A highly selective probe for human cytochrome P450 3A4: isoform selectivity, kinetic characterization and its applications

Bufalin 5β-hydroxylation was found to be an isoform-specific biotransformation probe substrate for cytochrome P450 3A4 (CYP3A4). The probe reaction was well-characterized and it can be used for measuring the real catalytic activities of CYP3A4 from different enzyme sources.

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2013-01, Vol.49 (84), p.9779-9781
Main Authors: Ge, Guang-Bo, Ning, Jing, Hu, Liang-Hai, Dai, Zi-Ru, Hou, Jie, Cao, Yun-Feng, Yu, Zhen-Wen, Ai, Chun-Zhi, Gu, Jing-Kai, Ma, Xiao-Chi, Yang, Ling
Format: Article
Language:English
Subjects:
Biocatalysis
Bufanolides - chemistry
Bufanolides - metabolism
Cytochrome P-450 CYP3A - chemistry
Cytochrome P-450 CYP3A - metabolism
Humans
Hydroxylation
Isoenzymes - chemistry
Isoenzymes - metabolism
Kinetics
Models, Molecular
Molecular Conformation
Molecular Probes - chemistry
Molecular Probes - metabolism
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Description
Summary:Bufalin 5β-hydroxylation was found to be an isoform-specific biotransformation probe substrate for cytochrome P450 3A4 (CYP3A4). The probe reaction was well-characterized and it can be used for measuring the real catalytic activities of CYP3A4 from different enzyme sources.
ISSN:1359-7345
1364-548X
DOI:10.1039/c3cc45250f