Evidence map›Paper›PMID 29070681›Full record

ArticleThe Journal of biological chemistry2017

Differential catalytic promiscuity of the alkaline phosphatase superfamily bimetallo core reveals mechanistic features underlying enzyme evolution.

Fanny Sunden, Ishraq AlSadhan, Artem Lyubimov, Tzanko Doukov, Jeffrey Swan, Daniel Herschlag

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 15% 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

15 citing papers in PubMed, 33 citations in OpenAlex.

  1. Widespread promiscuous alkaline phosphatases underscore ancient microbial phosphite utilization.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  8. ENPP1's regulation of extracellular cGAMP is a ubiquitous mechanism of attenuating STING signaling.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Bu-Gu-Sheng-Sui decoction promotes osteogenesisFrontiers in pharmacology · 2022
    Article
  10. High throughput and quantitative enzymology in the genomic era.Current opinion in structural biology · 2021
    Review
  11. Article
  12. A mechanistic view of enzyme evolution.Protein science : a publication of the Protein Society · 2020
    Review
  13. Article
  14. Article
  15. Evolutionary repurposing of a sulfatase: A new Michaelis complex leads to efficient transition state charge offset.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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

6 authors at 2 institutions in 2 countries.

Fanny SundenFrom the Department of Biochemistry, Beckman Center.
Ishraq AlSadhanFrom the Department of Biochemistry, Beckman Center.
Artem Lyubimovthe Departments of Molecular and Cellular Physiology.
Tzanko Doukovthe Macromolecular Crystallographic Group, Stanford Synchrotron Radiation Lightsource, National Accelerator Laboratory, Stanford University, Stanford, California 94309.
Jeffrey SwanFrom the Department of Biochemistry, Beckman Center.
Daniel HerschlagFrom the Department of Biochemistry, Beckman Center, herschla@stanford.edu.
Stanford University · USStanford Medicine · US

Funding

Study of Nonenzymatic and Enzymatic Phosphoryl TransferR01GM064798 · NIGMS · STANFORD UNIVERSITY · PI Polly Morrell Fordyce, DANIEL HERSCHLAG · 2002 to 2026
$5.9M
Enzymology of a Catalytic RNA MoleculeR37GM049243 · NIGMS · STANFORD UNIVERSITY · PI HERSCHLAG, DANIEL · 2002 to 2011
$4.2M
ENZYMOLOGY OF A CATALYTIC RNA MOLECULER01GM049243 · NIGMS · STANFORD UNIVERSITY · PI HERSCHLAG, DANIEL · 1993 to 2016
$2.3M
NIGMS NIH HHS R01 GM049243NIGMS NIH HHS R01 GM064798NIGMS NIH HHS R37 GM049243
6 · The paper itself

Abstract

Members of enzyme superfamilies specialize in different reactions but often exhibit catalytic promiscuity for one another's reactions, consistent with catalytic promiscuity as an important driver in the evolution of new enzymes. Wanting to understand how catalytic promiscuity and other factors may influence evolution across a superfamily, we turned to the well-studied alkaline phosphatase (AP) superfamily, comparing three of its members, two evolutionarily distinct phosphatases and a phosphodiesterase. We mutated distinguishing active-site residues to generate enzymes that had a common Zn

Indexed as

Evolution, MolecularAlkaline PhosphataseBacterial ProteinsBiocatalysisCatalytic DomainChryseobacteriumCrystallography, X-RayEscherichia coliEscherichia coli ProteinsKineticsModels, MolecularMutagenesis, Site-DirectedPhosphoric Diester HydrolasesPyrophosphatasesSubstrate SpecificityXanthomonasAlkaline PhosphataseBacterial ProteinsEscherichia coli Proteinsnucleotide pyrophosphatase - phosphodiesterase Iperiplasmic alkaline phosphatase, Chryseobacterium meningosepticumPhosphoric Diester HydrolasesPyrophosphatasesZincenzymeenzyme catalysisevolutionphosphatasesubstrate specificity

Identifiers

PMID29070681
PMCPMC5743071
OpenAlexW2766457884

What OpenQuestion holds

Textmetadata
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.