Mammalian Microsomal Cytochrome P450 Monooxygenase

Williams, Pamela A.; Cosme, Jose; Sridhar, Vandana; Johnson, Eric F.; McRee, Duncan E.

doi:10.1016/s1097-2765(00)80408-6

Cited by 707Pharmacogenetics and Drug MetabolismMetal-Catalyzed Oxygenation MechanismsEnzyme Structure and Function

Mammalian Microsomal Cytochrome P450 Monooxygenase

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Williams, Pamela A., Cosme, Jose, Sridhar, Vandana, Johnson, Eric F., McRee, Duncan E.·2000·Molecular Cell

DOI 10.1016/s1097-2765(00)80408-6

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Abstract

Microsomal cytochrome P450s participate in xenobiotic detoxification, procarcinogen activation, and steroid hormone synthesis. The first structure of a mammalian microsomal P450 suggests that the association of P450s with the endoplasmic reticulum involves a hydrophobic surface of the protein formed by noncontiguous portions of the polypeptide chain. This interaction places the entrance of the putative substrate access channel in or near the membrane and orients the face of the protein proximal to the heme cofactor perpendicular to the plane of the membrane for interaction with the P450 reductase. This structure offers a template for modeling other mammalian P450s and should aid drug discovery and the prediction of drug-drug interactions.

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Low-circulating levels of plasma XO in baseline conditions can increase in disease conditions by release from damaged cells in liver or other tissues.
“There are low-circulating levels of plasma XO in baseline conditions that can increase in disease conditions by the release from damaged cells in liver or other tissues (1010).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [1010]

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Authors: Williams, P. A., Cosme, J., Sridhar, V., Johnson, E. F., & McRee, D. E.
Affiliations: Scripps Research Institute (US)
Corresponding author: McRee, Duncan E.
ORCID: Williams, Pamela A.
Johnson, Eric F.
McRee, Duncan E.
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2000-01
Volume: 5
Issue: 1
Pages: 121-131
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/s1097-2765(00)80408-6
OpenAlex: W2051639214
Cited by: 696
References: 52
Citations by year: 2026: 4 · 2025: 5 · 2024: 10 · 2023: 5 · 2022: 8 · 2021: 7 · 2020: 19 · 2019: 15 · 2018: 18 · 2017: 18 · 2016: 21 · 2015: 13 · 2014: 18 · 2013: 20 · 2012: 11
FWCI: 53.02
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 4946 d)
Locations: Molecular Cell (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5p01gm048495-08)
National Institute of General Medical Sciences (R01GM031001, GM-31001, GM-48495)
Topics: Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords: cytochrome P450, endoplasmic reticulum, protein structure, NADPH-cytochrome P450 reductase, xenobiotic detoxification, procarcinogen activation, steroidogenesis, drug-drug interactions, drug discovery
MeSH terms: Cytochrome P450 Family 2, Amino Acid Sequence, Animals, Binding Sites, Cytochrome P-450 Enzyme System, Endoplasmic Reticulum, Heme, Mammals, Microsomes, Models, Molecular, Molecular Sequence Data, Steroid 21-Hydroxylase, Protein Structure, Secondary, Crystallography, X-Ray

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Mammalian Microsomal Cytochrome P450 Monooxygenase

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