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Journal articles on the topic 'Cytochrome P450'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Bandiera, S. "Expression and catalysis of sex-specific cytochrome P450 isozymes in rat liver." Canadian Journal of Physiology and Pharmacology 68, no. 6 (1990): 762–68. http://dx.doi.org/10.1139/y90-117.

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Research interest in the study of cytochromes P450 has recently been shifting to the characterization of "constitutively" expressed isozymes from that of the inducible forms. Several "constitutive" cytochrome P450 isozymes have been purified from rat liver including five immunochemically related proteins designated cytochromes P450f, P450g, P450h, P450i, and P450k. These hemoproteins have been identified as distinct isozymes on the basis of spectral, electrophoretic, and catalytic properties and NH2-terminal sequence analysis. Purification and immunoquantitation studies have indicated that the

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2

Ershov, P. V., Yu V. Mezentsev, E. O. Yablokov, et al. "Study specificity of isatin interactions with P450 cytochromes." Biomeditsinskaya Khimiya 64, no. 1 (2018): 61–65. http://dx.doi.org/10.18097/pbmc20186401061.

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Cytochrome P450-dependent monooxygenase systems exist basically in all living organisms, where they perform various important functions. The coordinated functioning of these systems involves many proteins participating in different protein-protein interactions (PPI). Previously, we have found that the endogenous non-peptide bioregulator isatin (indoledione-2,3), synthesized from indole by means of certain cytochromes P450 (e.g. P450 2E1, P450 2C19, P450 2A6) regulates affinity of some PPI. In this work, an attempt has been undertaken to register a direct interaction of isatin with a set of dif

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3

Godbole, Rucha C., Anupama A. Pable, and Vitthal T. Barvkar. "Transcriptome-wide identification, characterization, and phylogenomic analysis of cytochrome P450s from Nothapodytes nimmoniana reveal candidate genes involved in the camptothecin biosynthetic pathway." Genome 64, no. 1 (2021): 1–14. http://dx.doi.org/10.1139/gen-2020-0067.

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The plant Nothapodytes nimmoniana is an important source of camptothecin (CPT), an anticancer compound widely used in the treatment of colorectal, lung, and ovarian cancers. CPT is biosynthesized by the combination of the seco-iridoid and indole pathways in plants. The majority of the biosynthetic steps and associated genes still remain unknown. Certain reactions in the seco-iridoid pathway are catalyzed by cytochrome P450 enzymes. Hence, identifying transcriptionally active cytochrome P450 genes becomes essential in the elucidation of the CPT biosynthetic pathway. Here, we report the identifi

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4

Iwasaki, M., R. L. P. Lindberg, R. O. Juvonen та M. Negishi. "Site-directed mutagenesis of mouse steroid 7α-hydroxylase (cytochrome P-4507α): role of residue-209 in determining steroid-cytochrome P-450 interaction". Biochemical Journal 291, № 2 (1993): 569–73. http://dx.doi.org/10.1042/bj2910569.

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We have cloned a cDNA encoding mouse steroid 7 alpha-hydroxylase P450(7) alpha (cytochrome P-450(7) alpha) and expressed it in Saccharomyces cerevisiae. Mouse P450(7) alpha is 70% identical in its amino acid sequence with the mouse steroid 15 alpha-hydroxylase P450(15) alpha (2A4). The Leu at position 209 of P450(15) alpha is the most important residue to determine the steroid hydroxylase activity of the P450 [Lindberg and Negishi (1989) Nature (London) 339, 632-634]. The P450(7) alpha contains Asn at the position corresponding to the Leu-209 of P450(15) alpha, although both P450s hydroxylate

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5

Hodek, Petr, Tomáš Koblas, Helena Rýdlová, et al. "Chicken Egg Yolk as an Excellent Source of Highly Specific Antibodies Against Cytochromes P450." Collection of Czechoslovak Chemical Communications 69, no. 3 (2004): 659–73. http://dx.doi.org/10.1135/cccc20040659.

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Using chicken antibodies IgY (purified from egg yolks) against mammalian cytochromes P450 and by means of cytochrome P450 marker substrates, we found for the first time the presence of hepatopancreatic cytochrome P450 in crayfishOrconectes limosus(an inducible cytochrome P450 2B-like enzyme) and we were able to detect and quantify cytochrome P450 1A1 in microsomes of human livers. Expression levels of cytochrome P450 1A1 in human livers constituted less than 0.6% of the total hepatic cytochrome P450 complement. The results obtained in our study are clear examples that chicken IgY are suitable

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6

Rwere, Freeborn, Sangchoul Im, and Lucy Waskell. "The FMN “140s Loop” of Cytochrome P450 Reductase Controls Electron Transfer to Cytochrome P450." International Journal of Molecular Sciences 22, no. 19 (2021): 10625. http://dx.doi.org/10.3390/ijms221910625.

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Cytochrome P450 reductase (CYPOR) provides electrons to all human microsomal cytochrome P450s (cyt P450s). The length and sequence of the “140s” FMN binding loop of CYPOR has been shown to be a key determinant of its redox potential and activity with cyt P450s. Shortening the “140s loop” by deleting glycine-141(ΔGly141) and by engineering a second mutant that mimics flavo-cytochrome P450 BM3 (ΔGly141/Glu142Asn) resulted in mutants that formed an unstable anionic semiquinone. In an attempt to understand the molecular basis of the inability of these mutants to support activity with cyt P450, we

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7

Munro, A. W., K. J. McLean, K. R. Marshall, et al. "Cytochromes P450: novel drug targets in the war against multidrug-resistant Mycobacterium tuberculosis." Biochemical Society Transactions 31, no. 3 (2003): 625–30. http://dx.doi.org/10.1042/bst0310625.

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Novel drug strategies are desperately needed to combat the global threat posed by multidrug-resistant strains of Mycobacterium tuberculosis (Mtb). The genome sequence of Mtb has revealed an unprecedented number of cytochrome P450 enzymes in a prokaryote, suggesting fundamental physiological roles for many of these enzymes. Several azole drugs (known inhibitors of cytochromes P450) have been shown to have potent anti-mycobacterial activity, and the most effective azoles have extremely tight binding constants for one of the Mtb P450s (CYP121). The structure of CYP121 has been determined at atomi

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8

Hrubý, Kamil, Eva Anzenbacherová, Pavel Anzenbacher, and Milan Nobilis. "Biotransformation of Benfluron by Rat Hepatic Cytochrome P450. Identification of Individual CYP-Enzymes Involved in Biotransformation of Benfluron, Prospective Antineoplastic Based on Benzo[c]fluorene." Collection of Czechoslovak Chemical Communications 65, no. 8 (2000): 1374–86. http://dx.doi.org/10.1135/cccc20001374.

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Benfluron, 5-[2-(dimethylamino)ethoxy]-7H-benzo[c]fluoren-7-one hydrochloride, a prospective antineoplastic agent, is metabolised by cytochromes P450 to N-demethyl and 9-hydroxy derivatives. To prove the participation of individual cytochrome P450 isoforms in formation of these metabolites, selective induction of cytochromes P450, inhibition of benfluron biotransformation using inhibitors specific for individual cytochromes P450, and inhibition by benfluron of "marker" enzyme activities characteristic of certain cytochromes P450 were used. N-Demethylbenfluron appears to be formed mainly by the

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9

Shumyantseva, Victoria V., Tatiana V. Bulko, Polina I. Koroleva, et al. "Human Cytochrome P450 2C9 and Its Polymorphic Modifications: Electroanalysis, Catalytic Properties, and Approaches to the Regulation of Enzymatic Activity." Processes 10, no. 2 (2022): 383. http://dx.doi.org/10.3390/pr10020383.

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The electrochemical properties of cytochrome P450 2C9 (CYP2C9) and polymorphic modifications P450 2C9*2 (CYP2C9*2) and P450 2C9*3 (CYP2C9*3) were studied. To analyze the comparative electrochemical and electrocatalytic activity, the enzymes were immobilized on electrodes modified with a membrane-like synthetic surfactant (didodecyldimethylammonium bromide (DDAB)). An adequate choice of the type of modified electrode was confirmed by cyclic voltammetry of cytochromes P450 under anaerobic conditions, demonstrating well-defined peaks of reduction and oxidation of the heme iron. The midpoint poten

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10

Pratiwi, R. A., N. S. W. Yahya, and Y. Chi. "Bio function of Cytochrome P450 on fungus: a review." IOP Conference Series: Earth and Environmental Science 959, no. 1 (2022): 012023. http://dx.doi.org/10.1088/1755-1315/959/1/012023.

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Abstract Cytochrome P450 is the superfamily of proteins involved in the metabolism of organisms, including fungi. Fungal have more diverse P450 families than plants, animals, or bacteria. Research on fungal P450 has blossomed and become an important area in biology and ecology. Cytochrome P450 could be detoxifying natural and environmental contaminants to survive in several ecological niches. Furthermore, the presence of the fungal Cytochrome P450 as an antifungal drug target is a promising approach for the controlling of pest and plant pathogenic fungi. To date, numerous studies have revealed

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11

RAMESH, CHANDRA, and ANEJA RITU. "Cytochrome P450 Enzymes : Significance, Multiplicity of Isoforms, Substrates, Catalytic and Regulatory Mechanisms, Physiological Functions and Clinical Correlation." Journal of Indian Chemical Society Vol. 75, Oct-Dec 1998 (1998): 795–803. https://doi.org/10.5281/zenodo.5923316.

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Dr. B. R. Ambedkar Center for Biomedical Research Department of Chemistry, University of Delhi, Delhi-110 007 <em>Manuscript received 14 September 1998</em> Historically there has been considerable interest in comparing patterns of biotransformation of xenobiotic chemicals in experimental animal models and humans, e.g. in areas such as drug metabolism and chemical carcinogenesis. With the availability of more basic knowledge it has become possible to attribute the oxidation of selected chemicals to individual cytochrome P450 enzymes in animals and humans. Further, these cytochrome P450 enzymes

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12

McFadyen, Morag C. E., William T. Melvin, and Graeme I. Murray. "Cytochrome P450 enzymes: Novel options for cancer therapeutics." Molecular Cancer Therapeutics 3, no. 3 (2004): 363–71. http://dx.doi.org/10.1158/1535-7163.363.3.3.

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Abstract The concept of overexpression of individual forms of cytochrome P450 enzymes in tumor cells is now becoming well recognized. Indeed, a growing body of research highlights the overexpression of P450s, particularly CYP1B1, in tumor cells as representing novel targets for anticancer therapy. The purpose of this review is to outline the novel therapeutic options and opportunities arising from both enhanced endogenous expression of cytochrome P450 in tumors and cytochrome P450-mediated gene therapy.

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13

McLean, K. J., M. Sabri, K. R. Marshall, et al. "Biodiversity of cytochrome P450 redox systems." Biochemical Society Transactions 33, no. 4 (2005): 796–801. http://dx.doi.org/10.1042/bst0330796.

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P450s (cytochrome P450 mono-oxygenases) are a superfamily of haem-containing mono-oxygenase enzymes that participate in a wide range of biochemical pathways in different organisms from all of the domains of life. To facilitate their activity, P450s require sequential delivery of two electrons passed from one or more redox partner enzymes. Although the P450 enzymes themselves show remarkable similarity in overall structure, it is increasingly apparent that there is enormous diversity in the redox partner systems that drive the P450 enzymes. This paper examines some of the recent advances in our

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14

Lamb, David C., Alec H. Follmer, Jared V. Goldstone, et al. "On the occurrence of cytochrome P450 in viruses." Proceedings of the National Academy of Sciences 116, no. 25 (2019): 12343–52. http://dx.doi.org/10.1073/pnas.1901080116.

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Genes encoding cytochrome P450 (CYP; P450) enzymes occur widely in the Archaea, Bacteria, and Eukarya, where they play important roles in metabolism of endogenous regulatory molecules and exogenous chemicals. We now report that genes for multiple and unique P450s occur commonly in giant viruses in the Mimiviridae, Pandoraviridae, and other families in the proposed order Megavirales. P450 genes were also identified in a herpesvirus (Ranid herpesvirus 3) and a phage (Mycobacterium phage Adler). The Adler phage P450 was classified as CYP102L1, and the crystal structure of the open form was solved

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15

Reed, James R., J. Patrick Connick, Dongmei Cheng, George F. Cawley, and Wayne L. Backes. "Effect of homomeric P450–P450 complexes on P450 function." Biochemical Journal 446, no. 3 (2012): 489–97. http://dx.doi.org/10.1042/bj20120636.

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Previous studies have shown that the presence of one P450 enzyme can affect the function of another. The goal of the present study was to determine if P450 enzymes are capable of forming homomeric complexes that affect P450 function. To address this problem, the catalytic activities of several P450s were examined in reconstituted systems containing NADPH–POR (cytochrome P450 reductase) and a single P450. CYP2B4 (cytochrome P450 2B4)-, CYP2E1 (cytochrome P450 2E1)- and CYP1A2 (cytochrome P450 1A2)-mediated activities were measured as a function of POR concentration using reconstituted systems c

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16

Wan, Linrong, Anlian Zhou, Wenfu Xiao, et al. "Cytochrome P450 monooxygenase genes in the wild silkworm, Bombyx mandarina." PeerJ 9 (February 3, 2021): e10818. http://dx.doi.org/10.7717/peerj.10818.

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Wild (Bombyx mandarina) and domestic silkworms (B. mori) are good models for investigating insect domestication, as 5000 years of artificial breeding and selection have resulted in significant differences between B. mandarina and B. mori. In this study, we improved the genome assemblies to the chromosome level and updated the protein-coding gene annotations for B. mandarina. Based on this updated genome, we identified 68 cytochrome P450 genes in B. mandarina. The cytochrome P450 repository in B. mandarina is smaller than in B. mori. Certain currently unknown key genes, rather than gene number,

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17

Kim, Donghak, and F. Peter Guengerich. "CYTOCHROME P450 ACTIVATION OF ARYLAMINES AND HETEROCYCLIC AMINES." Annual Review of Pharmacology and Toxicology 45, no. 1 (2005): 27–49. http://dx.doi.org/10.1146/annurev.pharmtox.45.120403.100010.

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Arylamines and heterocyclic arylamines (HAAs) are of particular interest because of demonstrated carcinogenicity in animals and humans and the broad exposure to many of these compounds. The activation of these, and also some arylamine drugs, involves N-hydroxylation, usually by cytochrome P450 (P450). P450 1A2 plays a prominent role in these reactions. However, P450 1A1 and 1B1 and other P450s are also important in humans as well as experimental animals. Some arylamines (including drugs) are N-hydroxylated predominantly by P450s other than those in Family 1. Other oxygenases can also have role

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18

Chun, Y. J., T. Shimada, M. R. Waterman, and F. P. Guengerich. "Understanding electron transport systems of Streptomyces cytochrome P450." Biochemical Society Transactions 34, no. 6 (2006): 1183–85. http://dx.doi.org/10.1042/bst0341183.

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Streptomyces spp. are known to produce various types of biologically active compounds including antibiotics, antiparasitic agents, herbicides and immunosuppressants. P450 (cytochrome P450) enzymes may have key roles in these biosynthetic and biotransformation reactions. Recent genomic analysis of Streptomyces coelicolor A3(2) indicates that S. coelicolor may have six ferredoxins (Fdxs), four putative Fdx reductases (FdRs) and 18 P450 genes. However, there are few clues to explain the mechanisms and functions of Streptomyces P450 systems. To solve these questions, we have expressed and purified

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19

Gnedenko, O. V., L. A. Kaluzhskiy, A. A. Molnar, et al. "SPR-biosensor assay for analysis of small compounds interaction with human cytochrome P450 51A1 (CYP51A1)." Biomeditsinskaya Khimiya 59, no. 4 (2013): 388–98. http://dx.doi.org/10.18097/pbmc20135904388.

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The SPR assay for human cytochrome P450 51A1's (CYP51A1) ligand screening was developed. Assay has been validated with known azole inhibitors of cytochrome P450s. The studied azoles selectively interacted with human cytochrome P450 51A1, which showed the highest affinity towards ketoconazole. The efficiency of the SPR assay was showed with 19 steroid and triterpene compounds, which were not investigated as potential ligands of CYP51A1.

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20

Beneš, Martin, Jiří Hudeček, Pavel Anzenbacher, and Martin Hof. "Coumarin 6, Hypericin, Resorufins, and Flavins: Suitable Chromophores for Fluorescence Correlation Spectroscopy of Biological Molecules." Collection of Czechoslovak Chemical Communications 66, no. 6 (2001): 855–69. http://dx.doi.org/10.1135/cccc20010855.

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In this work we show that the dyes coumarin 6, hypericin, 7-O-ethylresorufin and resorufin are suitable for fluorescence correlation spectroscopy (FCS) and demonstrate the use of these dyes in physiologically relevant protein studies. Since coumarins are metabolised by cytochromes P450, the binding of coumarin 6 to cytochrome P450 3A4 was investigated by FCS. Coumarin 6 appears to be a very bright non-covalent cytochrome P450 label. When titrating cytochrome P450 3A4 with coumarin 6, the diffusion time of the coumarin 6/ cytochrome P450 3A4 complex increases roughly two-fold at protein concent

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Popova, Olga, Daria Bylinskaya, Anastasia Nikitina та Olga Ukrainskaya. "The role of nicotinamide-β-adenine dinucleotide phosphate-H-cytochrome P450 oxidoreductase in the activation of cytochromes". BIO Web of Conferences 181 (2025): 01027. https://doi.org/10.1051/bioconf/202518101027.

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The aim of this theoretical study is to investigate the mechanisms of action of these enzymes in the context of metabolism in highly productive animals. The relevance is due to the active development of agriculture and increased interest in a detailed study of the cytochrome P450 system for obtaining high-quality livestock products. This work highlights the functional significance of the enzyme Nicotinamide-β- adenine dinucleotide phosphate-H-cytochrome P450 oxidoreductase in the processes of activation of cytochromes P450. An analysis of existing data on the interaction of Nicotinamide-β-aden

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22

Koroleva, P. I., and V. V. Shumyantseva. "Design of model systems based on cytochrome P450 3A4 and riboflavin complexes for increasing the electrocatalysis efficiency." Journal Biomed 17, no. 3E (2021): 37–41. http://dx.doi.org/10.33647/2713-0428-17-3e-37-41.

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Cytochromes P450 (CYP) are a large class of enzymes, whose active site is type b heme. The main function of cytochromes P450 is biotransformation of endogenous and exogenous compounds in the organism. The cytochrome P450 3A4 metabolizes about 50% of all modern medications; therefore, its catalytic properties present significant research interest. P450 cytochromes can be effectively investigated using electrochemical systems that consist of a solid base (electrode) and a modifier facilitating enzyme immobilization. In this case, the electron donor is an electrode substituting a natural electron

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23

Ronzhin, N., E. Posokhina, O. Mogilnaya, A. Puzyr, J. Gitelson, and V. Bondar. "CYTOCHROME P450 SYSTEM MAY BE INVOLVED IN THE LIGHT EMISSION OF HIGHER FUNGI." Russian Journal of Biological Physics and Chemisrty 7, no. 2 (2022): 320–24. http://dx.doi.org/10.29039/rusjbpc.2022.0522.

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The paper presents data that testify in favor of the participation of the cytochrome P450 system in the light emission of higher fungi. Extracts from mycelia of different species of luminous basidiomycetes containing fungal luminescent systems that provide luminescence in vitro were obtained. Applied conditions for the isolation of luminescent systems (sonication, centrifugation at 40000g) indicate the presence of membrane structures in the extracts, in particular, microsomes formed as a result of ultrasonic disintegration of the endoplasmic reticulum (ER). Differential spectral analysis of th

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24

Henderson, C. J., A. Sahraouei, and C. R. Wolf. "Cytochrome P450s and chemoprevention." Biochemical Society Transactions 28, no. 2 (2000): 42–46. http://dx.doi.org/10.1042/bst0280042.

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The cytochrome P450 mono-oxygenase system represents a major defence against chemical challenge from the environment, constituting part of an adaptive response mounted by an organism following exposure to harmful agents. Cytochrome P450s are also able to catalyse the activation of compounds to toxic products, and participate in a variety of essential ‘housekeeping’ functions, such as biosynthesis of steroid hormones and fatty acid oxidation. It is clear that the modulation of expression of these enzymes can have a significant effect on chemical toxicity, carcinogenicity and mutagenicity. The c

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25

Ye, Min, Bidhan Nayak, Lei Xiong, et al. "The Role of Insect Cytochrome P450s in Mediating Insecticide Resistance." Agriculture 12, no. 1 (2022): 53. http://dx.doi.org/10.3390/agriculture12010053.

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In many organisms, cytochrome P450 enzymes are the primary detoxifying enzymes. Enhanced P450 activity can be mediated by the emergence of new genes, increased transcription due to mutations in the promoter regions, changes in enzyme structures and functions due to mutations in protein-coding regions, or changes in post-translational modifications; all of these changes are subject to insecticide selection pressure. Multiple signalling pathways and key effector molecules are involved in the regulation of insect P450s. Increased P450 activity is a key mechanism inducing insect resistance. Hence,

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Barbosa-Sicard, Eduardo, Eva Kaergel, Dominik N. Muller, Horst Honeck, Friedrich C. Luft, and Wolf-Hagen Schunck. "Cytochrome P450 Isoform Expression in Human Vascular Endothelial Cells." Hypertension 36, suppl_1 (2000): 698. http://dx.doi.org/10.1161/hyp.36.suppl_1.698-a.

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P29 Epoxy derivatives of arachidonic acid may act as important autocrine and paracrine mediators of endothelial function including regulation of vascular tone and control of inflammation. To identify potential candidates for catalyzing the synthesis of these and further arachidonic acid metabolites, we studied human vascular endothelial cells for the expression of individual cytochrome P450 isoforms belonging to the CYP families 1, 2, 3 and 4. An RT-PCR screening performed with subfamily- and isoform-specific primer pairs revealed mRNAs for the P450 forms 1A1, 1B1, 2C8, 2E1, 2J2, 3A7, 4A11 and

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Marchenko, M. M., G. P. Kopylchuk, and O. V. Ketsa. "Low doses x-ray irradiation influence on liver detoxication system in rats with transplanted guerin's carcinoma." Biomeditsinskaya Khimiya 56, no. 2 (2010): 266–73. http://dx.doi.org/10.18097/pbmc20105602266.

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The activity of detoxication enzymes in liver microsomal fraction of preliminary radiation-exposed rats was investigated. It was shown that preliminary organism exposure to radiation reduced cytochrome Р450 and glutathione-S-transferase activity in liver microsomal fraction in the latent and logarithmic phases of oncogenesis compared with the unirradiated rats with tumor.Low level of cytochrome Р450 activity can be caused by transition of microsomal cytochrome P450 in P420 inactive form.The preliminary radiation does not influence the enzyme activity of liver cytochrome P450 and glutathione-S-

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Lewis, David F. V. "Structural Models for Cytochrome P450�Mediated Catalysis." Scientific World JOURNAL 3 (2003): 536–45. http://dx.doi.org/10.1100/tsw.2003.41.

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This review focuses on the structural models for cytochrome P450 that are improving our knowledge and understanding of the P450 catalytic cycle, and the way in which substrates bind to the enzyme leading to catalytic conversion and subsequent formation of mono-oxygenated metabolites. Various stages in the P450 reaction cycle have now been investigated using X-ray crystallography and electronic structure calculations, whereas homology modelling of mammalian P450s is currently revealing important aspects of pharmaceutical and other xenobiotic metabolism mediated by P450 involvement. These featur

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Hu, Z., Q. Lin, H. Chen, Z. Li, F. Yin, and X. Feng. "Identification of a novel cytochrome P450 gene,CYP321E1from the diamondback moth,Plutella xylostella(L.) and RNA interference to evaluate its role in chlorantraniliprole resistance." Bulletin of Entomological Research 104, no. 6 (2014): 716–23. http://dx.doi.org/10.1017/s0007485314000510.

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AbstractInsect cytochrome P450 monooxygenases (P450s) play an important role in catalysis of many reactions leading to insecticides resistance. Our previous studies on transcriptome analysis of chlorantraniliprole-resistant development in the diamondback moth,Plutella xylostellarevealed that up-regulation of cytochrome P450s are one of the main factors leading to the development of chlorantraniliprole resistance. Here, we report for the first time a novel cytochrome P450 geneCYP321E1, which belongs to the cytochrome P450 gene family CYP321. Real-time quantitative PCR (RT–qPCR) analyses indicat

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30

McLean, K. J., A. J. Dunford, M. Sabri, et al. "CYP121, CYP51 and associated redox systems in Mycobacterium tuberculosis: towards deconvoluting enzymology of P450 systems in a human pathogen." Biochemical Society Transactions 34, no. 6 (2006): 1178–82. http://dx.doi.org/10.1042/bst0341178.

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An extraordinary array of P450 (cytochrome P450) enzymes are encoded on the genome of the human pathogen Mycobacterium tuberculosis (Mtb) and in related mycobacteria and actinobacteria. These include the first characterized sterol 14α-demethylase P450 (CYP51), a known target for azole and triazole drugs in yeasts and fungi. To date, only two Mtb P450s have been characterized in detail: CYP51 and CYP121. The CYP121 P450 shows structural relationships with P450 enzymes involved in synthesis of polyketide antibiotics. Both P450s exhibit tight binding to a range of azole drugs (e.g. clotrimazole a

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Paul Bolwell, G. "Cytochrome P450:." Phytochemistry 35, no. 1 (1993): 279. http://dx.doi.org/10.1016/s0031-9422(00)90557-0.

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32

Ehrenpreis, Eli D., and Seymour Ehrenpreis. "CYTOCHROME P450." Clinics in Liver Disease 2, no. 3 (1998): 457–70. http://dx.doi.org/10.1016/s1089-3261(05)70021-0.

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Roos, P. H., and N. Jakubowski. "Cytochrome P450." Analytical and Bioanalytical Chemistry 392, no. 6 (2008): 1015–17. http://dx.doi.org/10.1007/s00216-008-2415-z.

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34

D'Arcy, P. F. "Cytochrome P450." International Journal of Pharmaceutics 103, no. 1 (1994): 99. http://dx.doi.org/10.1016/0378-5173(94)90211-9.

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35

Poulos, Thomas L. "Cytochrome P450." Current Opinion in Structural Biology 5, no. 6 (1995): 767–74. http://dx.doi.org/10.1016/0959-440x(95)80009-3.

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36

Coulson, C. J. "Cytochrome P450." Trends in Biochemical Sciences 10, no. 2 (1985): 92. http://dx.doi.org/10.1016/0968-0004(85)90255-5.

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Shumyantseva, V. V., T. V. Bulko, O. V. Gnedenko, E. O. Yablokov, S. A. Usanov, and A. S. Ivanov. "Adrenodoxins and their role in the cytochrome P450 systems." Biomeditsinskaya Khimiya 68, no. 1 (2022): 47–54. http://dx.doi.org/10.18097/pbmc20226801047.

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The role of partner proteins in the formation of functional complexes in cytochrome P450 systems was investigated by means of optical biosensor technique. Kinetic constants and equilibrium dissociation constants of complexes of cytochrome CYP11A1 (P450scc) with wild-type adrenodoxin (Adx WT) and mutant forms of adrenodoxin R106D and D109R were determined using an optical biosensor. Wild-type adrenodoxin (Kd = (1.23±0.09)⋅10⁻⁶ M) and mutant D109R (Kd = (2.37±0.09)⋅10⁻⁸ M) formed complexes with cytochrome P450scc. For the R106D mutant, no complex formation was detected. To investigate the possib

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Kuzikov, A. V., T. V. Bulko, P. I. Koroleva, et al. "Electroanalytical and electrocatalytical characteristics of cytochrome P450 3A4 using electrodes modified with nanocomposite carbon nanomaterials." Biomeditsinskaya Khimiya 66, no. 1 (2020): 64–70. http://dx.doi.org/10.18097/pbmc20206601064.

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The electroanalytical characteristics of recombinant cytochrome P450 3A4 (P450 3A4) immobilized on the surface of screen-printed graphite electrodes modified with multi-walled carbon nanotubes have been studied. The role and the influence of graphite working electrode modification with carbon nanotubes on electroanalytical characteristics of cytochrome P450 3A4 have been demonstrated. The conditions for the immobilization of cytochrome P450 3A4 on the obtained screen-printed graphite electrodes modified with carbon multi-walled nanotubes have been optimized. The electrochemical parameters of t

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Li, Zhong, Yuanyuan Jiang, F. Peter Guengerich, Li Ma, Shengying Li, and Wei Zhang. "Engineering cytochrome P450 enzyme systems for biomedical and biotechnological applications." Journal of Biological Chemistry 295, no. 3 (2019): 833–49. http://dx.doi.org/10.1074/jbc.rev119.008758.

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Cytochrome P450 enzymes (P450s) are broadly distributed among living organisms and play crucial roles in natural product biosynthesis, degradation of xenobiotics, steroid biosynthesis, and drug metabolism. P450s are considered as the most versatile biocatalysts in nature because of the vast variety of substrate structures and the types of reactions they catalyze. In particular, P450s can catalyze regio- and stereoselective oxidations of nonactivated C–H bonds in complex organic molecules under mild conditions, making P450s useful biocatalysts in the production of commodity pharmaceuticals, fin

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Nelson, David R. "A world of cytochrome P450s." Philosophical Transactions of the Royal Society B: Biological Sciences 368, no. 1612 (2013): 20120430. http://dx.doi.org/10.1098/rstb.2012.0430.

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The world we live in is a biosphere influenced by all organisms who inhabit it. It is also an ecology of genes, with some having rather startling effects. The premise put forth in this issue is cytochrome P450 is a significant player in the world around us. Life and the Earth itself would be visibly different and diminished without cytochrome P450s. The contributions to this issue range from evolution on the billion year scale to the colour of roses, from Darwin to Rachel Carson; all as seen through the lens of cytochrome P450.

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Correia, Maria Almira, Sheila Sadeghi, and Eduardo Mundo-Paredes. "CYTOCHROME P450 UBIQUITINATION: Branding for the Proteolytic Slaughter?" Annual Review of Pharmacology and Toxicology 45, no. 1 (2005): 439–64. http://dx.doi.org/10.1146/annurev.pharmtox.45.120403.100127.

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The hepatic cytochromes P450 (P450s) are monotopic endoplasmic reticulum (ER)-anchored hemoproteins engaged in the enzymatic oxidation of a wide variety of endo- and xenobiotics. In the course of these reactions, the enzymes generate reactive O2 species and/or reactive metabolic products that can attack the P450 heme and/or protein moiety and structurally and functionally damage the enzyme. The in vivo conformational unraveling of such a structurally damaged P450 signals its rapid removal via the cellular sanitation system responsible for the proteolytic disposal of structurally aberrant, abno

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Unterweger, Birgit, Dieter M. Bulach, Judith Scoble, et al. "CYP101J2, CYP101J3, and CYP101J4, 1,8-Cineole-Hydroxylating Cytochrome P450 Monooxygenases from Sphingobium yanoikuyae Strain B2." Applied and Environmental Microbiology 82, no. 22 (2016): 6507–17. http://dx.doi.org/10.1128/aem.02067-16.

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ABSTRACTWe report the isolation and characterization of three new cytochrome P450 monooxygenases: CYP101J2, CYP101J3, and CYP101J4. These P450s were derived fromSphingobium yanoikuyaeB2, a strain that was isolated from activated sludge based on its ability to fully mineralize 1,8-cineole. Genome sequencing of this strain in combination with purification of native 1,8-cineole-binding proteins enabled identification of 1,8-cineole-binding P450s. The P450 enzymes were cloned, heterologously expressed (N-terminally His6tagged) inEscherichia coliBL21(DE3), purified, and spectroscopically characteri

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Mthethwa, Bongumusa, Wanping Chen, Mathula Ngwenya, et al. "Comparative Analyses of Cytochrome P450s and Those Associated with Secondary Metabolism in Bacillus Species." International Journal of Molecular Sciences 19, no. 11 (2018): 3623. http://dx.doi.org/10.3390/ijms19113623.

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Cytochrome P450 monooxygenases (CYPs/P450s) are among the most catalytically-diverse enzymes, capable of performing enzymatic reactions with chemo-, regio-, and stereo-selectivity. Our understanding of P450s’ role in secondary metabolite biosynthesis is becoming broader. Among bacteria, Bacillus species are known to produce secondary metabolites, and recent studies have revealed the presence of secondary metabolite biosynthetic gene clusters (BGCs) in these species. However, a comprehensive comparative analysis of P450s and P450s involved in the synthesis of secondary metabolites in Bacillus s

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Zheng, Xiaoyan, Ping Li, and Xu Lu. "Research advances in cytochrome P450-catalysed pharmaceutical terpenoid biosynthesis in plants." Journal of Experimental Botany 70, no. 18 (2019): 4619–30. http://dx.doi.org/10.1093/jxb/erz203.

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Advances in the role of cytochrome P450s in pharmaceutical terpenoid biosynthesis are reviewed, and different cloning strategies to identify new cytochrome P450 genes in the biosynthesis of natural terpenoids are summarized.

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Moskaleva, N. E., and V. G. Zgoda. "Current methods of cytochrome P450 analysis." Biomeditsinskaya Khimiya 58, no. 6 (2012): 617–34. http://dx.doi.org/10.18097/pbmc20125806617.

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Current review describes recent approaches of cytochrome P450 concentration and activity evaluation. Special attention paid to modern methods of proteomic analysis such as electrophoresis and chromato-mass-spectrometry. Methods of targeted proteomic applicable for quantitative and qualitative study of P450s in biological samples as well as methods for the enzyme activity measurements are reviewed. Finally, data on correlation between certain P450 isoform content and its specific enzymatic activities were described and discussed in the review.

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Guengerich, F. Peter, Clayton J. Wilkey, and Thanh T. N. Phan. "Human cytochrome P450 enzymes bind drugs and other substrates mainly through conformational-selection modes." Journal of Biological Chemistry 294, no. 28 (2019): 10928–41. http://dx.doi.org/10.1074/jbc.ra119.009305.

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Cytochrome P450 (P450) enzymes are major catalysts involved in the oxidations of most drugs, steroids, carcinogens, fat-soluble vitamins, and natural products. The binding of substrates to some of the 57 human P450s and other mammalian P450s is more complex than a two-state system and has been proposed to involve mechanisms such as multiple ligand occupancy, induced-fit, and conformational-selection. Here, we used kinetic analysis of binding with multiple concentrations of substrates and computational modeling of these data to discern possible binding modes of several human P450s. We observed

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Guengerich, F. Peter. "Cytochrome P450 research and The Journal of Biological Chemistry." Journal of Biological Chemistry 294, no. 5 (2019): 1671–80. http://dx.doi.org/10.1074/jbc.tm118.004144.

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In honor of the 100th birthday of Dr. Herbert Tabor, JBC's Editor-in-Chief for 40 years, I will review here JBC's extensive coverage of the field of cytochrome P450 (P450) research. Research on the reactions catalyzed by these enzymes was published in JBC before it was even realized that they were P450s, i.e. they have a “pigment” with an absorption maximum at 450 nm. After the P450 pigment discovery, reported in JBC in 1962, the journal proceeded to publish the methods for measuring P450 activities and many seminal findings. Since then, the P450 field has grown extensively, with significant p

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Moran, F. M., J. J. Ford, C. J. Corbin, et al. "Regulation of Microsomal P450, Redox Partner Proteins, and Steroidogenesis in the Developing Testes of the Neonatal Pig." Endocrinology 143, no. 9 (2002): 3361–69. http://dx.doi.org/10.1210/en.2002-220329.

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Abstract Testicular growth and plasma androgen concentrations increase markedly in the first weeks of neonatal life of pigs. The regulation of steroidogenesis through this period was examined by measuring total microsomal cytochromes P450 (P450), 17α-hydroxylase/17,20-lyase P450 (P450c17) and aromatase P450 (P450arom) enzyme activities, and the redox partner proteins nicotinamide adenine dinucleotide phosphate, reduced form (NADPH)-cytochrome P450 reductase (reductase) and cytochrome b5 in testicular microsomes. Testes were collected from 1–24 d of age, and testicular development was suppresse

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Nzuza, Nomfundo, Tiara Padayachee, Puleng Rosinah Syed, et al. "Ancient Bacterial Class Alphaproteobacteria Cytochrome P450 Monooxygenases Can Be Found in Other Bacterial Species." International Journal of Molecular Sciences 22, no. 11 (2021): 5542. http://dx.doi.org/10.3390/ijms22115542.

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Cytochrome P450 monooxygenases (CYPs/P450s), heme-thiolate proteins, are well-known players in the generation of chemicals valuable to humans and as a drug target against pathogens. Understanding the evolution of P450s in a bacterial population is gaining momentum. In this study, we report comprehensive analysis of P450s in the ancient group of the bacterial class Alphaproteobacteria. Genome data mining and annotation of P450s in 599 alphaproteobacterial species belonging to 164 genera revealed the presence of P450s in only 241 species belonging to 82 genera that are grouped into 143 P450 fami

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Yamazaki, Hiroshi, Elizabeth M. J. Gillam, Mi-Sook Dong, William W. Johnson, F. Peter Guengerich, and Tsutomu Shimada. "Reconstitution of Recombinant Cytochrome P450 2C10(2C9) and Comparison with Cytochrome P450 3A4 and Other Forms: Effects of Cytochrome P450–P450 and Cytochrome P450–b5Interactions." Archives of Biochemistry and Biophysics 342, no. 2 (1997): 329–37. http://dx.doi.org/10.1006/abbi.1997.0125.

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