amy K ArnetteDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, USA.
Linda S ShimizuDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, USA.
Tomasz BorowskiJerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, 30-239 Krakow, Poland.
Maksymilian ChruszczDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, USA. Electronic address: chruszcz@mailbox.sc.edu.
University of South Carolina · USJerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences · PL

Funding

Metallopolymer and Antibiotic Bioconjugates against Multidrug Resistant BacteriaR01AI120987 · NIAID · UNIVERSITY OF SOUTH CAROLINA AT COLUMBIA · PI TANG, CHUANBING · 2016 to 2019
$1.4M
NIAID NIH HHS R01 AI120987
6 · The paper itself

Abstract

backgroundThe products of the lysine biosynthesis pathway, meso-diaminopimelate and lysine, are essential for bacterial survival. This paper focuses on the structural and mechanistic characterization of 4-hydroxy-tetrahydrodipicolinate reductase (DapB), which is one of the enzymes from the lysine biosynthesis pathway. DapB catalyzes the conversion of (2S, 4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate (HTPA) to 2,3,4,5-tetrahydrodipicolinate in an NADH/NADPH dependent reaction. Genes coding for DapBs were identified as essential for many pathogenic bacteria, and therefore DapB is an interesting new target for the development of antibiotics.

methodsWe have combined experimental and computational approaches to provide novel insights into mechanism of the DapB catalyzed reaction.

resultsStructures of DapBs originating from Mycobacterium tuberculosis and Vibrio vulnificus in complexes with NAD

conclusionsThis is the first report presenting the detailed mechanism of reaction catalyzed by DapB. GENERAL SIGNIFICANCE: Structural data in combination with information on the reaction mechanism provide a background for development of DapB inhibitors, including transition-state analogues.

Indexed as

Biosynthetic PathwaysCatalytic DomainHumansLysineModels, MolecularMycobacterium tuberculosisOxidoreductasesProtein ConformationSubstrate SpecificityTuberculosisVibrio InfectionsVibrio vulnificusLysineOxidoreductases4-Hydroxy-2,3,4,5-tetrahydrodipicolinateDapBDHDPDihydrodipicolinateHTPALysine biosynthesismeso-Diaminopimelate

Identifiers

PMID32980502
PMCPMC7708434
OpenAlexW3087886073

What OpenQuestion holds

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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.