Evidence map›Paper›PMID 22035792›Full record

ArticleChemistry & biology2011

Structural and mechanistic insights into C-P bond hydrolysis by phosphonoacetate hydrolase.

Vinayak Agarwal, Svetlana A Borisova, William W Metcalf, Wilfred A van der Donk, Satish K Nair

Abstract read
In one paragraph

Article in Chemistry & biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

21 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Structure-function analysis of PorXScientific reports · 2024
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. c-di-AMP hydrolysis by the phosphodiesterase AtaC promotes differentiation of multicellular bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Journal of applied crystallography · 2014
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. Answers to the carbon-phosphorus lyase conundrum.Chembiochem : a European journal of chemical biology · 2012
    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

5 authors at 2 institutions in 1 country.

Vinayak AgarwalCenter for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Svetlana A Borisova
William W Metcalf
Wilfred A van der Donk
Satish K Nair
University of Illinois Urbana-Champaign · USHoward Hughes Medical Institute · US

Funding

Structural Elucidation and Biosynthesis P01GM077596 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI METCALF, WILLIAM W · 2007 to 2016
$15.3M
Howard Hughes Medical InstituteNIGMS NIH HHS P01 GM077596
6 · The paper itself

Abstract

Bacteria have evolved pathways to metabolize phosphonates as a nutrient source for phosphorus. In Sinorhizobium meliloti 1021, 2-aminoethylphosphonate is catabolized to phosphonoacetate, which is converted to acetate and inorganic phosphate by phosphonoacetate hydrolase (PhnA). Here we present detailed biochemical and structural characterization of PhnA that provides insights into the mechanism of C-P bond cleavage. The 1.35 Å resolution crystal structure reveals a catalytic core similar to those of alkaline phosphatases and nucleotide pyrophosphatases but with notable differences, such as a longer metal-metal distance. Detailed structure-guided analysis of active site residues and four additional cocrystal structures with phosphonoacetate substrate, acetate, phosphonoformate inhibitor, and a covalently bound transition state mimic provide insight into active site features that may facilitate cleavage of the C-P bond. These studies expand upon the array of reactions that can be catalyzed by enzymes of the alkaline phosphatase superfamily.

Indexed as

AcetatesAlkaline PhosphataseBacterial ProteinsCatalytic DomainCrystallography, X-RayEnzyme InhibitorsHydrolysisMetalsModels, MolecularPhosphonoacetic AcidProtein ConformationSinorhizobium melilotiSubstrate SpecificityAcetatesAlkaline PhosphataseBacterial ProteinsEnzyme InhibitorsMetalsphosphonoacetate hydrolasePhosphonoacetic Acid

Identifiers

PMID22035792
PMCPMC4321816
OpenAlexW2057851278

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.