Evidence map›Paper›PMID 30577795›Full record

ArticleBMC evolutionary biology2018

Classification, substrate specificity and structural features of D-2-hydroxyacid dehydrogenases: 2HADH knowledgebase.

Dorota Matelska, Ivan G Shabalin, Jagoda Jabłońska, Marcin J Domagalski, Jan Kutner, Krzysztof Ginalski, Wladek Minor

Erratum issuedAbstract read
In one paragraph

Article in BMC evolutionary biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

20 citing papers in PubMed.

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  16. The diversity and evolution of microbial dissimilatory phosphite oxidation.Proceedings of the National Academy of Sciences of the United States of America · 2021
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Dorota MatelskaDepartment of Molecular Physiology and Biological Physics, University of Virginia, 1340 Jefferson Park Avenue, Charlottesville, VA, 22908, USA.
Ivan G ShabalinDepartment of Molecular Physiology and Biological Physics, University of Virginia, 1340 Jefferson Park Avenue, Charlottesville, VA, 22908, USA.
Jagoda JabłońskaLaboratory of Bioinformatics and Systems Biology, Centre of New Technologies, University of Warsaw, Zwirki i Wigury 93, 02-089, Warsaw, Poland.
Marcin J DomagalskiDepartment of Molecular Physiology and Biological Physics, University of Virginia, 1340 Jefferson Park Avenue, Charlottesville, VA, 22908, USA.
Jan KutnerDepartment of Molecular Physiology and Biological Physics, University of Virginia, 1340 Jefferson Park Avenue, Charlottesville, VA, 22908, USA.
Krzysztof GinalskiLaboratory of Bioinformatics and Systems Biology, Centre of New Technologies, University of Warsaw, Zwirki i Wigury 93, 02-089, Warsaw, Poland. k.ginalski@cent.uw.edu.pl.
Wladek MinorDepartment of Molecular Physiology and Biological Physics, University of Virginia, 1340 Jefferson Park Avenue, Charlottesville, VA, 22908, USA. wladek@iwonka.med.virginia.edu.

Funding

The NYSGRC: A Large Scale Center for PSI:BiologyU54GM094662 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI SEIDEL, RONALD D · 2010 to 2014
$32.6M
Integrated resource for reproducibility in macromolecular crystallographyU01HG008424 · NHGRI · UNIVERSITY OF VIRGINIA · PI MINOR, WLADEK · 2015 to 2017
$1.5M
Accurate measurements of phasing signal to determine macromolecular structuresR01GM118619 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI OTWINOWSKI, ZBYSZEK · 2017 to 2020
$1.3M
NHGRI NIH HHS U01 HG008424NIAID NIH HHS HHSN272201200026CNIAID NIH HHS HHSN272201700060CNIGMS NIH HHS R01 GM118619NIGMS NIH HHS U54 GM094662NIH HHS GM094662NIH HHS GM118619NIH HHS HG008424
6 · The paper itself

Abstract

backgroundThe family of D-isomer specific 2-hydroxyacid dehydrogenases (2HADHs) contains a wide range of oxidoreductases with various metabolic roles as well as biotechnological applications. Despite a vast amount of biochemical and structural data for various representatives of the family, the long and complex evolution and broad sequence diversity hinder functional annotations for uncharacterized members.

resultsWe report an in-depth phylogenetic analysis, followed by mapping of available biochemical and structural data on the reconstructed phylogenetic tree. The analysis suggests that some subfamilies comprising enzymes with similar yet broad substrate specificity profiles diverged early in the evolution of 2HADHs. Based on the phylogenetic tree, we present a revised classification of the family that comprises 22 subfamilies, including 13 new subfamilies not studied biochemically. We summarize characteristics of the nine biochemically studied subfamilies by aggregating all available sequence, biochemical, and structural data, providing comprehensive descriptions of the active site, cofactor-binding residues, and potential roles of specific structural regions in substrate recognition. In addition, we concisely present our analysis as an online 2HADH enzymes knowledgebase.

conclusionsThe knowledgebase enables navigation over the 2HADHs classification, search through collected data, and functional predictions of uncharacterized 2HADHs. Future characterization of the new subfamilies may result in discoveries of enzymes with novel metabolic roles and with properties beneficial for biotechnological applications.

Indexed as

Knowledge BasesAlcohol OxidoreductasesAmino Acid SequenceCatalytic DomainCoenzymesLikelihood FunctionsPhylogenySubstrate SpecificityAlcohol OxidoreductasesCoenzymesD-2-hydroxyacid dehydrogenaseD-isomer specific 2-hydroxyacid dehydrogenasesMolecular evolutionSequence-structure-function relationshipSubstrate promiscuitySubstrate specificity

Identifiers

PMID30577795
PMCPMC6303947

What OpenQuestion holds

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Registered trials

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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.