Evidence map›Paper›PMID 21605342›Full record

ReviewThe FEBS journal2011

Characterizing the complexity of enzymes on the basis of their mechanisms and structures with a bio-computational analysis.

Gemma L Holliday, Julia D Fischer, John B O Mitchell, Janet M Thornton

Open access · bronzeAbstract readReview
In one paragraph

Review in The FEBS journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

18 citing papers in PubMed, 34 citations in OpenAlex.

  1. Can the origin of biosynthetic routes be explained by a Frankenstein's monster-like spontaneous assembly of prebiotic reactants?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Article
  2. Article
  3. Deletion of a previously uncharacterized lipoprotein lirL confers resistance to an inhibitor of type II signal peptidase inProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Can an Imidazole Be Formed from an Alanyl-Seryl-Glycine Tripeptide under Possible Prebiotic Conditions?Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 2017
    Article
  12. Electric Fields and Enzyme Catalysis.Annual review of biochemistry · 2017
    Review
  13. Extending enzyme molecular recognition with an expanded amino acid alphabet.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  14. Biocuration in the structure-function linkage database: the anatomy of a superfamily.Database : the journal of biological databases and curation · 2017
    Article
  15. Article
  16. The natural history of biocatalytic mechanisms.PLoS computational biology · 2014
    Article
  17. Enzyme informatics.Current topics in medicinal chemistry · 2012
    Review
  18. 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

4 authors at 2 institutions in 1 country.

Gemma L HollidayEMBL-EBI, Wellcome Trust Genome Campus, Cambridge, UK. gemma@ebi.ac.uk
Julia D Fischer
John B O Mitchell
Janet M Thornton
European Bioinformatics Institute · GBUniversity of St Andrews · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Enzymes are basically composed of 20 naturally occurring amino acids, yet they catalyse a dizzying array of chemical reactions, with regiospecificity and stereospecificity and under physiological conditions. In this review, we attempt to gain some understanding of these complex proteins, from the chemical versatility of the catalytic toolkit, including the use of cofactors (both metal ions and organic molecules), to the complex mapping of reactions to proteins (which is rarely one-to-one), and finally the structural complexity of enzymes and their active sites, often involving multidomain or multisubunit assemblies. This work highlights how the enzymes that we see today reflect millions of years of evolution, involving de novo design followed by exquisite regulation and modulation to create optimal fitness for life.

Indexed as

Catalytic DomainComputational BiologyComputer SimulationModels, MolecularAmino AcidsAnimalsCoenzymesEnzymesHumansMolecular StructureAmino AcidsCoenzymesEnzymes

Identifiers

PMID21605342
PMCPMC3258480
OpenAlexW2155260111

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.