Evidence map›Paper›PMID 27423402›Full record

ArticleJournal of molecular biology2016

Chopping and Changing: the Evolution of the Flavin-dependent Monooxygenases.

Maria Laura Mascotti, Maximiliano Juri Ayub, Nicholas Furnham, Janet M Thornton, Roman A Laskowski

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

48 citing papers in PubMed, 105 citations in OpenAlex.

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  7. Unlocking the catalytic precision of ligand-controlled enzymatic halogenation.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  14. Structure and Function of the α-Hydroxylation Bimodule of the Mupirocin Polyketide Synthase.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023
    Article
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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

5 authors at 3 institutions in 2 countries.

Maria Laura MascottiIMIBIO-SL CONICET, Facultad de Química Bioquímica y Farmacia, Universidad Nacional de San Luis, Ejército de los Andes 950, San Luis D5700HHW, Argentina. Electronic address: mlmascotti@unsl.edu.ar.
Maximiliano Juri AyubIMIBIO-SL CONICET, Facultad de Química Bioquímica y Farmacia, Universidad Nacional de San Luis, Ejército de los Andes 950, San Luis D5700HHW, Argentina.
Nicholas FurnhamDepartment of Pathogen Molecular Biology, London School of Hygiene and Tropical Medicine, Keppel Street, London WC1E 7HT, UK.
Janet M ThorntonEMBL-EBI, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, UK.
Roman A LaskowskiEMBL-EBI, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, UK. Electronic address: roman@ebi.ac.uk.
Consejo Nacional de Investigaciones Científicas y Técnicas · AREuropean Bioinformatics Institute · GBUniversity of London · GB

Funding

Medical Research Council MR/K020420/1
6 · The paper itself

Abstract

Flavin-dependent monooxygenases play a variety of key physiological roles and are also very powerful biotechnological tools. These enzymes have been classified into eight different classes (A-H) based on their sequences and biochemical features. By combining structural and sequence analysis, and phylogenetic inference, we have explored the evolutionary history of classes A, B, E, F, and G and demonstrate that their multidomain architectures reflect their phylogenetic relationships, suggesting that the main evolutionary steps in their divergence are likely to have arisen from the recruitment of different domains. Additionally, the functional divergence within in each class appears to have been the result of other mechanisms such as a complex set of single-point mutations. Our results reinforce the idea that a main constraint on the evolution of cofactor-dependent enzymes is the functional binding of the cofactor. Additionally, a remarkable feature of this family is that the sequence of the key flavin adenine dinucleotide-binding domain is split into at least two parts in all classes studied here. We propose a complex set of evolutionary events that gave rise to the origin of the different classes within this family.

Indexed as

Biological EvolutionCoenzymesFlavinsMixed Function OxygenasesPhylogenyProtein DomainsSequence AnalysisCoenzymesFlavinsMixed Function Oxygenasescofactor-binding enzymesenzyme evolutionflavin-dependent monooxygenasesmultidomain architecture

Identifiers

PMID27423402
PMCPMC4981433
OpenAlexW2488883307

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.