Expression of human cytochrome P450 enzymes in yeast and bacteria and relevance to studies on catalytic specificity

Guengerich, FP, Gillam, Emj, Ohmori, S, Sandhu, P, Brian, WR, Sari, MA and Iwasaki, M (1993) Expression of human cytochrome P450 enzymes in yeast and bacteria and relevance to studies on catalytic specificity. Toxicology, 82 1-3: 21-37. doi:10.1016/0300-483X(93)90057-Y


Author Guengerich, FP
Gillam, Emj
Ohmori, S
Sandhu, P
Brian, WR
Sari, MA
Iwasaki, M
Title Expression of human cytochrome P450 enzymes in yeast and bacteria and relevance to studies on catalytic specificity
Journal name Toxicology   Check publisher's open access policy
ISSN 0300-483X
Publication date 1993-10-05
Sub-type Article (original research)
DOI 10.1016/0300-483X(93)90057-Y
Volume 82
Issue 1-3
Start page 21
End page 37
Total pages 17
Language eng
Subject 3005 Toxicology
Abstract Heterologous expression systems can be utilized to great advantage in the study of cytochrome P450 (P450) and other enzymes involved in the biotransformation of drugs and other xenobiotics. The list of studies made possible with the technology includes discernment of catalytic specificity, elucidation of structure-activity relationships, and various biophysical measurements. There are advantages and disadvantages to each of the vector systems and choices must be made on the basis of needs. Yeast expression systems were used to establish that different P450 2C enzymes are involved in the hydroxylations of tolbutamide and (S)-mephenytion. P450 3A4 was also expressed in yeast and its very broad catalytic specificity was confirmed. Recently, it has been possible to express P450 3A4 as well as other human and animal P450s in bacteria after slight modification of their 5′-coding sequences.
Keyword Aflatoxin B1
Cytochrome P450
Cytochrome P450 3A4
Escherichia coli
Saccharomyces cerevesiae
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
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