Recent insights into function, structure and modification of cytochrome P450 153 a family.
CYP153A family
Fatty acid hydroxylation
Molecular modifications biosynthesis
Protein structure
Journal
Molecular biology reports
ISSN: 1573-4978
Titre abrégé: Mol Biol Rep
Pays: Netherlands
ID NLM: 0403234
Informations de publication
Date de publication:
Aug 2023
Aug 2023
Historique:
received:
25
03
2023
accepted:
26
05
2023
medline:
31
7
2023
pubmed:
25
6
2023
entrez:
24
6
2023
Statut:
ppublish
Résumé
Cytochrome P450 153 A (CYP153A) is a versatile enzyme that can catalyze a wide range of oxidation reactions on various substrates. This review provides a comprehensive overview of the current state of knowledge on CYP153A, including its classification, structure, function, and potential applications in biotechnology and pharmaceuticals. The CYP153A family encompasses many enzymes with different functions on a variety of substrates. We also discuss the structural features that are responsible for the different substrate specificities. Additionally, the enzyme has been engineered to increase its catalytic activity and modifications have been made to enhance its properties further. Despite its potential, challenges and limitations associated with studying and exploiting CYP153A remain, such as low expression levels and substrate inhibition. Nonetheless, ongoing research is exploring new ways to harness the enzyme's capabilities, particularly in synthetic biology, biocatalysis, and drug discovery, making it an exciting target for future research.
Identifiants
pubmed: 37355495
doi: 10.1007/s11033-023-08553-8
pii: 10.1007/s11033-023-08553-8
doi:
Substances chimiques
Cytochrome P-450 Enzyme System
9035-51-2
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
6955-6961Subventions
Organisme : Key Innovation Project of Qilu University of Technology (Shan-dong Academy of Sciences)
ID : no. 2022JBZ01-06
Organisme : Science Foundation of Shandong Province
ID : nos. ZR2019MC010 and ZR2017ZB0208
Organisme : Focus on Research and Development Plan in Shandong Province
ID : no. 2019JZZY011003
Informations de copyright
© 2023. The Author(s), under exclusive licence to Springer Nature B.V.
Références
Manikandan P, Nagini S (2018) Cytochrome P450 structure, function and clinical significance: a review. Curr Drug Targets 19:38–54. https://doi.org/10.2174/1389450118666170125144557
doi: 10.2174/1389450118666170125144557
pubmed: 28124606
Bordeaux M, Galarneau A, Fajula F, Drone J (2010) A regioselective Biocatalyst for Alkane activation under mild conditions. Angew Chem Int Ed 50:2075–2079. https://doi.org/10.1002/anie.201005597
doi: 10.1002/anie.201005597
Zanno A, Kwiatkowski N, Vaz A, Guardiola-Diaz HM (2005) MT FdR: a ferredoxin reductase from M. tuberculosis that couples to MT CYP51. Acta Biochim 1707:157–169. https://doi.org/10.1016/j.bbabio.2004.11.010
doi: 10.1016/j.bbabio.2004.11.010
Oliveira M, Discola KF, Alves SV, Barbosa JARG, Guimarães B (2005) Crystallization and preliminary X-ray diffraction analysis of NADPH-dependent thioredoxin reductase I from Saccharomyces cerevisiae. Acta Crystallogr A 61:387–390. https://doi.org/10.1107/S174430910500758X
doi: 10.1107/S174430910500758X
Arnold C, Konkel A, Fischer R, Schunck WH (2010) Cytochrome P450-dependent metabolism of omega-6 and omega-3 long-chain polyunsaturated fatty acids. Pharmacol Rep 62:536–547. https://doi.org/10.1016/s1734-1140(10)70311-x
doi: 10.1016/s1734-1140(10)70311-x
pubmed: 20631419
Daiber A, Shoun H, Ullrich V (2005) Nitric oxide reductase (P450nor) from Fusarium oxysporum. J Inorg Biochem 354–377. https://doi.org/10.1016/j.jinorgbio.2004.09.018
Girhard UM (2012) Cytochrome P450 monooxygenases: an update on perspectives for synthetic application. Trends Biotechnol 30:26–36. https://doi.org/10.1016/j.tibtech.2011.06.012
doi: 10.1016/j.tibtech.2011.06.012
pubmed: 21782265
Zhou R, Cong H, Zhang A, Bell SG, Zhou W, Wong LL (2011) Crystallization and preliminary X-ray analysis of CYP153C1 from Novosphingobium aromaticivorans DSM12444. ACTA CRYSTALLOGR F 67:964–967. https://doi.org/10.1107/S174430911102464X
doi: 10.1107/S174430911102464X
Dahlbäck H, Wikvall K (2019) 25-Hydroxylation of vitamin D3 by a cytochrome P-450 from rabbit liver mitochondria. Biochem J 252:207–213. https://doi.org/10.1042/bj2520207
doi: 10.1042/bj2520207
Yan Y, Wu J, Hu G, Gao C, Guo L, Chen X, Liu L, Song W (2022) Current state and future perspectives of cytochrome P450 enzymes for C-H and C = C oxygenation. Synth Syst 7:13. https://doi.org/10.1016/j.synbio.2022.04.009
doi: 10.1016/j.synbio.2022.04.009
Funhoff EG, Bauer U, Garcia-Rubio I, Witholt B, Van Beilen JB (2006) CYP153A6, a Soluble P450 Oxygenase Catalyzing Terminal-Alkane Hydroxylation. J Bacteriol 188:5220–5227. https://doi.org/10.1128/JB.00286-06
doi: 10.1128/JB.00286-06
pubmed: 16816194
pmcid: 1539980
Funhoff EG, Salzmann J, Bauer U, Witholt B, Beilen J (2007) Hydroxylation and epoxidation reactions catalyzed by CYP153 enzymes. Enzyme Microb Technol 40:806–812. https://doi.org/10.1016/j.enzmictec.2006.06.014
doi: 10.1016/j.enzmictec.2006.06.014
Matías A, Musumeci ML, Daniela V (2017) Prospecting biotechnologically-relevant Monooxygenases from Cold Sediment Metagenomes: an in Silico Approach. Mar Drugs 15:114–132. https://doi.org/10.3390/md15040114
doi: 10.3390/md15040114
Chulwoo P, Woojun P (2018) Survival and energy producing strategies of Alkane Degraders under Extreme Conditions and their biotechnological potential. FRONT MICROBIOL 9:1081. https://doi.org/10.3389/fmicb.2018.01081
doi: 10.3389/fmicb.2018.01081
Hoffmann SM, Danesh-Azari H, Spandolf C, Weissenborn MJ, Grogan G, Hauer B (2016) Structure-guided redesign of CYP153AM.aq for the Improved Terminal Hydroxylation of fatty acids. ChemCatChem 8:3176–3176. https://doi.org/10.1002/cctc.201601209
doi: 10.1002/cctc.201601209
Thomas M, Hans-Heinrich F, Otmar A, Ulrich H (2001) Molecular characterization of the 56-kDa CYP153 from Acinetobacter sp. EB104. Biochem Biophys Res Commun 286:652–658. https://doi.org/10.1006/bbrc.2001.5449
doi: 10.1006/bbrc.2001.5449
Fujita N, Sumisa F, Shindo K, Kabumoto H, Arisawa A, Ikenaga H, Misawa N (2009) Comparison of two vectors for functional expression of a bacterial cytochrome P450 gene in Escherichia coli using CYP153 genes. Biosci Biotechnol Biochem 73:1825–1830. https://doi.org/10.1271/bbb.90199
doi: 10.1271/bbb.90199
pubmed: 19661686
Yong N, Liang JL, Fang H, Tang Y (2014) Characterization of a CYP153 alkane hydroxylase gene in a Gram-positive Dietzia sp. DQ12-45-1b and its “team role” with alkW1 in alkane degradation. Appl Microbiol Biotechnol 98:163–173. https://doi.org/10.1007/s00253-013-4821-1
doi: 10.1007/s00253-013-4821-1
Koch DJ, Chen MM, Beilen JV, Arnold FH (2009) In vivo evolution of butane oxidation by terminal alkane hydroxylases AlkB and CYP153A6. AEM 75:337–344. https://doi.org/10.1128/AEM.01758-08
doi: 10.1128/AEM.01758-08
Poulos TL, Meharenna YT (2007) Structures of P450 proteins and their molecular phylogeny. Met Ions Life Sci 3:57–96. https://doi.org/10.1002/9780470028155.ch3
doi: 10.1002/9780470028155.ch3
Demet S, Michael W, Florian W, Jürgen P (2010) Prediction and analysis of the modular structure of cytochrome P450 monooxygenases. BMC Struct Biol 10:34. https://doi.org/10.1186/1472-6807-10-34
doi: 10.1186/1472-6807-10-34
Poulos TL, Follmer AH (2022) Updating the paradigm: Redox Partner binding and Conformational Dynamics in Cytochromes P450. Acc Chem Res. https://doi.org/10.1021/acs.accounts.1c00632
doi: 10.1021/acs.accounts.1c00632
pubmed: 34965086
Xu L, Du Y (2018) Rational and semi-rational engineering of cytochrome P450s for biotechnological applications. Synth Syst 3:1–8. https://doi.org/10.1007/978-1-4899-6790-9
doi: 10.1007/978-1-4899-6790-9
Pham SQ, Pompidor G, Liu J, Li XD, Li Z (2012) Evolving P450pyr hydroxylase for highly enantioselective hydroxylation at non-activated carbon atom. ChemComm 48:4618–4620. https://doi.org/10.1039/c2cc30779k
doi: 10.1039/c2cc30779k
Li Z, Yang Y, Liu J (2014) Engineering of P450pyr hydroxylase for the highly regio- and Enantioselective Subterminal Hydroxylation of Alkane. Angewandte Chemie
Kirton SB, Baxter CA, Sutcliffe MJ (2019) Comparative modelling of cytochromes P450. Adv Drug Deliv Rev 54:385–406. https://doi.org/10.1016/S0169-409X(02)00010-8
doi: 10.1016/S0169-409X(02)00010-8
Fiorentini F, Hatzl AM, Schmidt S, Savino S, Glieder A, Mattevi A (2018) The Extreme Structural plasticity in the CYP153 subfamily of P450s directs development of designer hydroxylases. Biochemistry 57:1–30. https://doi.org/10.1021/acs.biochem.8b01052
doi: 10.1021/acs.biochem.8b01052
Gao L, Zhao J, Lv Y, Dong Y, Wang J, Wang Y (2020) Crystal structure of a cytochrome P450 CYP153A variant from Mycobacterium sp. WY-01 with high activity towards medium-chain fatty acids. Int J Biol Macromol 147:711–718
Scheps D, Malca SH, Richter SM, Marisch K, Nestl BM, Hauer B (2013) Synthesis of ω-hydroxy dodecanoic acid based on an engineered CYP153A fusion construct. Microb Biotechnol 6:694–707. https://doi.org/10.1111/1751-7915.12073
doi: 10.1111/1751-7915.12073
pubmed: 23941649
pmcid: 3815936
Nebel BA, Scheps D, Malca SH, Nestl BM, Breuer M, Wagner H-G, Breitscheidel B, Kratz D, Hauer B (2014) Biooxidation of n-butane to 1-butanol by engineered P450 monooxygenase under increased pressure. J Biotechno 191:86–92. https://doi.org/10.1016/j.jbiotec.2014.08.022
doi: 10.1016/j.jbiotec.2014.08.022
Seifert A, SGrohmann, KKriening, SUrlacher VBLaschat, SPleiss J (2009) Rational design of a minimal and highly enriched CYP102A1 mutant Library with Improved Regio-, stereo- and chemoselectivity. ChemBioChem 10:1426–1426. https://doi.org/10.1002/cbic.200800799
doi: 10.1002/cbic.200800799
Sandra N, Łukasz G, Jürgen P, bernhard H (2016) Semirational Protein Engineering of CYP153AM.aq.-CPRBM3 for Efficient Terminal Hydroxylation of Short- to Long-Chain Fatty Acids. Chembiochem: 1–10. https://doi.org/10.1002/cbic.201600207
Jung E, Park B, Yoo G, Kim HW, J., and, Choi K, Y (2018) Semi-rational engineering of CYP153A35 to enhance ω-hydroxylation activity toward palmitic acid. Appl Microbiol Biotechnol 102:269–277. https://doi.org/10.1007/s00253-017-8584-y
doi: 10.1007/s00253-017-8584-y
pubmed: 29124283
Duan Y, Ba L, Gao J, Gao X, Zhu D, Jong RD, Mink D, Kaluzna I, Lin Z (2016) Semi-rational engineering of cytochrome CYP153A from Marinobacter aquaeolei for improved ω-hydroxylation activity towards oleic acid. Appl Microbiol Biotechnol 100:1–10. https://doi.org/10.1007/s00253-016-7634-1
doi: 10.1007/s00253-016-7634-1
Ji Y, Mao G, Wang Y, Bartlam M (2013) Structural insights into diversity and n-alkane biodegradation mechanisms of alkane hydroxylases. Front Microbiol 4:1–13. https://doi.org/10.3389/fmicb.2013.00058
doi: 10.3389/fmicb.2013.00058
Wang L, Wang W, Lai Q, Shao Z (2010) Gene diversity of CYP153A and AlkB alkane hydroxylases in oil-degrading bacteria isolated from the Atlantic Ocean. Environ Microbiol 12:1230–1242. https://doi.org/10.1111/j.1462-2920.2010.02165.x
doi: 10.1111/j.1462-2920.2010.02165.x
pubmed: 20148932
Ahsan M, Patil M, Jeon H, Sung S, Chung T, Yun H (2018) Biosynthesis of Nylon 12 Monomer, ω-Aminododecanoic acid using Artificial self-sufficient P450, AlkJ and ω-TA. Catalysts 8:1–13. https://doi.org/10.3390/catal8090400
doi: 10.3390/catal8090400
Fasan R (2012) Tuning P450 enzymes as oxidation catalysts. ACS Catal 2:647–666. https://doi.org/10.1021/cs300001x
doi: 10.1021/cs300001x
Lundemo M, Notonier S, Striedner G, Hauer B, Woodley J (2016) Process limitations of a whole-cell P450 catalyzed reaction using a CYP153A-CPR fusion construct expressed in Escherichia coli. Appl Microbiol Biotechnol 100:1197–1208. https://doi.org/10.1007/s00253-015-6999-x
doi: 10.1007/s00253-015-6999-x
pubmed: 26432459
Cornelissen S, Julsing MK, Volmer J, Riechert O, Schmid A, Bühler B (2013) Whole-cell-based CYP153A6-catalyzed (S)-limonene hydroxylation efficiency depends on host background and profits from monoterpene uptake via AlkL. Biotechnol Bioeng 110:1282–1292. https://doi.org/10.1002/bit.24801
doi: 10.1002/bit.24801
pubmed: 23239244
Malca SH, Scheps D, Kuehnel L, Venegas-Venegas E, Seifert A, Nestl BM, Hauer B (2012) Bacterial CYP153A monooxygenases for the synthesis of omega-hydroxylated fatty acids. ChemComm 48:5115–5117. https://doi.org/10.1039/c2cc18103g
doi: 10.1039/c2cc18103g