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1دورية أكاديمية
المؤلفون: Won Choi, Seo Young Park, Hyun Min Kim, Thanh Dat Mai, Ju Hui Do, Hye Min Jang, Hyeon Bae Hwang, Eun Gyeong Song, Jae Sung Shim, Young Hee Joung
المصدر: Applied Biological Chemistry, Vol 66, Iss 1, Pp 1-10 (2023)
مصطلحات موضوعية: NADPH-cytochrome P450 reductase, Heterologous expression, Enzymatic characterization, Agriculture (General), S1-972, Chemistry, QD1-999
وصف الملف: electronic resource
العلاقة: https://doaj.org/toc/2468-0842Test
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2دورية أكاديمية
المصدر: Biomedicines, Vol 12, Iss 5, p 1052 (2024)
مصطلحات موضوعية: cytochrome b5 reductase, cytochrome P450 reductase, ovarian cancer, peritoneal fluid, antioxidant capacity, Biology (General), QH301-705.5
وصف الملف: electronic resource
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3دورية أكاديمية
المؤلفون: Yuyang Pan, Zhibo Yan, Songlyu Xue, Chufan Xiao, Guangjian Li, Wenyong Lou, Mingtao Huang
مصطلحات موضوعية: Biophysics, Biochemistry, Medicine, Genetics, Molecular Biology, Pharmacology, Biotechnology, Plant Biology, Space Science, Biological Sciences not elsewhere classified, Chemical Sciences not elsewhere classified, Information Systems not elsewhere classified, varied physiological benefits, remarkable conversion rate, highest reported values, f3h ), flavonoid, cytochrome p450 reductase, culture medium composition, 29 ± 20, 26 %, one, dhq ), known, saccharomyces cerevisiae dihydroquercetin, 3 ′- hydroxylase, l dhq, dhq yield, dhq synthesis, dhq production
الإتاحة: https://doi.org/10.1021/acs.jafc.3c09376.s001Test
https://figshare.com/articles/journal_contribution/Optimizing_the_Biosynthesis_of_Dihydroquercetin_from_Naringenin_in_Saccharomyces_cerevisiae/25267315Test -
4دورية أكاديمية
المؤلفون: Qihang Chen, Zikai Chao, Ke Wang, Xinglong Wang, Hao Meng, Xirong Liu, Xiaoyu Shan, Jingwen Zhou
مصطلحات موضوعية: Biophysics, Biochemistry, Microbiology, Biotechnology, Ecology, Biological Sciences not elsewhere classified, Chemical Sciences not elsewhere classified, Information Systems not elsewhere classified, steroidal pharmaceutical production, step process involving, multienzyme cascade process, molecular dynamics simulations, molar conversion rate, cortexolone (< b, developed p450 variants, l ), respectively, cytochrome p450 reductase, hydrocortisone (< b, p450bm3 variants revealed, least two enzymes, engineering p450bm3 synthesis, corticosteroids biosynthetic pathway, p450bm3 variants, hydrocortisone synthesis, sufficient p450bm3, six enzymes, simplified two, cytochrome p450s, biosynthetic steps
الإتاحة: https://doi.org/10.1021/acscatal.3c06137.s001Test
https://figshare.com/articles/journal_contribution/Simplification_of_Corticosteroids_Biosynthetic_Pathway_by_Engineering_P450BM3/25334784Test -
5دورية أكاديمية
المؤلفون: Yunhee Hwang, Hyun Gyu Hwang, Ji Yeon Lee, Gyoo Yeol Jung
مصطلحات موضوعية: Biophysics, Biochemistry, Microbiology, Genetics, Pharmacology, Biotechnology, Plant Biology, Computational Biology, Space Science, Environmental Sciences not elsewhere classified, Chemical Sciences not elsewhere classified, redesigning strains due, precisely rewires flux, isoflavonoid primarily found, intricate regulatory nodes, food industry due, enzyme homologue libraries, cytochrome p450 reductase, highest reported production, genistein biosynthetic pathway, based genetic regulators, genetic regulators, genistein production, unoptimized strain, transcriptional repressor, systematic engineering, study devised, significant nutritional, remarkable conversion, primary precursor
الإتاحة: https://doi.org/10.1021/acs.jafc.3c09687.s001Test
https://figshare.com/articles/journal_contribution/Systematic_Engineering_of_Genistein_Biosynthetic_Pathway_through_Genetic_Regulators_and_Combinatorial_Enzyme_Screening/25343314Test -
6دورية أكاديمية
المصدر: Advances in Autism, 2021, Vol. 8, Issue 4, pp. 332-342.
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7دورية أكاديمية
المؤلفون: Jingping Cheng, Guodong Li, Xue Wang, Congwei Yang, Furong Xu, Zigang Qian, Xiaohui Ma
المصدر: Molecules, Vol 28, Iss 21, p 7409 (2023)
مصطلحات موضوعية: Aconitum vilmorinianum, NADPH-cytochrome P450 reductase, diterpene alkaloids, class II CPR, transfer electrons, Organic chemistry, QD241-441
وصف الملف: electronic resource
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8دورية أكاديمية
المؤلفون: Mingxuan Wang, Jing Li, Wenjie Cong, Jianguo Zhang
المصدر: Current Issues in Molecular Biology, Vol 44, Iss 5, Pp 1828-1837 (2022)
مصطلحات موضوعية: ω3 desaturase, ω6 desaturase, NADPH–cytochrome P450 reductase, enzyme kinetics, Mortierella alpina, Biology (General), QH301-705.5
وصف الملف: electronic resource
العلاقة: https://www.mdpi.com/1467-3045/44/5/125Test; https://doaj.org/toc/1467-3037Test; https://doaj.org/toc/1467-3045Test
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9دورية أكاديمية
المؤلفون: Bahramian Nasab, S., Homaei, A., Fernández-Lafuente, Roberto, Del Arco, J., Fernández-Lucas, J.
المساهمون: University of Hormozgan, Irán
مصطلحات موضوعية: marine enzymes, cytochrome P450 reductase, purification, biotechnology
العلاقة: Marine Drugs; Publisher's version; https://doi.org/10.3390Test/ md21020099; Sí; Marine Drugs 2023, 21(2), 99; 16603397 (ISSN); http://hdl.handle.net/10261/358108Test; https://www.scopus.com/inward/record.uri?eid=2-s2.0-85148862023&doi=10.3390%2fmd21020099&partnerID=40&md5=96e3d542c9d7e7e373439ddda2bc07b1Test
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10دورية أكاديمية
المؤلفون: Bahramian Nasab, Soudeh, Homaei, Ahmad, FERNANDEZ LAFUENTE, ROBERTO, Del Arco, Jon, Fernández-Lucas, Jesús
مصطلحات موضوعية: Marine enzymes, Cytochrome P450 reductase, Purification, Biotechnology
وصف الملف: 12 páginas; application/pdf
العلاقة: Marine Drugs; 1. Hale, S.S.; Buffum, H.W.; Hughes, M.M. Six decades of change in pollution and benthic invertebrate biodiversity in a southern New England estuary. Mar. Pollut. Bull. 2018, 133, 77–87. [CrossRef] [PubMed]; 2. Gaur, N.; Narasimhulu, K.; PydiSetty, Y. Recent advances in the bio-remediation of persistent organic pollutants and its effect on environment. J. Clean. Prod. 2018, 198, 1602–1631. [CrossRef]; 3. Ismail, M.; Akhtar, K.; Khan, M.; Kamal, T.; Khan, M.A.; Asiri, A.M.; Seo, J.; Khan, S.B. Pollution, toxicity and carcinogenicity of organic dyes and their catalytic bio-remediation. Curr. Pharm. Des. 2019, 25, 3645–3663. [CrossRef]; 4. Razzaghi, M.; Homaei, A.; Vianello, F.; Azad, T.; Sharma, T.; Nadda, A.K.; Stevanato, R.; Bilal, M.; Iqbal, H. Industrial applications of immobilized nano-biocatalysts. Bioprocess Biosyst. Eng. 2022, 45, 237–256. [CrossRef] [PubMed]; 5. Ranjbari, N.; Razzaghi, M.; Fernandez-Lafuente, R.; Shojaei, F.; Satari, M.; Homaei, A. Improved features of a highly stable protease from Penaeus vannamei by immobilization on glutaraldehyde activated graphene oxide nanosheets. Int. J. Biol. Macromol. 2019, 130, 564–572. [CrossRef]; 6. Yan, H.; Wu, L.; Yu, J. The environmental impact analysis of hazardous materials and the development of green technology in the shipbreaking process. Ocean Eng. 2018, 161, 187–194. [CrossRef]; 7. Homaei, A. Purification and biochemical properties of highly efficient alkaline phosphatase from Fenneropenaeus merguiensis brain. J. Mol. Catal. B Enzym. 2015, 118, 16–22. [CrossRef]; 8. Ufarte, L.; Laville, E.; Duquesne, S.; Potocki-Veronese, G. Metagenomics for the discovery of pollutant degrading enzymes. Biotechnol. Adv. 2015, 33, 1845–1854. [CrossRef]; 9. Kadri, T.; Rouissi, T.; Brar, S.K.; Cledon, M.; Sarma, S.; Verma, M. Biodegradation of polycyclic aromatic hydrocarbons (PAHs) by fungal enzymes: A review. J. Environ. Sci. 2017, 51, 52–74. [CrossRef]; 11. Ahuja, S.K.; Ferreira, G.M.; Moreira, A.R. Utilization of enzymes for environmental applications. Crit. Rev. Biotechnol. 2004, 24, 125–154. [CrossRef]; 12. Nikolaivits, E.; Dimarogona, M.; Fokialakis, N.; Topakas, E. Marine-derived biocatalysts: Importance, accessing, and application in aromatic pollutant bioremediation. Front. Microbiol. 2017, 8, 265. [CrossRef] [PubMed]; 13. Menzorova, N.I.; Seitkalieva, A.V.; Rasskazov, V.A. Enzymatic methods for the determination of pollution in seawater using salt resistant alkaline phosphatase from eggs of the sea urchin Strongylocentrotus intermedius. Mar. Pollut. Bull. 2014, 79, 188–195. [CrossRef] [PubMed]; 14. Seitkalieva, A.V.; Menzorova, N.I.; Rasskazov, V.A. Application of different enzyme assays and biomarkers for pollution monitoring of the marine environment. Environ. Monit. Assess. 2016, 188, 1–13. [CrossRef] [PubMed]; 15. Ducharme, J.; Auclair, K. Use of bioconjugation with cytochrome P450 enzymes. Biochim. Et Biophys. Acta (BBA) Proteins Proteom. 2018, 1866, 32–51. [CrossRef] [PubMed]; 16. Rudeck, J.; Bert, B.; Marx-Stoelting, P.; Schönfelder, G.; Vogl, S. Liver lobe and strain differences in the activity of murine cytochrome p450 enzymes. Toxicology 2018, 404, 76–85. [CrossRef] [PubMed]; 17. Brummund, J.; Müller, M.; Schmitges, T.; Kaluzna, I.; Mink, D.; Hilterhaus, L.; Liese, A. Process development for oxidations of hydrophobic compounds applying cytochrome P450 monooxygenases in-vitro. J. Biotechnol. 2016, 233, 143–150. [CrossRef]; 18. Sharma, B.; Dangi, A.K.; Shukla, P. Contemporary enzyme based technologies for bioremediation: A review. J. Environ. Manag. 2018, 210, 10–22. [CrossRef] [PubMed]; 19. Zheng, S.; Chen, B.; Qiu, X.; Lin, K.; Yu, X. Three novel cytochrome P450 genes identified in the marine polychaete Perinereis nuntia and their transcriptional response to xenobiotics. Aquat. Toxicol. 2013, 134, 11–22. [CrossRef]; 20. Han, J.; Won, E.-J.; Kang, H.-M.; Lee, M.-C.; Jeong, C.-B.; Kim, H.-S.; Hwang, D.-S.; Lee, J.-S. Marine copepod cytochrome P450 genes and their applications for molecular ecotoxicological studies in response to oil pollution. Mar. Pollut. Bull. 2017, 124, 953–961. [CrossRef]; 21. Basilone, G.; Gargano, A.; Corriero, A.; Zupa, R.; Santamaria, N.; Mangano, S.; Ferreri, R.; Pulizzi, M.; Mazzola, S.; Bonanno, A. Liver melanomacrophage centres and CYP1A expression as response biomarkers to environmental pollution in European anchovy (Engraulis encrasicolus) from the western Mediterranean Sea. Mar. Pollut. Bull. 2018, 131, 197–204. [CrossRef] [PubMed]; 22. Mundle, S.O.; Spain, J.C.; Lacrampe-Couloume, G.; Nishino, S.F.; Lollar, B.S. Branched pathways in the degradation of cDCE by cytochrome P450 in Polaromonas sp. JS666. Sci. Total Environ. 2017, 605, 99–105. [CrossRef] [PubMed]; 23. Gunasekaran, V.; Donmez, E.; Girhard, M.; Urlacher, V.B.; Constantí, M. Biodegradation of fuel oxygenates and their effect on the expression of a newly identified cytochrome P450 gene in Achromobacter xylosoxidans MCM2/2/1. Process Biochem. 2014, 49, 124–129. [CrossRef]; 24. Wu, R.-R.; Dang, Z.; Yi, X.-Y.; Yang, C.; Lu, G.-N.; Guo, C.-L.; Liu, C.-Q. The effects of nutrient amendment on biodegradation and cytochrome P450 activity of an n-alkane degrading strain of Burkholderia sp. GS3C. J. Hazard. Mater. 2011, 186, 978–983. [CrossRef] [PubMed]; 25. Pandey, A.V.; Flück, C.E. NADPH P450 oxidoreductase: Structure, function, and pathology of diseases. Pharmacol. Ther. 2013, 138, 229–254. [CrossRef] [PubMed]; 26. Klotz, A.V.; Stegeman, J.J.; Walsh, C. An aryl hydrocarbon hydroxylating hepatic cytochrome P-450 from the marine fish Stenotomus chrysops. Arch. Biochem. Biophys. 1983, 226, 578–592. [CrossRef]; 27. Sen, A.; Arinc, E. Purification and characterization of cytochrome P450 reductase from liver microsomes of feral leaping mullet (Liza saliens). J. Biochem. Mol. Toxicol. 1998, 12, 103–113. [CrossRef]; 28. Arinç, E. Characterization of cytochrome P450 dependent mixed-function oxidase system of gilthead seabream (Sparus aurata; Sparidae) liver. Comp. Biochem. Physiol. Part B Comp. Biochem. 1993, 104, 133–139. [CrossRef]; 29. Kojima, H.; Takahashi, K.; Sakane, F.; Koyama, J. Purification and characterization of NADPH-cytochrome c reductase from porcine polymorphonuclear leukocytes. J. Biochem. 1987, 102, 1083–1088. [CrossRef]; 30. Kubota, S.; Yoshida, Y.; Kumaoka, H.; Furumichi, A. Studies on the microsomal electron-transport system of anaerobically grown yeast: V. Purification and characterization of NADPH-cytochrome c reductase. J. Biochem. 1977, 81, 197–205. [CrossRef]; 31. Shen, A.L.; Porter, T.; Wilson, T.; Kasper, C. Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed mutagenesis. J. Biol. Chem. 1989, 264, 7584–7589. [CrossRef] [PubMed]; 32. Kuzu, M.; Ciftci, M. Purification and characterization of NADPH-cytochrome P450 reductase from Lake Van fish liver microsomes and investigation of some chemical and metals’ effects on the enzyme activity. Turk. J. Chem. 2015, 39, 149–158. [CrossRef]; 33. Kuwahara, T.; White, R.A., Jr.; Agosin, M. A cytosolic FAD-containing enzyme catalyzing cytochrome c reduction in Trypanosoma cruzi. I. Purification and some properties. Arch. Biochem. Biophys. 1985, 239, 18–28. [CrossRef] [PubMed]; 34. Tsou, C.-Y.; Matsunaga, S.; Okada, S. Molecular cloning and functional characterization of NADPH-dependent cytochrome P450 reductase from the green microalga Botryococcus braunii, B race. J. Biosci. Bioeng. 2018, 125, 30–37. [CrossRef]; 35. Milhim, M.; Gerber, A.; Neunzig, J.; Hannemann, F.; Bernhardt, R. A Novel NADPH-dependent flavoprotein reductase from Bacillus megaterium acts as an efficient cytochrome P450 reductase. J. Biotechnol. 2016, 231, 83–94. [CrossRef]; 36. Lee, G.-Y.; Kim, H.M.; Ma, S.H.; Park, S.H.; Joung, Y.H.; Yun, C.-H. Heterologous expression and functional characterization of the NADPH-cytochrome P450 reductase from Capsicum annuum. Plant Physiol. Biochem. 2014, 82, 116–122. [CrossRef]; 37. Takahashi, N.; Saito, T.; Goda, Y.; Tomita, K. Characterization of microsomal NADPH-dependent aldehyde reductase from rat brain. J. Biochem. 1986, 99, 513–519. [CrossRef]; 38. Bradford, M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248–254. [CrossRef]; 39. Guengerich, F.P.; Martin, M.V.; Sohl, C.D.; Cheng, Q. Measurement of cytochrome P450 and NADPH–cytochrome P450 reductase. Nat. Protoc. 2009, 4, 1245. [CrossRef]; 40. Williams, J.; Kamin, H. The preparation and properties of microsomal TPNH-cytochrome c reductase from pig liver. J. Biol. Chem. 1962, 237, 587–595. [CrossRef]; 41. Yonetani, T. Studies on cytochrome c peroxidase II. Stoichiometry between enzyme, H2O2, and ferrocytochrome c and enzymic determination of extinction coefficients of cytochrome c. J. Biol. Chem. 1965, 240, 4509–4514. [CrossRef] [PubMed]; 42. Swift, M.L. GraphPad prism, data analysis, and scientific graphing. J. Chem. Inf. Comput. Sci. 1997, 37, 411–412. [CrossRef]; 43. Arrhenius, S. On the reaction velocity of the inversion of cane sugar by acids. J. Phys. Chem 1889, 4, 226.; 44. Copeland, R.A. Enzymes: A Practical Introduction to Structure, Mechanism, and Data Analysis; John Wiley & Sons: Hoboken, NJ, USA, 2004.; 45. Lamb, S.B.; Lamb, D.C.; Kelly, S.L.; Stuckey, D.C. Cytochrome P450 immobilisation as a route to bioremediation/biocatalysis. FEBS Lett. 1998, 431, 343–346. [CrossRef]; 12; 21; Bahramian Nasab, S.; Homaei, A.; Fernandez-Lafuente, R.; Del Arco, J.; Fernández-Lucas, J. A Novel, Highly Potent NADPH-Dependent Cytochrome P450 Reductase from Waste Liza klunzingeri Liver. Mar. Drugs 2023, 21, 99. https://doi.org/10.3390Test/ md21020099; https://hdl.handle.net/11323/10385Test; Corporación Universidad de la Costa; REDICUC - Repositorio CUC; https://repositorio.cuc.edu.coTest/