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Relevant bibliographies by topics / CYP10181

Academic literature on the topic 'CYP10181'

Author: Grafiati

Published: 10 December 2022

Last updated: 29 January 2023

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Journal articles on the topic "CYP10181"

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Hussain, Haitham A., and John M. Ward. "Enhanced Heterologous Expression of Two Streptomyces griseolus Cytochrome P450s and Streptomyces coelicolor Ferredoxin Reductase as Potentially Efficient Hydroxylation Catalysts." Applied and Environmental Microbiology 69, no. 1 (January 2003): 373–82. http://dx.doi.org/10.1128/aem.69.1.373-382.2003.

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ABSTRACT The herbicide-inducible, soluble cytochrome P450s CYP105A1 and CYP105B1 and their adjacent ferredoxins, Fd1 and Fd2, of Streptomyces griseolus were expressed in Escherichia coli to high levels. Conditions for high-level expression of active enzyme able to catalyze hydroxylation have been developed. Analysis of the expression levels of the P450 proteins in several different E. coli expression hosts identified E. coli BL21 Star(DE3)pLysS as the optimal host cell to express CYP105B1 as judged by CO difference spectra. Examination of the codons used in the CYP1051A1 sequence indicated that it contains a number of codons corresponding to rare E. coli tRNA species. The level of its expression was improved in the modified forms of E. coli BL21(DE3), which contain extra copies of rare codon E. coli tRNA genes. The activity of correctly folded cytochrome P450s was further enhanced by cloning a ferredoxin reductase from Streptomyces coelicolor downstream of CYP105A1 and CYP105B1 and their adjacent ferredoxins. Expression of CYP105A1 and CYP105B1 was also achieved in Streptomyces lividans 1326 by cloning the P450 genes and their ferredoxins into the expression vector pBW160. S. lividans 1326 cells containing CYP105A1 or CYP105B1 were able efficiently to dealkylate 7-ethoxycoumarin.

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Yang, Wen, Stephen G. Bell, Hui Wang, Weihong Zhou, Mark Bartlam, Luet-Lok Wong, and Zihe Rao. "The structure of CYP101D2 unveils a potential path for substrate entry into the active site." Biochemical Journal 433, no. 1 (December 15, 2010): 85–93. http://dx.doi.org/10.1042/bj20101017.

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The cytochrome P450 CYP101D2 from Novosphingobium aromaticivorans DSM12444 is closely related to CYP101D1 from the same bacterium and to P450cam (CYP101A1) from Pseudomonas putida. All three are capable of oxidizing camphor stereoselectively to 5-exo-hydroxycamphor. The crystal structure of CYP101D2 revealed that the likely ferredoxin-binding site on the proximal face is largely positively charged, similar to that of CYP101D1. However, both the native and camphor-soaked forms of CYP101D2 had open conformations with an access channel. In the active site of the camphor-soaked form, the camphor carbonyl interacted with the haem-iron-bound water. Two other potential camphor-binding sites were also identified from electron densities in the camphor-soaked structure: one located in the access channel, flanked by the B/C and F/G loops and the I helix, and the other in a cavity on the surface of the enzyme near the F helix side of the F/G loop. The observed open structures may be conformers of the CYP101D2 enzyme that enable the substrate to enter the buried active site via a conformational selection mechanism. The second and third binding sites may be intermediate locations of substrate entry and translocation into the active site, and provide insight into a multi-step substrate-binding mechanism.

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Unterweger, Birgit, Dieter M. Bulach, Judith Scoble, David J. Midgley, Paul Greenfield, Dena Lyras, Priscilla Johanesen, and Geoffrey J. Dumsday. "CYP101J2, CYP101J3, and CYP101J4, 1,8-Cineole-Hydroxylating Cytochrome P450 Monooxygenases from Sphingobium yanoikuyae Strain B2." Applied and Environmental Microbiology 82, no. 22 (September 2, 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 characterized. Recombinant whole-cell biotransformation inE. colidemonstrated that all three P450s hydroxylate 1,8-cineole using electron transport partners fromE. colito yield a product putatively identified as (1S)-2α-hydroxy-1,8-cineole or (1R)-6α-hydroxy-1,8-cineole. The new P450s belong to the CYP101 family and share 47% and 44% identity with other 1,8-cineole-hydroxylating members found inNovosphingobium aromaticivoransandPseudomonas putida. Compared to P450cin(CYP176A1), a 1,8-cineole-hydroxylating P450 fromCitrobacter braakii, these enzymes share less than 30% amino acid sequence identity and hydroxylate 1,8-cineole in a different orientation. Expansion of the enzyme toolbox for modification of 1,8-cineole creates a starting point for use of hydroxylated derivatives in a range of industrial applications.IMPORTANCECYP101J2, CYP101J3, and CYP101J4 are cytochrome P450 monooxygenases fromS. yanoikuyaeB2 that hydroxylate the monoterpenoid 1,8-cineole. These enzymes not only play an important role in microbial degradation of this plant-based chemical but also provide an interesting route to synthesize oxygenated 1,8-cineole derivatives for applications as natural flavor and fragrance precursors or incorporation into polymers. The P450 cytochromes also provide an interesting basis from which to compare other enzymes with a similar function and expand the CYP101 family. This could eventually provide enough bacterial parental enzymes with similar amino acid sequences to enablein vitroevolution via DNA shuffling.

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Sarkar, Md Raihan, and Stephen G. Bell. "Complementary and selective oxidation of hydrocarbon derivatives by two cytochrome P450 enzymes of the same family." Catalysis Science & Technology 10, no. 17 (2020): 5983–95. http://dx.doi.org/10.1039/d0cy01040e.

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The cytochrome P450 enzymes CYP101B1 and CYP101C1, from a Novosphingobium bacterium, can efficiently hydroxylate hydrocarbon derivatives containing a carbonyl moiety. Cyclic ketones (C9 to C15) were oxidised with contrasting yet high selectivity.

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Amaya, José A., Dipanwita Batabyal, and Thomas L. Poulos. "Proton Relay Network in the Bacterial P450s: CYP101A1 and CYP101D1." Biochemistry 59, no. 31 (June 23, 2020): 2896–902. http://dx.doi.org/10.1021/acs.biochem.0c00329.

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Lamb, David C., Li Lei, Bin Zhao, Hang Yuan, Colin J. Jackson, Andrew G. S. Warrilow, Tove Skaug, et al. "Streptomyces coelicolor A3(2) CYP102 Protein, a Novel Fatty Acid Hydroxylase Encoded as a Heme Domain without an N-Terminal Redox Partner." Applied and Environmental Microbiology 76, no. 6 (January 22, 2010): 1975–80. http://dx.doi.org/10.1128/aem.03000-09.

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ABSTRACT The gene from Streptomyces coelicolor A3(2) encoding CYP102B1, a recently discovered CYP102 subfamily which exists solely as a single P450 heme domain, has been cloned, expressed in Escherichia coli, purified, characterized, and compared to its fusion protein family members. Purified reconstitution metabolism experiments with spinach ferredoxin, ferredoxin reductase, and NADPH revealed differences in the regio- and stereoselective metabolism of arachidonic acid compared to that of CYP102A1, exclusively producing 11,12-epoxyeicosa-5,8,14-trienoic acid in addition to the shared metabolites 18-hydroxy arachidonic acid and 14,15-epoxyeicosa-5,8,11-trienoic acid. Consequently, in order to elucidate the physiological function of CYP102B1, transposon mutagenesis was used to generate an S. coelicolor A3(2) strain lacking CYP102B1 activity and the phenotype was assessed.

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Subedi, Pradeep, Hackwon Do, Jun Hyuck Lee, and Tae-Jin Oh. "Crystal Structure and Biochemical Analysis of a Cytochrome P450 CYP101D5 from Sphingomonas echinoides." International Journal of Molecular Sciences 23, no. 21 (November 1, 2022): 13317. http://dx.doi.org/10.3390/ijms232113317.

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Cytochrome P450 enzymes (CYPs) are heme-containing enzymes that catalyze hydroxylation with a variety of biological molecules. Despite their diverse activity and substrates, the structures of CYPs are limited to a tertiary structure that is similar across all the enzymes. It has been presumed that CYPs overcome substrate selectivity with highly flexible loops and divergent sequences around the substrate entrance region. Here, we report the newly identified CYP101D5 from Sphingomonas echinoides. CYP101D5 catalyzes the hydroxylation of β-ionone and flavonoids, including naringenin and apigenin, and causes the dehydrogenation of α-ionone. A structural investigation and comparison with other CYP101 families indicated that spatial constraints at the substrate-recognition site originate from the B/C loop. Furthermore, charge distribution at the substrate binding site may be important for substrate selectivity and the preference for CYP101D5.

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Dezvarei, Shaghayegh, Joel H. Z. Lee, and Stephen G. Bell. "Stereoselective hydroxylation of isophorone by variants of the cytochromes P450 CYP102A1 and CYP101A1." Enzyme and Microbial Technology 111 (April 2018): 29–37. http://dx.doi.org/10.1016/j.enzmictec.2018.01.002.

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Shumyantseva, V. V., A. V. Kuzikov, R. A. Masamrekh, Y. Khatri, M. G. Zavialova, R. Bernhardt, and A. I. Archakov. "Direct electrochemistry of CYP109C1, CYP109C2 and CYP109D1 from Sorangium cellulosum So ce56." Electrochimica Acta 192 (February 2016): 72–79. http://dx.doi.org/10.1016/j.electacta.2016.01.162.

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Ueno, Motoi, Midori Yamashita, Michizane Hashimoto, Motohiro Hino, and Akihiko Fujie. "Oxidative activities of heterologously expressed CYP107B1 and CYP105D1 in whole-cell biotransformation using Streptomyces lividans TK24." Journal of Bioscience and Bioengineering 100, no. 5 (November 2005): 567–72. http://dx.doi.org/10.1263/jbb.100.567.

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Dissertations / Theses on the topic "CYP10181"

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Maurer, Steffen Christian. "Oxidationsreaktionen mittels der Cytochrom P450-Monooxygenase CYP102A1 in Enzymreaktoren." [S.l. : s.n.], 2006. http://nbn-resolving.de/urn:nbn:de:bsz:93-opus-28118.

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Povsic, Manca. "Rational redesign of cytochrome P450 BM3 (CYP102A1) towards industrially relevant drug metabolites." Thesis, University of Manchester, 2016. https://www.research.manchester.ac.uk/portal/en/theses/rational-redesign-of-cytochrome-p450-bm3-cyp102a1-towards-industrially-relevant-drug-metabolites(1e9b4e44-0211-4ffc-8684-7db1c9a21791).html.

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Human drug metabolites are frequently biologically active, with many implications for human health. Pharmaceutical companies have become increasingly aware of the need to identify and test these metabolites. The P450 BM3 enzyme from Bacillus megaterium offers substantial advantages to the current methods of metabolite synthesis, as its soluble, catalytically self-sufficient nature, coupled with its high catalytic activity, make P450 BM3 ideal for engineering towards specificity for human drugs. The highly-active I401P BM3 mutant was characterized for its reactivity towards human drugs and for the development of a human P450-like metabolite profile. The I401P mutant exhibits binding to molecules including alkaloids, steroids, and azole drugs, along with many other compounds. I401P binds/oxidizes human CYP substrates, including alosetron, phenacetin, caffeine, nicotine and diclofenac. LC-MS product identification shows that I401P BM3 forms 4OH-diclofenac, the major human metabolite for diclofenac. I401P BM3 also produces nornicotine, the second major human metabolite of nicotine. I401P BM3 also forms theophylline, theobromine and paraxanthine, the three major human metabolites of caffeine. Thermostability (DSC) data show that the I401P mutation destabilizes the BM3 heme domain in both its substrate-free and substrate-bound forms. The I401P heme domain X-ray crystal structure reinforces previous structural observations that the Pro401 mutation causes the BM3 protein to adopt a high-spin, "substrate-bound" state, with a displaced heme iron axial water, producing a "catalytically primed" mutant with greater diversity in substrate selectivity. The destabilisation of the BM3 heme domain structure due to the Pro401 mutation increases conformational plasticity in this mutant, allowing it to function as a platform for future mutagenesis aimed at improved binding and metabolite yield from specific drug substrates. Further proline mutations (A330P, A330P/I401P and A82F/F87V/I401P) were examined for increased affinity for drug substrates. The A330P mutant shows no novel drug substrate specificity, despite its reported affinity for small molecules. The A330P/I401P double mutant demonstrates weak binding to WT BM3 and I401P substrates, but no synergistic effects were obtained by combining the two mutations. The double mutant exhibits very low solvent tolerance and significant structural destabilisation. DSC data confirms this, with the double mutant destabilising the BM3 heme domain by up to 20 °C. Initial work with the A82F/F87V/I401P mutant showed increased affinity for A82F/F87V- and I401P-type substrates, including diclofenac. LC-MS product analysis confirms that the A82F/F87V/I401P mutant oxidises diclofenac into its major human metabolite 4OH-diclofenac. These data indicate that human-like oxidation reactions are feasible with BM3 mutants. In this work, proline insertion mutants were generated that introduced novel affinity for biotechnologically relevant substrates. In particular the I401P mutant offers an excellent platform for future biotechnological engineering.

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Putkaradze, Natalia [Verfasser], and Rita [Akademischer Betreuer] Bernhardt. "Biotechnologically important biotransformations by CYP106A2 and CYP109E1 from Bacillus megaterium / Natalia Putkaradze ; Betreuer: Rita Bernhardt." Saarbrücken : Saarländische Universitäts- und Landesbibliothek, 2018. http://d-nb.info/1166140024/34.

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Putkaradze, Natalia Verfasser], and Rita [Akademischer Betreuer] [Bernhardt. "Biotechnologically important biotransformations by CYP106A2 and CYP109E1 from Bacillus megaterium / Natalia Putkaradze ; Betreuer: Rita Bernhardt." Saarbrücken : Saarländische Universitäts- und Landesbibliothek, 2018. http://d-nb.info/1166140024/34.

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Koe, Gary Shizumi. "Decomposition of 1,2-dibromo-3-chloropropane (DBCP) by cytochrome P-450cam (CYP101)." Diss., Restricted to subscribing institutions, 2009. http://proquest.umi.com/pqdweb?did=2025617391&sid=1&Fmt=2&clientId=1564&RQT=309&VName=PQD.

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Baker, George. "The characterisation of the flavocytochrome P450-CPR fusion enzymes CYP505A30 from Myceliophthora thermophila and CYP102A1 from Bacillus megaterium." Thesis, University of Manchester, 2016. https://www.research.manchester.ac.uk/portal/en/theses/the-characterisation-of-the-flavocytochrome-p450cpr-fusion-enzymes-cyp505a30-from-myceliophthora-thermophila-and-cyp102a1-from-bacillus-megaterium(f064fb08-300f-4d09-a03a-f00017c4ba68).html.

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High catalytic activity and a broad substrate range are characteristic of P450 fusion enzymes of the CYP102A class. P450 BM3 (CYP102A1, BM3) is a paradigm for the P450 fusion enzymes and is accredited with the highest monooxygenase activity in the P450 superfamily, a property which has led to its engineering and exploitation for biotechnologically valuable oxidation reactions. Initial research in the thesis focused on characterisation of a novel P450-redox partner fusion enzyme from the thermophilic fungus Myceliophthora thermophila (CYP505A30, P450MT1). Sequence alignments revealed a P450 domain and a diflavin P450 reductase domain with high sequence similarity to BM3’s domains (41% and 31% amino acid identity, respectively). The purified 118 kDa protein is soluble and exhibits characteristic P450 spectral properties, giving a Soret absorption shift to 450 nm upon binding CO to its ferrous heme iron. Binding titrations of intact P450 MT1 and its expressed P450 (heme) domain with fatty acid substrates and imidazole-based inhibitors revealed type I (blue) and II (red) Soret shifts, respectively, typical of other members of the P450 superfamily, and enabled determination of substrate binding constants. HPLC analysis confirmed stoichiometric amounts of bound FAD and FMN cofactors. Subsequent kinetic and biochemical studies included stopped-flow kinetic experiments showing that NADPH-dependent reduction of P450 MT1’s FAD cofactor occurs with a rate constant of ~150 s-1 at 20 °C. P450 MT1 has an unconventional substrate hydroxylation profile for saturated fatty acids. It hydroxylates these substrates predominantly at positions ω-1, ω-2 and ω-3. However, an unusual property of this enzyme is observed in its strong preference (~85% of total converted product) for either the ω-1 or the ω-2 position on odd and even chain length fatty acids, respectively. However, it displays higher selectivity for branched chain fatty acids over straight chain fatty acids, e.g. for the substrate iso-myristic acid, similar to BM3’s properties. Other work done focused on biophysical characterisation of the model P450-reductase fusion enzyme P450 BM3 from Bacillus megaterium. A combination of alternative structural techniques to X-ray crystallography were used to characterise the enzyme. More specifically, electron microscopy (EM) and nuclear magnetic resonance (NMR) were used to gain greater insights into the intimate associations of the enzyme monomers in BM3’s dimeric structure. These studies led to the first structural insights into how P450 BM3’s dimeric complex is organised. Dimerisation in BM3 arises predominantly from self-association of the enzyme’s FAD domains, and wild-type and mutant BM3 FAD domain forms were also characterised. Key FAD domain mutations that prevented intra-/inter-monomer disulphide bond formation facilitated the crystallization and determination of the FAD domain structure, the final part of the BM3 enzyme to have its three dimensional structure resolved. Data reported in this thesis give new insights into the biochemistry of biotechnologically important P450 monooxygenase enzymes from mesophilic and thermophilic microorganisms.

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Janocha, Simon [Verfasser], and Rita [Akademischer Betreuer] Bernhardt. "Umsatz von Harzsäuren durch die bakteriellen Cytochrome CYP105A1 und CYP106A2 - strukturelle Grundlagen und potentielle Anwendungen / Simon Janocha. Betreuer: Rita Bernhardt." Saarbrücken : Saarländische Universitäts- und Landesbibliothek, 2014. http://d-nb.info/1053725043/34.

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Janocha, Simon Verfasser], and Rita [Akademischer Betreuer] [Bernhardt. "Umsatz von Harzsäuren durch die bakteriellen Cytochrome CYP105A1 und CYP106A2 - strukturelle Grundlagen und potentielle Anwendungen / Simon Janocha. Betreuer: Rita Bernhardt." Saarbrücken : Saarländische Universitäts- und Landesbibliothek, 2014. http://d-nb.info/1053725043/34.

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Walsh, Mark E. "The reductive dehalogenation of hexachloroethane and #gamma# - lindane by cytochrome P450 â†câ†aâ†m (CYP101)." Thesis, University of Oxford, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.249197.

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Kleser, Michael Werner [Verfasser], and Rita [Akademischer Betreuer] Bernhardt. "Etablierung einer Biotransformation zur stereoselektiven Hydroxylierung der Sulfonylharnstoffe Glimepirid und Glibenclamid sowie von Vitamin D3 mit CYP105A1 / Michael Werner Kleser. Betreuer: Rita Bernhardt." Saarbrücken : Saarländische Universitäts- und Landesbibliothek, 2012. http://d-nb.info/1051588863/34.

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