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Journal articles on the topic 'CYP101C1'

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Author: Grafiati

Published: 10 December 2022

Last updated: 29 January 2023

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1

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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2

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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3

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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4

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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5

Ma, Ming, Stephen G. Bell, Wen Yang, Yiming Hao, Nicholas H. Rees, Mark Bartlam, Weihong Zhou, Luet-Lok Wong, and Zihe Rao. "Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444." ChemBioChem 12, no. 1 (December 10, 2010): 88–99. http://dx.doi.org/10.1002/cbic.201000537.

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6

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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7

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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8

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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9

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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10

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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11

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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12

Kan, Jie, Tao Peng, Tongwang Huang, Guangming Xiong, and Zhong Hu. "NarL, a Novel Repressor for CYP108j1 Expression during PAHs Degradation in Rhodococcus sp. P14." International Journal of Molecular Sciences 21, no. 3 (February 1, 2020): 983. http://dx.doi.org/10.3390/ijms21030983.

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Rhodococcus sp. P14 was isolated from crude-oil-contaminated sediments, and a wide range of polycyclic aromatic hydrocarbons (PAHs) could be used as the sole source of carbon and energy. A key CYP450 gene, designated as cyp108j1 and involved in the degradation of PAHs, was identified and was able to hydroxylate various PAHs. However, the regulatory mechanism of the expression of cyp108j1 remains unknown. In this study, we found that the expression of cyp108j1 is negatively regulated by a LuxR (helix-turn-helix transcription factors in acyl-homoserine lactones-mediated quorum sensing) family regulator, NarL (nitrate-dependent two-component regulatory factor), which is located upstream of cyp108j1. Further analysis revealed that NarL can directly bind to the promoter region of cyp108j1. Mutational experiments demonstrated that the binding site between NarL and the cyp108j1 promoter was the palindromic sequence GAAAGTTG-CAACTTTC. Together, the finding reveal that NarL is a novel repressor for the expression of cyp108j1 during PAHs degradation.

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13

Hall, Emma A., and Stephen G. Bell. "The efficient and selective biocatalytic oxidation of norisoprenoid and aromatic substrates by CYP101B1 from Novosphingobium aromaticivorans DSM12444." RSC Advances 5, no. 8 (2015): 5762–73. http://dx.doi.org/10.1039/c4ra14010a.

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14

Hall, Emma A., Md Raihan Sarkar, and Stephen G. Bell. "The selective oxidation of substituted aromatic hydrocarbons and the observation of uncoupling via redox cycling during naphthalene oxidation by the CYP101B1 system." Catalysis Science & Technology 7, no. 7 (2017): 1537–48. http://dx.doi.org/10.1039/c7cy00088j.

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15

Sarkar, Md Raihan, Samrat Dasgupta, Simon M. Pyke, and Stephen G. Bell. "Selective biocatalytic hydroxylation of unactivated methylene C–H bonds in cyclic alkyl substrates." Chemical Communications 55, no. 34 (2019): 5029–32. http://dx.doi.org/10.1039/c9cc02060h.

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16

Su, Min, Sumita Chakraborty, Yoichi Osawa, and Haoming Zhang. "Cryo-EM reveals the architecture of the dimeric cytochrome P450 CYP102A1 enzyme and conformational changes required for redox partner recognition." Journal of Biological Chemistry 295, no. 6 (January 3, 2020): 1637–45. http://dx.doi.org/10.1074/jbc.ra119.011305.

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Cytochrome P450 family 102 subfamily A member 1 (CYP102A1) is a self-sufficient flavohemeprotein and a highly active bacterial enzyme capable of fatty acid hydroxylation at a >3,000 min−1 turnover rate. The CYP102A1 architecture has been postulated to be responsible for its extraordinary catalytic prowess. However, the structure of a functional full-length CYP102A1 enzyme remains to be determined. Herein, we used a cryo-EM single-particle approach, revealing that full-length CYP102A1 forms a homodimer in which both the heme and FAD domains contact each other. The FMN domain of one monomer was located close to the heme domain of the other monomer, exhibiting a trans configuration. Moreover, full-length CYP102A1 is highly dynamic, existing in multiple conformational states, including open and closed states. In the closed state, the FMN domain closely contacts the FAD domain, whereas in the open state, one of the FMN domains rotates away from its FAD domain and traverses to the heme domain of the other monomer. This structural arrangement and conformational dynamics may facilitate rapid intraflavin and trans FMN-to-heme electron transfers (ETs). Results with a variant having a 12-amino-acid deletion in the CYP102A1 linker region, connecting the catalytic heme and the diflavin reductase domains, further highlighted the importance of conformational dynamics in the ET process. Cryo-EM revealed that the Δ12 variant homodimer is conformationally more stable and incapable of FMN-to-heme ET. We conclude that closed-to-open alternation is crucial for redox partner recognition and formation of an active ET complex for CYP102A1 catalysis.

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17

Park, Chan Mi, Hyun Seo Park, Gun Su Cha, Ki Deok Park, and Chul-Ho Yun. "Regioselective Hydroxylation of Rhododendrol by CYP102A1 and Tyrosinase." Catalysts 10, no. 10 (September 25, 2020): 1114. http://dx.doi.org/10.3390/catal10101114.

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Rhododendrol (RD) is a naturally occurring phenolic compound found in many plants. Tyrosinase (Ty) converts RD to RD-catechol and subsequently RD-quinone via two-step oxidation reactions, after which RD-melanin forms spontaneously from RD-quinone. RD is cytotoxic in melanocytes and lung cancer cells, but not in keratinocytes and fibroblasts. However, the function of RD metabolites has not been possible to investigate due to the lack of available high purity metabolites. In this study, an enzymatic strategy for RD-catechol production was devised using engineered cytochrome P450 102A1 (CYP102A1) and Ty, and the product was analyzed using high-performance liquid chromatography (HPLC), LC-MS, and NMR spectroscopy. Engineered CYP102A1 regioselectively produced RD-catechol via hydroxylation at the ortho position of RD. Although RD-quinone was subsequently formed by two step oxidation in Ty catalyzed reactions, L-ascorbic acid (LAA) inhibited RD-quinone formation and contributed to regioselective production of RD-catechol. When LAA was present, the productivity of RD-catechol by Ty was 5.3-fold higher than that by engineered CYP102A1. These results indicate that engineered CYP102A1 and Ty can be used as effective biocatalysts to produce hydroxylated products, and Ty is a more cost-effective biocatalyst for industrial applications than engineered CYP102A1.

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18

Ivanov, Yu D., N. S. Bukharina, P. A. Frantsuzov, T. O. Pleshakova, N. V. Krohin, S. L. Kanashenko, and A. I. Archakov. "Oligomeric state investigation of flavocytochrome CYP102A1 using afm with standard and supersharp probes." Biomeditsinskaya Khimiya 59, no. 4 (2013): 378–87. http://dx.doi.org/10.18097/pbmc20135904378.

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Atomic force microscopy with two types of probes – standard (radius of curvature R~10 nm) and supersharp (R~2 nm) – was used to determine CYP102A1oligomeric state. CYP102A1 images were obtained in a liquid, air and vacuum environment using the standard probes, also a ratio of monomers to oligomers (a) of CYP102A1 were determined as a=0.48:0.52. At the same time use of standard probes did not allow to resolve the structure of these oligomers. Supersharp probes allowed to obtain the data about the monomers to oligomers ratio, and also about the dimers/trimers/tetramers ratio in air and vacuum. So, a ratio a of CYP102A1 in liquid can be determined by the standard probes, and an oligomeric state of protein can be specified by the supersharp probes.

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19

Nguyen, Ngoc Anh, Ngoc Tan Cao, Thi Huong Ha Nguyen, Jung-Hwan Ji, Gun Su Cha, Hyung-Sik Kang, and Chul-Ho Yun. "Enzymatic Production of 3-OH Phlorizin, a Possible Bioactive Polyphenol from Apples, by Bacillus megaterium CYP102A1 via Regioselective Hydroxylation." Antioxidants 10, no. 8 (August 23, 2021): 1327. http://dx.doi.org/10.3390/antiox10081327.

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Phlorizin is the most abundant glucoside of phloretin from the apple tree and its products. Phlorizin and its aglycone phloretin are currently considered health-beneficial polyphenols from apples useful in treating hyperglycemia and obesity. Recently, we showed that phloretin could be regioselectively hydroxylated to make 3-OH phloretin by Bacillus megaterium CYP102A1 and human P450 enzymes. The 3-OH phloretin has a potent inhibitory effect on differentiating 3T3-L1 preadipocytes into adipocytes and lipid accumulation. The glucoside of 3-OH phloretin would be a promising agent with increased bioavailability and water solubility compared with its aglycone. However, procedures to make 3-OH phlorizin, a glucoside of 3-OH phloretin, using chemical methods, are not currently available. Here, a biocatalytic strategy for the efficient synthesis of a possibly valuable hydroxylated product, 3-OH phlorizin, was developed via CYP102A1-catalyzed regioselective hydroxylation. The production of 3-OH phlorizin by CYP102A1 was confirmed by HPLC and LC–MS spectroscopy in addition to enzymatic removal of its glucose moiety for comparison to 3-OH phloretin. Taken together, in this study, we found a panel of mutants from B. megaterium CYP102A1 could catalyze regioselective hydroxylation of phlorizin to produce 3-OH phlorizin, a catechol product.

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20

Xu, Lian-Hua, Shinya Fushinobu, Haruo Ikeda, Takayoshi Wakagi, and Hirofumi Shoun. "Crystal Structures of Cytochrome P450 105P1 from Streptomyces avermitilis: Conformational Flexibility and Histidine Ligation State." Journal of Bacteriology 191, no. 4 (December 12, 2008): 1211–19. http://dx.doi.org/10.1128/jb.01276-08.

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ABSTRACT The polyene macrolide antibiotic filipin is widely used as a probe for cholesterol in biological membranes. The filipin biosynthetic pathway of Streptomyces avermitilis contains two position-specific hydroxylases, C26-specific CYP105P1 and C1′-specific CYP105D6. In this study, we describe the three X-ray crystal structures of CYP105P1: the ligand-free wild-type (WT-free), 4-phenylimidazole-bound wild-type (WT-4PI), and ligand-free H72A mutant (H72A-free) forms. The BC loop region in the WT-free structure has a unique feature; the side chain of His72 within this region is ligated to the heme iron. On the other hand, this region is highly disordered and widely open in WT-4PI and H72A-free structures, respectively. Histidine ligation of wild-type CYP105P1 was not detectable in solution, and a type II spectral change was clearly observed when 4-phenylimidazole was titrated. The H72A mutant showed spectroscopic characteristics that were almost identical to those of the wild-type protein. In the H72A-free structure, there is a large pocket that is of the same size as the filipin molecule. The highly flexible feature of the BC loop region of CYP105P1 may be required to accept a large hydrophobic substrate.

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21

Syed, Khajamohiddin, Aleksey Porollo, Ying Wai Lam, Paul E. Grimmett, and Jagjit S. Yadav. "CYP63A2, a Catalytically Versatile Fungal P450 Monooxygenase Capable of Oxidizing Higher-Molecular-Weight Polycyclic Aromatic Hydrocarbons, Alkylphenols, and Alkanes." Applied and Environmental Microbiology 79, no. 8 (February 15, 2013): 2692–702. http://dx.doi.org/10.1128/aem.03767-12.

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ABSTRACTCytochrome P450 monooxygenases (P450s) are known to oxidize hydrocarbons, albeit with limited substrate specificity across classes of these compounds. Here we report a P450 monooxygenase (CYP63A2) from the model ligninolytic white rot fungusPhanerochaete chrysosporiumthat was found to possess a broad oxidizing capability toward structurally diverse hydrocarbons belonging to mutagenic/carcinogenic fused-ring higher-molecular-weight polycyclic aromatic hydrocarbons (HMW-PAHs), endocrine-disrupting long-chain alkylphenols (APs), and crude oil aliphatic hydrocarbonn-alkanes. A homology-based three-dimensional (3D) model revealed the presence of an extraordinarily large active-site cavity in CYP63A2 compared to the mammalian PAH-oxidizing (CYP3A4, CYP1A2, and CYP1B1) and bacterial aliphatic-hydrocarbon-oxidizing (CYP101D and CYP102A1) P450s. This structural feature in conjunction with ligand docking simulations suggested potential versatility of the enzyme. Experimental characterization using recombinantly expressed CYP63A2 revealed its ability to oxidize HMW-PAHs of various ring sizes, including 4 rings (pyrene and fluoranthene), 5 rings [benzo(a)pyrene], and 6 rings [benzo(ghi)perylene], with the highest enzymatic activity being toward the 5-ring PAH followed by the 4-ring and 6-ring PAHs, in that order. Recombinant CYP63A2 activity yielded monohydroxylated PAH metabolites. The enzyme was found to also act as an alkane ω-hydroxylase that oxidizedn-alkanes with various chain lengths (C9to C12and C15to C19), as well as alkyl side chains (C3to C9) in alkylphenols (APs). CYP63A2 showed preferential oxidation of long-chain APs and alkanes. To our knowledge, this is the first P450 identified from any of the biological kingdoms that possesses such broad substrate specificity toward structurally diverse xenobiotics (PAHs, APs, and alkanes), making it a potent enzyme biocatalyst candidate to handle mixed pollution (e.g., crude oil spills).

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22

Kaderbhai, Mustak A., Cynthia C. Ugochukwu, Steven L. Kelly, and David C. Lamb. "Export of Cytochrome P450 105D1 to the Periplasmic Space of Escherichia coli." Applied and Environmental Microbiology 67, no. 5 (May 1, 2001): 2136–38. http://dx.doi.org/10.1128/aem.67.5.2136-2138.2001.

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ABSTRACT CYP105D1, a cytochrome P450 from Streptomyces griseus, was appended at its amino terminus to the secretory signal of Escherichia coli alkaline phosphatase and placed under the transcriptional control of the nativephoA promoter. Heterologous expression in E. coli phosphate-limited medium resulted in abundant synthesis of recombinant CYP105D1 that was translocated across the bacterial inner membrane and processed to yield authentic, heme-incorporated P450 within the periplasmic space. Cell extract and whole-cell activity studies showed that the periplasmically located CYP105D1 competently catalyzed NADH-dependent oxidation of the xenobiotic compounds benzo[a]pyrene and erythromycin, further revealing the presence in the E. coli periplasm of endogenous functional redox partners. This system offers substantial advantages for the application of P450 enzymes to whole-cell biotransformation strategies, where the ability of cells to take up substrates or discard products may be limited.

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23

Takita, Teisuke, Hiro Sakuma, Ren Ohashi, Somaye Nilouyal, Sho Nemoto, Moeka Wada, Yuya Yogo, et al. "Comparison of the stability of CYP105A1 and its variants engineered for production of active forms of vitamin D." Bioscience, Biotechnology, and Biochemistry 86, no. 4 (February 4, 2022): 444–54. http://dx.doi.org/10.1093/bbb/zbac019.

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ABSTRACT CYP105A1 from Streptomyces griseolus converts vitamin D3 to its biologically active form, 1α,25-dihydroxy vitamin D3. R73A/R84A mutation enhanced the 1α- and 25-hydroxylation activity for vitamin D3, while M239A mutation generated the 1α-hydroxylation activity for vitamin D2. In this study, the stability of six CYP105A1 enzymes, including 5 variants (R73A/R84A, M239A, R73A/R84A/M239A (=TriA), TriA/E90A, and TriA/E90D), was examined. Circular dichroism analysis revealed that M239A markedly reduces the enzyme stability. Protein fluorescence analysis disclosed that these mutations, especially M239A, induce large changes in the local conformation around Trp residues. Strong stabilizing effect of glycerol was observed. Nondenaturing PAGE analysis showed that CYP105A1 enzymes are prone to self-association. Fluorescence analysis using a hydrophobic probe 8-anilino-1-naphthalenesulfonic acid suggested that M239A mutation enhances self-association and that E90A and E90D mutations, in cooperation with M239A, accelerate self-association with little effect on the stability.

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24

Faletrov, Y. V., V. O. Maliugin, N. S. Frolova, and V. M. Shkumatov. "<i>In silico</i> evaluation of new affine interactions of methylcoumarin with cytochromes P450." Proceedings of the National Academy of Sciences of Belarus, Chemical Series 58, no. 2 (June 8, 2022): 186–90. http://dx.doi.org/10.29235/1561-8331-2022-58-2-186-190.

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4-methyl-7-methoxycoumarin (CumOMe) has been synthesized and in silico calculations demonstrated localization of methoxy group within 0.4 nm from Fe ion of hem groups for some structures of human CYP19 & CYP46 as well as CYP152 S. paucimobilis, CYP158 St. coelicolor, HMUO C. diphtheriae, XPLA R. rhodochrous, CYP199A4 Rh. palustris, CYP101A1 Ps. putida and CYP51 M. tuberculosis.

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25

Nguyen, Thi, Soo-Jin Yeom, and Chul-Ho Yun. "Production of a Human Metabolite of Atorvastatin by Bacterial CYP102A1 Peroxygenase." Applied Sciences 11, no. 2 (January 10, 2021): 603. http://dx.doi.org/10.3390/app11020603.

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Atorvastatin is a widely used statin drug that prevents cardiovascular disease and treats hyperlipidemia. The major metabolites in humans are 2-OH and 4-OH atorvastatin, which are active metabolites known to show highly inhibiting effects on 3-hydroxy-3-methylglutaryl-CoA reductase activity. Producing the hydroxylated metabolites by biocatalysts using enzymes and whole-cell biotransformation is more desirable than chemical synthesis. It is more eco-friendly and can increase the yield of desired products. In this study, we have found an enzymatic strategy of P450 enzymes for highly efficient synthesis of the 4-OH atorvastatin, which is an expensive commercial product, by using bacterial CYP102A1 peroxygenase activity with hydrogen peroxide without NADPH. We obtained a set of CYP102A1 mutants with high catalytic activity toward atorvastatin using enzyme library generation, high-throughput screening of highly active mutants, and enzymatic characterization of the mutants. In the hydrogen peroxide supported reactions, a mutant, with nine changed amino acid residues compared to a wild-type among tested mutants, showed the highest catalytic activity of atorvastatin 4-hydroxylation (1.8 min−1). This result shows that CYP102A1 can catalyze atorvastatin 4-hydroxylation by peroxide-dependent oxidation with high catalytic activity. The advantages of CYP102A1 peroxygenase activity over NADPH-supported monooxygenase activity are discussed. Taken together, we suggest that the P450 peroxygenase activity can be used to produce drugs’ metabolites for further studies of their efficacy and safety.

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Nguyen, Thi Huong Ha, Soo-Jin Yeom, and Chul-Ho Yun. "Production of a Human Metabolite of Atorvastatin by Bacterial CYP102A1 Peroxygenase." Applied Sciences 11, no. 2 (January 10, 2021): 603. http://dx.doi.org/10.3390/app11020603.

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Atorvastatin is a widely used statin drug that prevents cardiovascular disease and treats hyperlipidemia. The major metabolites in humans are 2-OH and 4-OH atorvastatin, which are active metabolites known to show highly inhibiting effects on 3-hydroxy-3-methylglutaryl-CoA reductase activity. Producing the hydroxylated metabolites by biocatalysts using enzymes and whole-cell biotransformation is more desirable than chemical synthesis. It is more eco-friendly and can increase the yield of desired products. In this study, we have found an enzymatic strategy of P450 enzymes for highly efficient synthesis of the 4-OH atorvastatin, which is an expensive commercial product, by using bacterial CYP102A1 peroxygenase activity with hydrogen peroxide without NADPH. We obtained a set of CYP102A1 mutants with high catalytic activity toward atorvastatin using enzyme library generation, high-throughput screening of highly active mutants, and enzymatic characterization of the mutants. In the hydrogen peroxide supported reactions, a mutant, with nine changed amino acid residues compared to a wild-type among tested mutants, showed the highest catalytic activity of atorvastatin 4-hydroxylation (1.8 min−1). This result shows that CYP102A1 can catalyze atorvastatin 4-hydroxylation by peroxide-dependent oxidation with high catalytic activity. The advantages of CYP102A1 peroxygenase activity over NADPH-supported monooxygenase activity are discussed. Taken together, we suggest that the P450 peroxygenase activity can be used to produce drugs’ metabolites for further studies of their efficacy and safety.

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Follmer, Alec H., Mavish Mahomed, David B. Goodin, and Thomas L. Poulos. "Substrate-Dependent Allosteric Regulation in Cytochrome P450cam (CYP101A1)." Journal of the American Chemical Society 140, no. 47 (October 30, 2018): 16222–28. http://dx.doi.org/10.1021/jacs.8b09441.

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Whitehouse, Christopher J. C., Stephen G. Bell, and Luet-Lok Wong. "P450BM3(CYP102A1): connecting the dots." Chem. Soc. Rev. 41, no. 3 (2012): 1218–60. http://dx.doi.org/10.1039/c1cs15192d.

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29

Zhang, Aili, Ting Zhang, Emma A. Hall, Sean Hutchinson, Max J. Cryle, Luet-Lok Wong, Weihong Zhou, and Stephen G. Bell. "The crystal structure of the versatile cytochrome P450 enzyme CYP109B1 from Bacillus subtilis." Molecular BioSystems 11, no. 3 (2015): 869–81. http://dx.doi.org/10.1039/c4mb00665h.

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30

Batabyal, Dipanwita, and Thomas L. Poulos. "Effect of redox partner binding on CYP101D1 conformational dynamics." Journal of Inorganic Biochemistry 183 (June 2018): 179–83. http://dx.doi.org/10.1016/j.jinorgbio.2018.02.013.

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31

Cao, Ngoc Tan, Ngoc Anh Nguyen, Chan Mi Park, Gun Su Cha, Ki Deok Park, and Chul-Ho Yun. "A Novel Statin Compound from Monacolin J Produced Using CYP102A1-Catalyzed Regioselective C-Hydroxylation." Pharmaceuticals 14, no. 10 (September 26, 2021): 981. http://dx.doi.org/10.3390/ph14100981.

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Statins inhibit the 3-hydroxy-3-methyl-glutaryl-coenzyme A reductase (HMG-CoA reductase), which is the rate-limiting enzyme in cholesterol biosynthesis. Statin therapy reduces morbidity and mortality in those who are at high risk of cardiovascular disease. Monacolin J is a statin compound, which is an intermediate in the lovastatin biosynthesis pathway, in the fungus Aspergillus terreus. It is also found in red yeast rice, which is made by culturing rice with the yeast Monascus purpureus. Monacolin J has a hydroxyl substituent at position C’-8 of monacolin L. Here, a new statin derivative from monacolin J was made through the catalysis of CYP102A1 from Bacillus megaterium. A set of CYP102A1 mutants of monacolin J hydroxylation with high catalytic activity was screened. The major hydroxylated product was C-6′a-hydroxymethyl monacolin J, whose structure was confirmed using LC–MS and NMR analysis. The C-6′a-hydroxymethyl monacolin J has never been reported before. It showed a greater ability to inhibit HMG-CoA reductase than the monacolin J substrate itself. Human liver microsomes and human CYP3A4 also showed the ability to catalyze monacolin J in producing the same product of the CYP102A1-catalyzed reaction. This result motivates a new strategy for the development of a lead for the enzymatic and chemical processes to develop statin drug candidates.

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32

Ivanov, Yuri D., Amir Taldaev, Andrey V. Lisitsa, Elena A. Ponomarenko, and Alexander I. Archakov. "Prediction of Monomeric and Dimeric Structures of CYP102A1 Using AlphaFold2 and AlphaFold Multimer and Assessment of Point Mutation Effect on the Efficiency of Intra- and Interprotein Electron Transfer." Molecules 27, no. 4 (February 18, 2022): 1386. http://dx.doi.org/10.3390/molecules27041386.

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The three-dimensional structure of monomers and homodimers of CYP102A1/WT (wild-type) proteins and their A83F and A83I mutant forms was predicted using the AlphaFold2 (AF2) and AlphaFold Multimer (AFMultimer) programs, which were compared with the rate constants of hydroxylation reactions of these enzyme forms to determine the efficiency of intra- and interprotein electron transport in the CYP102A1 hydroxylase system. The electron transfer rate constants (ket), which determine the rate of indole hydroxylation by the CYP102A1 system, were calculated based on the distances (R) between donor-acceptor prosthetic groups (PG) FAD→FMN→HEME of these proteins using factor β, which describes an exponential decay from R the speed of electron transport (ET) according to the tunnelling mechanism. It was shown that the structure of monomers in the homodimer, calculated using the AlpfaFold Multimer program, is in good agreement with the experimental structures of globular domains (HEME-, FMN-, and FAD-domains) in CYP102A1/WT obtained by X-ray structural analysis, and the structure of isolated monomers predicted in AF2 does not coincide with the structure of monomers in the homodimer, although a high level of similarity in individual domains remains. The structures of monomers and homodimers of A83F and A83I mutants were also calculated, and their structures were compared with the wild-type protein. Significant differences in the structure of all isolated monomers with respect to the structures of monomers in homodimers were also found for them, and at the same time, insignificant differences were revealed for all homodimers. Comparative analysis for CYP102A1/WT between the calculated intra- and interprotein distances FAD→FMN→HEME and the rate constants of hydroxylation in these proteins showed that the distance between prosthetic groups both in the monomer and in the dimer allows the implementation of electron transfer between PGs, which is consistent with experimental literature data about kcat. For the mutant form of monomer A83I, an increase in the distance between PGs was obtained, which can restrict electron transportation compared to WT; however, for the dimer of this protein, a decrease in the distance between PGs was observed compared to the WT form, which can lead to an increase in the electron transfer rate constant and, accordingly, kcat. For the monomer and homodimer of the A83F mutant, the calculations showed an increase in the distance between the PGs compared to the WT form, which should have led to a decrease in the electron transfer rate, but at the same time, for the homodimer, the approach of the aromatic group F262 with heme can speed up transportation for this form and, accordingly, the rate of hydroxylation.

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33

Ivanov, Yuri D., Natalia S. Bukharina, Pavel A. Frantsuzov, Tatyana O. Pleshakova, Sergey L. Kanashenko, Natalia V. Medvedeva, Viktoriya V. Argentova, Viktor G. Zgoda, Andrew W. Munro, and Alexander I. Archakov. "AFM study of cytochrome CYP102A1 oligomeric state." Soft Matter 8, no. 17 (2012): 4602. http://dx.doi.org/10.1039/c2sm07333a.

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34

Whitehouse, Christopher J C., Stephen G Bell, and Luet-Lok Wong. "Desaturation of Alkylbenzenes by Cytochrome P450BM3(CYP102A1)." Chemistry - A European Journal 14, no. 35 (December 8, 2008): 10905–8. http://dx.doi.org/10.1002/chem.200801927.

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35

Whitehouse, Christopher J. C., Nicholas H. Rees, Stephen G. Bell, and Luet-Lok Wong. "Dearomatisation of o-Xylene by P450BM3 (CYP102A1)." Chemistry - A European Journal 17, no. 24 (April 26, 2011): 6862–68. http://dx.doi.org/10.1002/chem.201002465.

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36

Whitehouse, Christopher J. C., Stephen G. Bell, and Luet-Lok Wong. "ChemInform Abstract: P450BM3(CYP102A1): Connecting the Dots." ChemInform 43, no. 17 (March 29, 2012): no. http://dx.doi.org/10.1002/chin.201217268.

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37

Batabyal, Dipanwita, Huiying Li, and Thomas L. Poulos. "Synergistic Effects of Mutations in Cytochrome P450cam Designed To Mimic CYP101D1." Biochemistry 52, no. 32 (July 31, 2013): 5396–402. http://dx.doi.org/10.1021/bi400676d.

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38

Nikolaeva, V. M., V. V. Fokina, A. A. Shutov, A. V. Kazantsev, N. I. Strizhov, and M. V. Donova. "Construction and Functional Analysis of Mycolicibacterium smegmatis Recombinant Strains Carrying the Genes of Bacillary Cytochromes CYP106A1 and CYP106A2." Biotekhnologiya 37, no. 6 (2021): 34–47. http://dx.doi.org/10.21519/0234-2758-2021-37-6-34-47.

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Mycolicibacterium smegmatis mc2155 has been genetically modified to be used as a platform for the expression of foreign cytochrome P450 monooxygenases by introducing deletions in the kshB and kstD genes that encode key stages of the enzymatic destruction of the steroid nucleus. Three sets of genetic constructs have been created for heterologous expression of the genes of cytochromes P450 CYP106A1 from Bacillus megaterium DSM319 and CYP106A2 from Bacillus megaterium ATCC13368 in Mycolicibacterium smegmatis mc2155 (ΔkshBΔkstD) cells. The recombinant plasmids contained monocistronic expression cassettes of cytochrome genes (NS31 and pNS32), or tricistronic cassettes of cytochrome genes together with cDNA copies of adrenodoxin and andrenodoxin reductase genes of the bovine adrenal cortex (pNS33 and pNS34), or monocistronic gene cassettes of chimeric cytochromes fused with the DNA sequence encoding the CYP116B2 reductase domain from the soil bacterium Rhodococcus sp. NCIMB 9784 (pNS35 and pNS36). The recombinant strains of mycolicibacteria were shown to selectively monohydroxylate androstenedione (AD) under growth conditions. The product was identified as 15-hydroxyandrostenedione (15-OH-AD) by mass spectrometry and 1H and 13C NMR spectroscopy. The maximum level of 15-OH-AD production (17.3 ± 1.5 mg/L) was observed when using the recombinant M. smegmatis mc2155 (ΔkshBΔkstD) (pNS32) strain, which expresses a single cyp106A2 gene from B. megaterium ATCC13368. Host proteins of M. smegmatis mc2155 were shown to be capable of supplying electrons to heterologous cytochromes to support their hydroxylating activity. The results are of priority character, expand the understanding of the hydroxylation of steroid compounds by bacterial cytochromes CYP106A1/A2 and are important for the creation of microbial strains producing valuable hydroxysteroids. cyp106A1, cyp106A2, cytochrome P450, heterologous expression, Bacillus megaterium, Mycolicibacterium smegmatis, 15β-hydroxylation, bioconversion, steroids This work was supported by the Russian Science Foundation (project No. 21-64-00024).

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39

Ahsan, Md, Mahesh Patil, Hyunwoo Jeon, Sihyong Sung, Taeowan Chung, and Hyungdon Yun. "Biosynthesis of Nylon 12 Monomer, ω-Aminododecanoic Acid Using Artificial Self-Sufficient P450, AlkJ and ω-TA." Catalysts 8, no. 9 (September 18, 2018): 400. http://dx.doi.org/10.3390/catal8090400.

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ω-Aminododecanoic acid is considered as one of the potential monomers of Nylon 12, a high-performance member of the bioplastic family. The biosynthesis of ω-aminododecanoic acid from renewable sources is an attractive process in the polymer industry. Here, we constructed three artificial self-sufficient P450s (ArtssP450s) using CYP153A13 from Alcanivorax borkumensis and cytochrome P450 reductase (CPR) domains of natural self-sufficient P450s (CYP102A1, CYP102A5, and 102D1). Among them, artificial self-sufficient P450 (CYP153A13BM3CPR) with CYP102A1 CPR showed the highest catalytically activity for dodecanoic acid (DDA) substrate. This form of ArtssP450 was further co-expressed with ω-TA from Silicobacter pomeroyi and AlkJ from Pseudomonas putida GPo1. This single-cell system was used for the biotransformation of dodecanoic acid (DDA) to ω-aminododecanoic acid (ω-AmDDA), wherein we could successfully biosynthesize 1.48 mM ω-AmDDA from 10 mM DDA substrate in a one-pot reaction. The productivity achieved in the present study was five times higher than that achieved in our previously reported multistep biosynthesis method (0.3 mM).

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40

Nguyen, Thi Huong Ha, Su-Min Woo, Ngoc Anh Nguyen, Gun-Su Cha, Soo-Jin Yeom, Hyung-Sik Kang, and Chul-Ho Yun. "Regioselective Hydroxylation of Naringin Dihydrochalcone to Produce Neoeriocitrin Dihydrochalcone by CYP102A1 (BM3) Mutants." Catalysts 10, no. 8 (July 23, 2020): 823. http://dx.doi.org/10.3390/catal10080823.

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Naringin dihydrochalcone (DC) is originally derived from the flavonoid naringin, which occurs naturally in citrus fruits, especially in grapefruit. It is used as an artificial sweetener with a strong antioxidant activity with potential applications in food and pharmaceutical fields. At present, enzymatic and chemical methods to make products of naringin DC by hydroxylation reactions have not been developed. Here, an enzymatic strategy for the efficient synthesis of potentially valuable products from naringin DC, a glycoside of phloretin, was developed using Bacillus megaterium CYP102A1 monooxygenase. The major product was identified to be neoeriocitrin DC by NMR and LC-MS analyses. Sixty-seven mutants of CYP102A1 were tested for hydroxylation of naringin DC to produce neoeriocitrin DC. Six mutants with high activity were selected to determine the kinetic parameters and total turnover numbers (TTNs). The kcat value of the most active mutant was 11 min−1 and its TTN was 315. The productivity of neoeriocitrin DC production increased up to 1.1 mM h−1, which corresponds to 0.65 g L−1 h−1. In this study, we achieved a regioselective hydroxylation of naringin DC to produce neoeriocitrin DC.

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41

Balaraman, Priyadarshini, and Erika Plettner. "Chemotaxis by Pseudomonas putida (ATCC 17453) towards camphor involves cytochrome P450cam (CYP101A1)." Biochimica et Biophysica Acta (BBA) - General Subjects 1863, no. 2 (February 2019): 304–12. http://dx.doi.org/10.1016/j.bbagen.2018.10.018.

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42

Cryle, Max J., and James J. De Voss. "Carbon–carbon bond cleavage by cytochrome P450BioI(CYP107H1)." Chem. Commun., no. 1 (2004): 86–87. http://dx.doi.org/10.1039/b311652b.

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43

Syntrivanis, Leonidas-Dimitrios, Luet Lok Wong, and Jeremy Robertson. "Hydroxylation of Eleuthoside Synthetic Intermediates by P450BM3 (CYP102A1)." European Journal of Organic Chemistry 2018, no. 45 (November 14, 2018): 6369–78. http://dx.doi.org/10.1002/ejoc.201801206.

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44

Maurer, Steffen C, Katja Kühnel, Leonard A Kaysser, Sabine Eiben, Rolf D Schmid, and Vlada B Urlacher. "Catalytic Hydroxylation in Biphasic Systems using CYP102A1 Mutants." Advanced Synthesis & Catalysis 347, no. 7-8 (June 2005): 1090–98. http://dx.doi.org/10.1002/adsc.200505044.

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45

Ivanov, Yu D., K. A. Malsagova, S. G. Vesnin, V. Yu Tatur, N. D. Ivanova, and V. S. Ziborov. "The Registration of a Biomaser-Like Effect in an Enzyme System with an RTM Sensor." Journal of Sensors 2019 (August 21, 2019): 1–11. http://dx.doi.org/10.1155/2019/7608512.

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The concentration dependence of a microwave frequency radiation from a solution of a functioning enzyme system (ES) (with the example of cytochrome P450 BM3 (CYP102A1) system during lauric acid (LA) hydroxylation) has been studied with a radiothermometric sensor. Registration of the radiation from the enzyme solution has been performed in the frequency range from 3.4 to 4.2 GHz at the enzyme concentrations from 10−10 М to 10−6 М. It has been demonstrated that the catalysis of LA hydroxylation in a reconstituted CYP102A1 system is accompanied by a generation of microwave radiation over the entire range of concentrations studied. It has been found that a transition from a multipulse mode (at nanomolar enzyme concentrations from 10−10М to 10−8М) to a single-pulse mode (at micromolar enzyme concentrations from 10−7М to 10−6М) is observed. This effect is discussed on the basis of assumptions considering possible realization of biomaser-like radiation in the enzyme system. The discovered concentration-based effect of the transition of an unsynchronized pulsed radiation into a synchronized one in ES can further be used in the development of novel methods of noninvasive diagnostics of diseases, in mathematical modeling of the functioning of living systems, and in the development of next-generation quantum computers.

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46

Chang, Yan-Tyng, and Gilda H. Loew. "Construction and evaluation of a three-dimensional structure of cytochrome P450choP enzyme (CYP105C1)." "Protein Engineering, Design and Selection" 9, no. 9 (1996): 755–66. http://dx.doi.org/10.1093/protein/9.9.755.

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47

Kolesanova, Ekaterina F., Sergey A. Kozin, Andrey B. Rumyantsev, Christiane Jung, Gaston Hui Bon Hoa, and Alexander I. Archakov. "Epitope Mapping of Cytochrome P450cam (CYP101)." Archives of Biochemistry and Biophysics 341, no. 2 (May 1997): 229–37. http://dx.doi.org/10.1006/abbi.1997.9934.

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48

Roh, Changhyun, Kwon-Young Choi, Bishnu Prasad Pandey, and Byung-Gee Kim. "Hydroxylation of daidzein by CYP107H1 from Bacillus subtilis 168." Journal of Molecular Catalysis B: Enzymatic 59, no. 4 (August 2009): 248–53. http://dx.doi.org/10.1016/j.molcatb.2008.07.005.

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49

Kim, Vitchan, Young-Ran Lim, Inho Lee, Jong-ha Lee, Sangjun Han, Tan-Viet Pham, Harim Kim, Rowoon Lee, Lin-Woo Kang, and Donghak Kim. "Structural insights into CYP107G1 from rapamycin-producing Streptomyces rapamycinicus." Archives of Biochemistry and Biophysics 692 (October 2020): 108544. http://dx.doi.org/10.1016/j.abb.2020.108544.

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50

Shen, Chen, Wanli Zhao, Xuming Liu, and Jihua Liu. "Enzyme-catalyzed regio-selective demethylation of papaverine by CYP105D1." Biotechnology Letters 41, no. 1 (November 21, 2018): 171–80. http://dx.doi.org/10.1007/s10529-018-2626-0.

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