Conversion of five proluciferin esters by human cytochrome P450 enzymes.

cytochrome P450 drug metabolism fission yeast luminescence proluciferin ester

Journal

Biotechnology journal
ISSN: 1860-7314
Titre abrégé: Biotechnol J
Pays: Germany
ID NLM: 101265833

Informations de publication

Date de publication:
Jul 2021
Historique:
revised: 07 04 2021
received: 06 01 2021
accepted: 09 04 2021
pubmed: 29 4 2021
medline: 10 7 2021
entrez: 28 4 2021
Statut: ppublish

Résumé

Probe substrates are an important tool for activity monitoring of human drug metabolizing enzymes such as cytochromes P450 (CYPs). In the present study we have tested human CYPs for metabolization of five proluciferin ester substrates which had previously only been known to be hydroxylated by CYP26A1. It was found that these substrates were converted by another 21 human CYPs, which belong to the CYP families 1 to 4, 7, and 26. Thus, 66 new pairs of enzyme and substrate were identified. Correlation analysis indicated the presence of three distinct sets of enzymes with high similarity in their activity profiles that encompass a total of 16 individual enzymes. Some of these newly identified correlations may serve as a starting point for further study of those human CYPs whose activities are not yet satisfactorily understood.

Sections du résumé

BACKGROUND BACKGROUND
Probe substrates are an important tool for activity monitoring of human drug metabolizing enzymes such as cytochromes P450 (CYPs).
BRIEF METHODS UNASSIGNED
In the present study we have tested human CYPs for metabolization of five proluciferin ester substrates which had previously only been known to be hydroxylated by CYP26A1.
MAJOR RESULTS RESULTS
It was found that these substrates were converted by another 21 human CYPs, which belong to the CYP families 1 to 4, 7, and 26. Thus, 66 new pairs of enzyme and substrate were identified. Correlation analysis indicated the presence of three distinct sets of enzymes with high similarity in their activity profiles that encompass a total of 16 individual enzymes.
CONCLUSIONS CONCLUSIONS
Some of these newly identified correlations may serve as a starting point for further study of those human CYPs whose activities are not yet satisfactorily understood.

Identifiants

pubmed: 33909340
doi: 10.1002/biot.202100007
doi:

Substances chimiques

Esters 0
Cytochrome P-450 Enzyme System 9035-51-2

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

e2100007

Informations de copyright

© 2021 Wiley-VCH GmbH.

Références

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Auteurs

Shishir Sharma (S)

School of Pharmaceutical Science and Technology, Health Sciences Platform, Tianjin University, Tianjin, China.

Sangeeta Shrestha Sharma (SS)

School of Pharmaceutical Science and Technology, Health Sciences Platform, Tianjin University, Tianjin, China.

Xue Zhang (X)

School of Pharmaceutical Science and Technology, Health Sciences Platform, Tianjin University, Tianjin, China.

Jan-Philipp Bureik (JP)

Laboratoire Charles Fabry, Institut d'Optique Graduate School, CNRS, Université Paris Saclay, Palaiseau cedex, France.

Erik J Sorensen (EJ)

School of Pharmaceutical Science and Technology, Health Sciences Platform, Tianjin University, Tianjin, China.
Department of Chemistry, Princeton University, Princeton, New Jersey, USA.

Matthias Bureik (M)

School of Pharmaceutical Science and Technology, Health Sciences Platform, Tianjin University, Tianjin, China.

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