Evidence map›Paper›PMID 33036250›Full record

ArticleBiomolecules2020

Dissecting the Cytochrome P450 OleP Substrate Specificity: Evidence for a Preferential Substrate.

Giacomo Parisi, Ida Freda, Cécile Exertier, Cristina Cecchetti, Elena Gugole, Gabriele Cerutti, Lucia D'Auria, Alberto Macone, Beatrice Vallone, Carmelinda Savino and 1 more

Abstract read
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In one paragraph

Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

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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

11 authors.

Giacomo ParisiIstituto Pasteur-Fondazione Cenci Bolognetti and Department of Biochemical Sciences "Alessandro Rossi Fanelli", Sapienza, University of Rome, P. le Aldo Moro, 5, 00185 Rome, Italy.ORCID 0000-0002-3064-0928
Ida FredaIstituto Pasteur-Fondazione Cenci Bolognetti and Department of Biochemical Sciences "Alessandro Rossi Fanelli", Sapienza, University of Rome, P. le Aldo Moro, 5, 00185 Rome, Italy.ORCID 0000-0002-0756-9537
Cécile ExertierIstituto Pasteur-Fondazione Cenci Bolognetti and Department of Biochemical Sciences "Alessandro Rossi Fanelli", Sapienza, University of Rome, P. le Aldo Moro, 5, 00185 Rome, Italy.ORCID 0000-0001-7457-6895
Cristina CecchettiIstituto Pasteur-Fondazione Cenci Bolognetti and Department of Biochemical Sciences "Alessandro Rossi Fanelli", Sapienza, University of Rome, P. le Aldo Moro, 5, 00185 Rome, Italy.
Elena GugoleIstituto Pasteur-Fondazione Cenci Bolognetti and Department of Biochemical Sciences "Alessandro Rossi Fanelli", Sapienza, University of Rome, P. le Aldo Moro, 5, 00185 Rome, Italy.
Gabriele CeruttiIstituto Pasteur-Fondazione Cenci Bolognetti and Department of Biochemical Sciences "Alessandro Rossi Fanelli", Sapienza, University of Rome, P. le Aldo Moro, 5, 00185 Rome, Italy.
Lucia D'AuriaDepartment of Biochemical Sciences "Alessandro Rossi Fanelli", Sapienza, University of Rome, P. le Aldo Moro, 5, 00185 Rome, Italy.
Alberto MaconeDepartment of Biochemical Sciences "Alessandro Rossi Fanelli", Sapienza, University of Rome, P. le Aldo Moro, 5, 00185 Rome, Italy.ORCID 0000-0003-0455-1400
Beatrice ValloneIstituto Pasteur-Fondazione Cenci Bolognetti and Department of Biochemical Sciences "Alessandro Rossi Fanelli", Sapienza, University of Rome, P. le Aldo Moro, 5, 00185 Rome, Italy.
Carmelinda SavinoInstitute of Molecular Biology and Pathology c/o Department of Biochemical Sciences "Alessandro Rossi Fanelli", Sapienza, University of Rome, National Research Council, P.le Aldo Moro, 5, 00185 Rome, Italy.
Linda Celeste MontemiglioInstitute of Molecular Biology and Pathology c/o Department of Biochemical Sciences "Alessandro Rossi Fanelli", Sapienza, University of Rome, National Research Council, P.le Aldo Moro, 5, 00185 Rome, Italy.

Funding

Horizon 2020 823780Istituto Pasteur-Fondazione Cenci Bolognetti no protocol number providedSapienza Università di Roma RM118164227A5FD6
6 · The paper itself

Abstract

The cytochrome P450 OleP catalyzes the epoxidation of aliphatic carbons on both the aglycone 8.8a-deoxyoleandolide (DEO) and the monoglycosylated L-olivosyl-8.8a-deoxyoleandolide (L-O-DEO) intermediates of oleandomycin biosynthesis. We investigated the substrate versatility of the enzyme. X-ray and equilibrium binding data show that the aglycone DEO loosely fits the OleP active site, triggering the closure that prepares it for catalysis only on a minor population of enzyme. The open-to-closed state transition allows solvent molecules to accumulate in a cavity that forms upon closure, mediating protein-substrate interactions.

Indexed as

CatalysisCrystallography, X-RayCytochrome P-450 Enzyme SystemLactonesProtein DomainsRhamnoseStructure-Activity RelationshipSubstrate SpecificityCytochrome P-450 Enzyme SystemLactonesoleandolideRhamnose8.8a-deoxyoleandolideCYP107D1cytochrome P450molecular dockingoleandomycinOlePpreferential substrateX-ray crystallography

Identifiers

PMID33036250
PMCPMC7600006

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.