메뉴 건너뛰기




Volumn 80, Issue 4, 2014, Pages 1371-1379

Regio- and stereospecific hydroxylation of various steroids at the 16α position of the D ring by the Streptomyces griseus cytochrome P450 CYP154C3

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME P450 MONOOXYGENASES; DEHYDROEPIANDROSTERONE; EQUILIBRIUM DISSOCIATION CONSTANT; ESCHERICHIA COLI CELLS; HIGH RESOLUTION MASS SPECTROMETRY; OXYFUNCTIONALIZATION; STEREOSPECIFIC MANNER; STREPTOMYCES GRISEUS;

EID: 84893417195     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.03504-13     Document Type: Article
Times cited : (46)

References (40)
  • 1
    • 78649449149 scopus 로고    scopus 로고
    • Progress in tracing the evolutionary paths of cytochrome P450
    • Nelson DR. 2011. Progress in tracing the evolutionary paths of cytochrome P450. Biochim. Biophys. Acta 1814:14-18. http://dx.doi.org/10.1016/j.bbapap.2010.08.008.
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 14-18
    • Nelson, D.R.1
  • 5
    • 84879053350 scopus 로고    scopus 로고
    • Cytochromes P450: roles in diseases
    • Pikuleva IA, Waterman MR. 2013. Cytochromes P450: roles in diseases. J. Biol. Chem. 288:17091-17098. http://dx.doi.org/10.1074/jbc.R112.431916.
    • (2013) J. Biol. Chem , vol.288 , pp. 17091-17098
    • Pikuleva, I.A.1    Waterman, M.R.2
  • 6
    • 77952516353 scopus 로고    scopus 로고
    • Diversification of P450 genes during land plant evolution
    • Mizutani M, Ohta D. 2010. Diversification of P450 genes during land plant evolution. Annu. Rev. Plant Biol. 61:291-314. http://dx.doi.org/10.1146/annurev-arplant-042809-112305.
    • (2010) Annu. Rev. Plant Biol , vol.61 , pp. 291-314
    • Mizutani, M.1    Ohta, D.2
  • 7
    • 84868318849 scopus 로고    scopus 로고
    • Diversity of P450 enzymes in the biosynthesis of natural products
    • Podust LM, Sherman DH. 2012. Diversity of P450 enzymes in the biosynthesis of natural products. Nat. Prod. Rep. 29:1251-1266. http://dx.doi.org/10.1039/c2np20020a.
    • (2012) Nat. Prod. Rep , vol.29 , pp. 1251-1266
    • Podust, L.M.1    Sherman, D.H.2
  • 10
    • 84894298829 scopus 로고    scopus 로고
    • Pharmaceutically active secondary metabolites of marine actinobacteria
    • S0944-5013(13)00125-0
    • Manivasagan P, Venkatesan J, Sivakumar K, Kim SK. 2013. Pharmaceutically active secondary metabolites of marine actinobacteria. Microbiol. Res. 2013:S0944-5013(13)00125-0. http://dx.doi.org/10.1016/j.micres.2013.07.014.
    • (2013) Microbiol. Res , vol.2013
    • Manivasagan, P.1    Venkatesan, J.2    Sivakumar, K.3    Kim, S.K.4
  • 11
    • 84888012588 scopus 로고    scopus 로고
    • Production of hydroxy fatty acids by microbial fatty acid-hydroxylation enzymes
    • Kyoung-Rok K, Deok-kun O. 2013. Production of hydroxy fatty acids by microbial fatty acid-hydroxylation enzymes. Biotechnol. Adv. 31:1473-1485. http://dx.doi.org/10.1016/j.biotechadv.2013.07.004.
    • (2013) Biotechnol. Adv , vol.31 , pp. 1473-1485
    • Kyoung-Rok, K.1    Deok-kun, O.2
  • 14
    • 0021747522 scopus 로고
    • Microbial transformation of testosterone by Aspergillus fumigatus
    • Mahato SB, Mukherjee A. 1984. Microbial transformation of testosterone by Aspergillus fumigatus. J. Steroid Biochem. 21:341-342. http://dx.doi.org/10.1016/0022-4731(84)90289-9.
    • (1984) J. Steroid Biochem , vol.21 , pp. 341-342
    • Mahato, S.B.1    Mukherjee, A.2
  • 15
    • 0024637456 scopus 로고
    • Microbial transformation of steroids-II. Transformations of progesterone, testosterone and androstenedione by Phycomyces blakesleeanus
    • Smith KE, Latif S, Kirk DN. 1989. Microbial transformation of steroids-II. Transformations of progesterone, testosterone and androstenedione by Phycomyces blakesleeanus. J. Steroid Biochem. 32:445-451.
    • (1989) J. Steroid Biochem , vol.32 , pp. 445-451
    • Smith, K.E.1    Latif, S.2    Kirk, D.N.3
  • 16
    • 0025093424 scopus 로고
    • Microbial transformations of steroids-VI. Transformation of testosterone and androsterone by Botryosphaerica obtusa
    • Smith KE, Latif S, Kirk DN. 1990. Microbial transformations of steroids-VI. Transformation of testosterone and androsterone by Botryosphaerica obtusa. J. Steroid Biochem. 35:115-120.
    • (1990) J. Steroid Biochem , vol.35 , pp. 115-120
    • Smith, K.E.1    Latif, S.2    Kirk, D.N.3
  • 17
    • 0031727776 scopus 로고    scopus 로고
    • Biotransformation XLV: transformations of 4-ene-3-oxo steroids in Fusarium culmorum culture
    • Kolek T, Swizdor A. 1998. Biotransformation XLV: transformations of 4-ene-3-oxo steroids in Fusarium culmorum culture. J. Steroid Biochem. Mol. Biol. 67:63-69. http://dx.doi.org/10.1016/S0960-0760(98)00073-9.
    • (1998) J. Steroid Biochem. Mol. Biol , vol.67 , pp. 63-69
    • Kolek, T.1    Swizdor, A.2
  • 18
    • 0037809271 scopus 로고    scopus 로고
    • The 1.92-Å structure of Streptomyces coelicolor A3(2) CYP154C1: a new monooxygenase that functionalizes macrolide ring systems
    • Podust LM, Kim Y, Arase M, Neely BA, Beck BJ, Bach H, Sherman DH, Lamb DC, Kelly SL, Waterman MR. 2003. The 1.92-Å structure of Streptomyces coelicolor A3(2) CYP154C1: a new monooxygenase that functionalizes macrolide ring systems. J. Biol. Chem. 278:12214-12221. http://dx.doi.org/10.1074/jbc.M212210200.
    • (2003) J. Biol. Chem , vol.278 , pp. 12214-12221
    • Podust, L.M.1    Kim, Y.2    Arase, M.3    Neely, B.A.4    Beck, B.J.5    Bach, H.6    Sherman, D.H.7    Lamb, D.C.8    Kelly, S.L.9    Waterman, M.R.10
  • 19
    • 0346733324 scopus 로고    scopus 로고
    • Comparison of the 1.85 Å structure of CYP154A1 from Streptomyces coelicolor A3(2) with the closely related CYP154C1 and CYPs from antibiotic biosynthetic pathways
    • Podust LM, Bach H, Kim Y, Lamb DC, Arase M, Sherman DH, Kelly SL, Waterman MR. 2004. Comparison of the 1.85 Å structure of CYP154A1 from Streptomyces coelicolor A3(2) with the closely related CYP154C1 and CYPs from antibiotic biosynthetic pathways. Protein Sci. 13:255-268. http://dx.doi.org/10.1110/ps.03384804.
    • (2004) Protein Sci , vol.13 , pp. 255-268
    • Podust, L.M.1    Bach, H.2    Kim, Y.3    Lamb, D.C.4    Arase, M.5    Sherman, D.H.6    Kelly, S.L.7    Waterman, M.R.8
  • 20
    • 78049407027 scopus 로고    scopus 로고
    • Cyclization of a cellular dipentaenone by Streptomyces coelicolor cytochrome P450 154A1 without oxidation/reduction
    • Cheng Q, Lamb DC, Kelly SL, Lei L, Guengerich FP. 2010. Cyclization of a cellular dipentaenone by Streptomyces coelicolor cytochrome P450 154A1 without oxidation/reduction. J. Am. Chem. Soc. 132:15173-15175. http://dx.doi.org/10.1021/ja107801v.
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 15173-15175
    • Cheng, Q.1    Lamb, D.C.2    Kelly, S.L.3    Lei, L.4    Guengerich, F.P.5
  • 21
    • 79952572516 scopus 로고    scopus 로고
    • Characterization of cytochrome P450 monooxygenase CYP154H1 from the thermophilic soil bacterium Thermobifida fusca
    • Schallmey A, den Besten G, Teune IG, Kembaren RF, Janssen DB. 2011. Characterization of cytochrome P450 monooxygenase CYP154H1 from the thermophilic soil bacterium Thermobifida fusca. Appl. Microbiol. Biotechnol. 89:1475-1485. http://dx.doi.org/10.1007/s00253-010-2965-9.
    • (2011) Appl. Microbiol. Biotechnol , vol.89 , pp. 1475-1485
    • Schallmey, A.1    den Besten, G.2    Teune, I.G.3    Kembaren, R.F.4    Janssen, D.B.5
  • 22
    • 84885567349 scopus 로고    scopus 로고
    • Selective steroid oxyfunctionalisation by CYP154C5, a bacterial cytochrome P450
    • Bracco P, Janssen DB, Schallmey A. 2013. Selective steroid oxyfunctionalisation by CYP154C5, a bacterial cytochrome P450. Microb. Cell Fact. 12:95. http://dx.doi.org/10.1186/1475-2859-12-95.
    • (2013) Microb. Cell Fact , vol.12 , pp. 95
    • Bracco, P.1    Janssen, D.B.2    Schallmey, A.3
  • 23
    • 0343983880 scopus 로고
    • Oxidation of steroids by microorganisms. IV. 16α-Hydroxylation of 9α-fluorohydrocortisone and 9α-fluoroprednisolone by Streptomyces roseochromogenus
    • Thoma RW, Fried J, Bonanno S, Grabowich P. 1957. Oxidation of steroids by microorganisms. IV. 16α-Hydroxylation of 9α-fluorohydrocortisone and 9α-fluoroprednisolone by Streptomyces roseochromogenus. J. Am. Chem. Soc. 79:4818.
    • (1957) J. Am. Chem. Soc , vol.79 , pp. 4818
    • Thoma, R.W.1    Fried, J.2    Bonanno, S.3    Grabowich, P.4
  • 24
    • 0033461168 scopus 로고    scopus 로고
    • Microbial transformations of steroids-X. Progesterone transformation by Streptomyces roseochromogenes- purification and characterisation of the 16α-hydroxylase system
    • Berrie JR, Williams RAD, Smith KE. 1999. Microbial transformations of steroids-XI. Progesterone transformation by Streptomyces roseochromogenes- purification and characterisation of the 16α-hydroxylase system. J. Steroid Biochem. 71:153-165.
    • (1999) J. Steroid Biochem , vol.71 , pp. 153-165
    • Berrie, J.R.1    Williams, R.A.D.2    Smith, K.E.3
  • 25
    • 84889571903 scopus 로고    scopus 로고
    • Cluster screening: an effective approach for probing the substrate space of uncharacterized cytochrome P450s
    • [Epub ahead of print.]
    • Von BC, Le-Huu P, Urlacher VB. 2013. Cluster screening: an effective approach for probing the substrate space of uncharacterized cytochrome P450s. ChemBioChem [Epub ahead of print.] http://dx.doi.org/10.1002/cbic.201300271.
    • (2013) Chem Bio Chem
    • Von, B.C.1    Le-Huu, P.2    Urlacher, V.B.3
  • 27
    • 28044436696 scopus 로고    scopus 로고
    • Biosynthesis of hexahydroxyperylenequinone melanin via oxidative aryl coupling by cytochrome P-450 in Streptomyces griseus
    • Funa N, Funabashi M, Ohnishi Y, Horinouchi S. 2005. Biosynthesis of hexahydroxyperylenequinone melanin via oxidative aryl coupling by cytochrome P-450 in Streptomyces griseus. J. Bacteriol. 187:8149-8155. http://dx.doi.org/10.1128/JB.187.23.8149-8155.2005.
    • (2005) J. Bacteriol , vol.187 , pp. 8149-8155
    • Funa, N.1    Funabashi, M.2    Ohnishi, Y.3    Horinouchi, S.4
  • 29
    • 33745966649 scopus 로고    scopus 로고
    • Functional expression system for cytochrome P450 genes using the reductase domain of self-sufficient P450RhF from Rhodococcus sp. NCIMB 9784
    • Nodate M, Kubota M, Misawa N. 2006. Functional expression system for cytochrome P450 genes using the reductase domain of self-sufficient P450RhF from Rhodococcus sp. NCIMB 9784. Appl. Microbiol. Biotechnol. 71:455-462. http://dx.doi.org/10.1007/s00253-005-0147-y.
    • (2006) Appl. Microbiol. Biotechnol , vol.71 , pp. 455-462
    • Nodate, M.1    Kubota, M.2    Misawa, N.3
  • 30
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura T, Sato R. 1964. The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J. Biol. Chem. 239: 2370-2378.
    • (1964) J. Biol. Chem , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 31
    • 84894328324 scopus 로고    scopus 로고
    • A new cytochrome P450 system from Bacillus megaterium DSM319 for the hydroxylation of 11-keto-β-boswellic acid (KBA)
    • [Epub ahead of print.]
    • Brill E, Hannemann F, Zapp J, Brüning G, Jauch J, Bernhardt R. 2013. A new cytochrome P450 system from Bacillus megaterium DSM319 for the hydroxylation of 11-keto-β-boswellic acid (KBA). Appl. Microbiol. Biotechnol. [Epub ahead of print.] http://dx.doi.org/10.1007/s00253-013-5029-0.
    • (2013) Appl. Microbiol. Biotechnol
    • Brill, E.1    Hannemann, F.2    Zapp, J.3    Brüning, G.4    Jauch, J.5    Bernhardt, R.6
  • 32
    • 0017794351 scopus 로고
    • Measurement of substrate and inhibitor binding to microsomal cytochrome P-450 by optical-difference spectroscopy
    • Jefcoate CR. 1978. Measurement of substrate and inhibitor binding to microsomal cytochrome P-450 by optical-difference spectroscopy. Methods Enzymol. 52:258-279. http://dx.doi.org/10.1016/S0076-6879(78)52029-6.
    • (1978) Methods Enzymol , vol.52 , pp. 258-279
    • Jefcoate, C.R.1
  • 33
    • 84864583572 scopus 로고    scopus 로고
    • Biocatalytic synthesis of flavones and hydroxyl-small molecules by recombinant Escherichia coli cells expressing the cyanobacterial CYP110E1 gene
    • Makino T, Otomatsu T, Shindo K, Kitamura E, Sandmann G, Harada H, Misawa N. 2012. Biocatalytic synthesis of flavones and hydroxyl-small molecules by recombinant Escherichia coli cells expressing the cyanobacterial CYP110E1 gene. Microb. Cell Fact. 11:95. http://dx.doi.org/10.1186/1475-2859-11-95.
    • (2012) Microb. Cell Fact , vol.11 , pp. 95
    • Makino, T.1    Otomatsu, T.2    Shindo, K.3    Kitamura, E.4    Sandmann, G.5    Harada, H.6    Misawa, N.7
  • 34
    • 69949189242 scopus 로고    scopus 로고
    • Comparison of two vectors for functional expression of a bacterial cytochrome P450 gene in Escherichia coli using CYP153 genes
    • 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. http://dx.doi.org/10.1271/bbb.90199.
    • (2009) Biosci. Biotechnol. Biochem , vol.73 , pp. 1825-1830
    • Fujita, N.1    Sumisa, F.2    Shindo, K.3    Kabumoto, H.4    Arisawa, A.5    Ikenaga, H.6    Misawa, N.7
  • 35
    • 33749161882 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a self-sufficient cytochrome P450 monooxygenase from Rhodococcus ruber DSM 44319
    • Liu L, Schmid RD, Urlacher VB. 2006. Cloning, expression, and characterization of a self-sufficient cytochrome P450 monooxygenase from Rhodococcus ruber DSM 44319. Appl. Microbiol. Biotechnol. 72:876-882. http://dx.doi.org/10.1007/s00253-006-0355-0.
    • (2006) Appl. Microbiol. Biotechnol , vol.72 , pp. 876-882
    • Liu, L.1    Schmid, R.D.2    Urlacher, V.B.3
  • 36
    • 34547118130 scopus 로고    scopus 로고
    • Electron transport pathway for a Streptomyces cytochrome P450: cytochrome P450 105D5-catalyzed fatty acid hydroxylation in Streptomyces coelicolor A3(2)
    • Chun YJ, Shimada T, Sanchez-Ponce R, Martin MV, Lei L, Zhao B, Kelly SL, Waterman MR, Lamb DC, Guengerich FP. 2007. Electron transport pathway for a Streptomyces cytochrome P450: cytochrome P450 105D5-catalyzed fatty acid hydroxylation in Streptomyces coelicolor A3(2). J. Biol. Chem. 282:17486-17500. http://dx.doi.org/10.1074/jbc.M700863200.
    • (2007) J. Biol. Chem , vol.282 , pp. 17486-17500
    • Chun, Y.J.1    Shimada, T.2    Sanchez-Ponce, R.3    Martin, M.V.4    Lei, L.5    Zhao, B.6    Kelly, S.L.7    Waterman, M.R.8    Lamb, D.C.9    Guengerich, F.P.10
  • 38
    • 79251633167 scopus 로고    scopus 로고
    • Pentalenic acid is a shunt metabolite in the biosynthesis of the pentalenolactone family of metabolites: hydroxylation of 1-deoxypentalenic acid mediated by CYP105D7 (SAV_7469) of Streptomyces avermitilis
    • Takamatsu S, Xu LH, Fushinobu S, Shoun H, Komatsu M, Cane DE, Ikeda H. 2011. Pentalenic acid is a shunt metabolite in the biosynthesis of the pentalenolactone family of metabolites: hydroxylation of 1-deoxypentalenic acid mediated by CYP105D7 (SAV_7469) of Streptomyces avermitilis. J. Antibiot. 64:65-71. http://dx.doi.org/10.1038/ja.2010.135.
    • (2011) J. Antibiot , vol.64 , pp. 65-71
    • Takamatsu, S.1    Xu, L.H.2    Fushinobu, S.3    Shoun, H.4    Komatsu, M.5    Cane, D.E.6    Ikeda, H.7
  • 39
    • 79952440752 scopus 로고    scopus 로고
    • A new cytochrome P450 belonging to the 107L subfamily is responsible for the efficient hydroxylation of the drug terfenadine by Streptomyces platensis
    • Lombard M, Salard I, Sari MA, Mansuy D, Buisson D. 2011. A new cytochrome P450 belonging to the 107L subfamily is responsible for the efficient hydroxylation of the drug terfenadine by Streptomyces platensis. Arch. Biochem. Biophys. 508:54-63. http://dx.doi.org/10.1016/j.abb.2011.01.008.
    • (2011) Arch. Biochem. Biophys , vol.508 , pp. 54-63
    • Lombard, M.1    Salard, I.2    Sari, M.A.3    Mansuy, D.4    Buisson, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.