A passion for P450s (rememberances of the early history of research on cytochrome P450).

  title={A passion for P450s (rememberances of the early history of research on cytochrome P450).},
  author={Ronald W. Estabrook},
  journal={Drug metabolism and disposition: the biological fate of chemicals},
  volume={31 12},
  • R. Estabrook
  • Published 1 December 2003
  • Biology
  • Drug metabolism and disposition: the biological fate of chemicals
Many members of the superfamily of hemeproteins, known as cytochrome P450 (P450 or CYP), are currently described in the literature (over 2000 at the date of this writing) [see Nelson, 2003 (http://drnelson.utmem.edu/CytochromeP450.html)]. In mammalian tissues, the P450s play central roles in drug and xenobiotic metabolism as well as steroid hormone synthesis, fat-soluble vitamin metabolism, and the conversion of polyunsaturated fatty acids to biologically active molecules. P450s also play a… 

Figures from this paper

The Central Role of Cytochrome P450 in Xenobiotic Metabolism—A Brief Review on a Fascinating Enzyme Family

Human Cytochrome P450 (CYP) enzymes constitute a superfamily of membrane-bound hemoproteins that are responsible for the metabolism of a wide variety of clinically, physiologically, and

Fifty Years of Cytochrome P450 Research: Examples of What We Know and Do Not Know

Some of the early experimental groundwork including P450 multiplicity and activity, electron transfer, and cellular localization that led to the early understanding of the molecular properties of P450 enzymes are described.

Steroid hydroxylations: a paradigm for cytochrome P450 catalyzed mammalian monooxygenation reactions.

  • R. Estabrook
  • Biology, Chemistry
    Biochemical and biophysical research communications
  • 2005

Novel extrahepatic P450 enzymes with emphasis on the tumor specific CYP2W1

It is concluded that CYP2W1 most probably is a colonic enzyme expressed in fetal life and overexpressed in about 50% of human colon tumors, which suggest the use of the enzyme as drug target in cancer therapy, but more studies are needed in order to fully understand its role in tumor biology and its potential as drug targets.

Cytochrome P450: genotype to phenotype

  • R. Waring
  • Biology
    Xenobiotica; the fate of foreign compounds in biological systems
  • 2019
The cytochromes P450 comprise a family of enzymes that are responsible for around three-quarters of all drug metabolism reactions that occur in human populations andObfuscating factors discussed include gene splicing, single nucleotide polymorphisms, epigenetics and microRNA, transcription regulation and multiple gene copies.

The monooxygenase, peroxidase, and peroxygenase properties of cytochrome P450.

Modified bile acids and androstanes—Novel promising inhibitors of human cytochrome P450 17A1

Process development for oxidations of hydrophobic compounds applying cytochrome P450 monooxygenases in-vitro.

Characterization of the cytochrome P450 monooxygenase genes (P450ome) from the carotenogenic yeast Xanthophyllomyces dendrorhous

The carotenogenic yeast X. dendrorhous has thirteen P450-encoding genes having potential functions in primary, secondary and xenobiotic metabolism reactions, including some genes of great interest for fatty acid hydroxylation and aromatic compound degradation.



The metabolism of methylated aminoazo dyes. VI. Intracellular distribution and properties of the demethylase system.

Only very low levels of demethylase activity were found in the microsomes of the nonhepatic normal tissues studied and in the liver tumors induced by 3′-methyl-4-dimethylaminoazobenzene.

Hydroxylation of steroids at carbon 21.

Laboratory of Chemical Pharmacology, National Heart, Lung, and Blood Institute, NIH: a short history.

  • J. Gillette
  • Biology, Medicine
    Annual review of pharmacology and toxicology
  • 2000
The Laboratory of Chemical Pharmacology began in 1950 as the Section of Pharmacology within the National Heart Institute, the National Institutes of Health and was among the first to study the effects of drugs on the turnover of serotonin and norepinephrine in brain and other tissues.

Photochemical action spectra of carbon monoxide-inhibited respiration.


  • L. Smith
  • Biology
    Bacteriological reviews
  • 1954
The a-bands of the reduced pigments in the the developments leading up to the present convisible region of the spectrum can be seen at cepts of the mammalian cytochrome system, and 605, 564 and 551 mA, corresponding to a mixture Wyman's review of the hemoproteins gives of cytochromes a + as, b and c, respectively.

Studies on respiratory enzymes of the adrenal gland. II. The cortex.

The present study has attempted to define both the cytochromes present in the beef adrenal cortex, as well as their distribution among the cell fractions, and indicates the likelihood that cy tochrome cl is the unknown cytochrome mentioned by Huszák.

Pigments of rat liver microsomes.

Studies on the respiratory enzymes of the adrenal gland. I. The medulla.

The enzymatic demethylation of ephedrine.

  • J. Axelrod
  • Biology, Chemistry
    The Journal of pharmacology and experimental therapeutics
  • 1955
An enzyme system in rabbit liver microsomes which catalyzes the demethylation of ephedrine to yield norephedrine and formaldehyde is described. The enzyme system requires reduced triphosphopyridine