Evidence map›Paper›PMID 21545144›Full record

ArticleBiochemistry2011

Three-dimensional structure and catalytic mechanism of cytosine deaminase.

Richard S Hall, Alexander A Fedorov, Chengfu Xu, Elena V Fedorov, Steven C Almo, Frank M Raushel

Abstract read
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

22 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. The Discovery ofACS catalysis · 2026
    Article
  3. Article
  4. International journal of molecular sciences · 2025
    Article
  5. Review
  6. Article
  7. Why is manganese so valuable to bacterial pathogens?Frontiers in cellular and infection microbiology · 2023
    Review
  8. Article
  9. The current toolbox for APOBEC drug discovery.Trends in pharmacological sciences · 2022
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. The bacterialThe Journal of biological chemistry · 2017
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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 1 country.

Richard S HallDepartment of Chemistry, Texas A&M University, College Station, Texas 77842-3012, United States.
Alexander A Fedorov
Chengfu Xu
Elena V Fedorov
Steven C Almo
Frank M Raushel
Albert Einstein College of Medicine · USTexas A&M University · US

Funding

Theoretical and Computational ApproachesP01GM071790 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI RAUSHEL, FRANK M. · 2004 to 2013
$15.5M
NIGMS NIH HHS GM 71790NIGMS NIH HHS P01 GM071790
6 · The paper itself

Abstract

Cytosine deaminase (CDA) from E. coli is a member of the amidohydrolase superfamily. The structure of the zinc-activated enzyme was determined in the presence of phosphonocytosine, a mimic of the tetrahedral reaction intermediate. This compound inhibits the deamination of cytosine with a K(i) of 52 nM. The zinc- and iron-containing enzymes were characterized to determine the effect of the divalent cations on activation of the hydrolytic water. Fe-CDA loses activity at low pH with a kinetic pK(a) of 6.0, and Zn-CDA has a kinetic pK(a) of 7.3. Mutation of Gln-156 decreased the catalytic activity by more than 5 orders of magnitude, supporting its role in substrate binding. Mutation of Glu-217, Asp-313, and His-246 significantly decreased catalytic activity supporting the role of these three residues in activation of the hydrolytic water molecule and facilitation of proton transfer reactions. A library of potential substrates was used to probe the structural determinants responsible for catalytic activity. CDA was able to catalyze the deamination of isocytosine and the hydrolysis of 3-oxauracil. Large inverse solvent isotope effects were obtained on k(cat) and k(cat)/K(m), consistent with the formation of a low-barrier hydrogen bond during the conversion of cytosine to uracil. A chemical mechanism for substrate deamination by CDA was proposed.

Indexed as

CatalysisCytosineCytosine DeaminaseEscherichia coliEscherichia coli ProteinsGlutamic AcidHydrogen BondingHydrogen-Ion ConcentrationKineticsModels, MolecularZinccodA protein, E coliCytosineCytosine DeaminaseEscherichia coli ProteinsGlutamic AcidZinc

Identifiers

PMID21545144
PMCPMC3107989
OpenAlexW2015967099

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.