Evidence map›Paper›PMID 27322068›Full record

ArticleNature chemical biology2016

A family of metal-dependent phosphatases implicated in metabolite damage-control.

Lili Huang, Anna Khusnutdinova, Boguslaw Nocek, Greg Brown, Xiaohui Xu, Hong Cui, Pierre Petit, Robert Flick, Rémi Zallot, Kelly Balmant and 9 more

Abstract read
In one paragraph

Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

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  19. PKAN pathogenesis and treatment.Molecular genetics and metabolism · 2022
    Review
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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

19 authors.

Lili HuangFood Science and Human Nutrition Department, University of Florida, Gainesville, Florida, USA.
Anna KhusnutdinovaDepartment of Chemical Engineering &Applied Chemistry, University of Toronto, Toronto, Ontario, Canada.
Boguslaw NocekMidwest Center for Structural Genomics and Structural Biology Center, Biosciences Division, Argonne National Laboratory, Argonne, Illinois, USA.
Greg BrownDepartment of Chemical Engineering &Applied Chemistry, University of Toronto, Toronto, Ontario, Canada.
Xiaohui XuDepartment of Chemical Engineering &Applied Chemistry, University of Toronto, Toronto, Ontario, Canada.
Hong CuiDepartment of Chemical Engineering &Applied Chemistry, University of Toronto, Toronto, Ontario, Canada.
Pierre PetitDepartment of Chemical Engineering &Applied Chemistry, University of Toronto, Toronto, Ontario, Canada.
Robert FlickDepartment of Chemical Engineering &Applied Chemistry, University of Toronto, Toronto, Ontario, Canada.
Rémi ZallotMicrobiology and Cell Science Department, University of Florida, Gainesville, Florida, USA.
Kelly BalmantPlant Molecular and Cellular Biology Program, University of Florida, Gainesville, Florida, USA.
Michael J ZiemakHorticultural Sciences Department, University of Florida, Gainesville, Florida, USA.
John ShanklinBiological, Environmental, and Climate Sciences Department, Brookhaven National Laboratory, Upton, New York, USA.
Valérie de Crécy-LagardMicrobiology and Cell Science Department, University of Florida, Gainesville, Florida, USA.
Oliver FiehnMetabolomics Core, UC Davis Genome Center, University of California, Davis, Davis, California, USA.ORCID 0000-0002-6261-8928
Jesse F GregoryFood Science and Human Nutrition Department, University of Florida, Gainesville, Florida, USA.
Andrzej JoachimiakMidwest Center for Structural Genomics and Structural Biology Center, Biosciences Division, Argonne National Laboratory, Argonne, Illinois, USA.
Alexei SavchenkoDepartment of Chemical Engineering &Applied Chemistry, University of Toronto, Toronto, Ontario, Canada.
Alexander F YakuninDepartment of Chemical Engineering &Applied Chemistry, University of Toronto, Toronto, Ontario, Canada.ORCID 0000-0003-0813-6490
Andrew D HansonHorticultural Sciences Department, University of Florida, Gainesville, Florida, USA.

Funding

Midwest Center for Structural GenomicsU54GM094585 · NIGMS · UNIVERSITY OF CHICAGO · PI MINOR, WLADEK · 2010 to 2014
$33.7M
NIGMS NIH HHS U54 GM094585
6 · The paper itself

Abstract

DUF89 family proteins occur widely in both prokaryotes and eukaryotes, but their functions are unknown. Here we define three DUF89 subfamilies (I, II, and III), with subfamily II being split into stand-alone proteins and proteins fused to pantothenate kinase (PanK). We demonstrated that DUF89 proteins have metal-dependent phosphatase activity against reactive phosphoesters or their damaged forms, notably sugar phosphates (subfamilies II and III), phosphopantetheine and its S-sulfonate or sulfonate (subfamily II-PanK fusions), and nucleotides (subfamily I). Genetic and comparative genomic data strongly associated DUF89 genes with phosphoester metabolism. The crystal structure of the yeast (Saccharomyces cerevisiae) subfamily III protein YMR027W revealed a novel phosphatase active site with fructose 6-phosphate and Mg(2+) bound near conserved signature residues Asp254 and Asn255 that are critical for activity. These findings indicate that DUF89 proteins are previously unrecognized hydrolases whose characteristic in vivo function is to limit potentially harmful buildups of normal or damaged phosphometabolites.

Indexed as

Catalytic DomainMetalsModels, MolecularPhosphoric Monoester HydrolasesPhosphoric Triester HydrolasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMetalsPhosphoric Monoester HydrolasesPhosphoric Triester HydrolasesSaccharomyces cerevisiae ProteinsYMR027W protein, S cerevisiae

Identifiers

PMID27322068
PMCPMC7001580

What OpenQuestion holds

Textmetadata
LicenceTDM
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.