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Conversion of five proluciferin esters by human cytochrome P450 enzymes
Author(s) -
Sharma Shishir,
Sharma Sangeeta Shrestha,
Zhang Xue,
Bureik JanPhilipp,
Sorensen Erik J.,
Bureik Matthias
Publication year - 2021
Publication title -
biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.144
H-Index - 84
eISSN - 1860-7314
pISSN - 1860-6768
DOI - 10.1002/biot.202100007
Subject(s) - cytochrome p450 , enzyme , biochemistry , substrate (aquarium) , similarity (geometry) , chemistry , cytochrome , biology , ecology , artificial intelligence , computer science , image (mathematics)
Background Probe substrates are an important tool for activity monitoring of human drug metabolizing enzymes such as cytochromes P450 (CYPs). Brief Methods 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 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 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.