메뉴 건너뛰기




Volumn 95, Issue 1, 2012, Pages 123-133

CYP264B1 from Sorangium cellulosum so ce56: A fascinating norisoprenoid and sesquiterpene hydroxylase

Author keywords

CYP264B1; Cytochrome P450; Ionone; Nootkatone; Sorangium cellulosum So ce56; Terpenoid

Indexed keywords

CYP264B1; CYTOCHROME P450; IONONE; NOOTKATONE; SORANGIUM; TERPENOIDS;

EID: 84862019716     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-011-3727-z     Document Type: Article
Times cited : (31)

References (57)
  • 1
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • DOI 10.1093/bioinformatics/bti770
    • Arnold K, Bordoli L, Kopp J, Schwede T (2006) The SWISS-MODEL Workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22:195-201 (Pubitemid 43205406)
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 2
    • 77149159443 scopus 로고    scopus 로고
    • A cytochrome P450 class I electron transfer system from Novosphingobium aromaticivorans
    • Bell SG, Dale A, Rees NH, Wong LL (2009) A cytochrome P450 class I electron transfer system from Novosphingobium aromaticivorans. Appl Microbiol Biotechnol 86:163-175
    • (2009) Appl Microbiol Biotechnol , vol.86 , pp. 163-175
    • Bell, S.G.1    Dale, A.2    Rees, N.H.3    Wong, L.L.4
  • 3
    • 33744520321 scopus 로고    scopus 로고
    • Cytochromes P450 as versatile biocatalysts
    • Bernhardt R (2006) Cytochromes P450 as versatile biocatalysts. J Biotechnol 124:128-145
    • (2006) J Biotechnol , vol.124 , pp. 128-145
    • Bernhardt, R.1
  • 4
    • 70349153815 scopus 로고    scopus 로고
    • Bio-oxidation of terpenes: An approach for the flavor industry
    • Bicas JL, Dionisio AP, Pastore GM (2009) Bio-oxidation of terpenes: an approach for the flavor industry. Chem Rev 109:4518-4531
    • (2009) Chem Rev , vol.109 , pp. 4518-4531
    • Bicas, J.L.1    Dionisio, A.P.2    Pastore, G.M.3
  • 6
    • 0036208861 scopus 로고    scopus 로고
    • Optically ative inones and derivatives: Preparation and olfactory properties
    • Brenna E, Fuganti C, Serra S, Kraft P (2002) Optically ative inones and derivatives: preparation and olfactory properties. Eur J Org Chem 2002:967-978
    • (2002) Eur J Org Chem , vol.2002 , pp. 967-978
    • Brenna, E.1    Fuganti, C.2    Serra, S.3    Kraft, P.4
  • 8
    • 24144496039 scopus 로고    scopus 로고
    • Efficient terpene hydroxylation catalysts based upon P450 enzymes derived from actinomycetes
    • DOI 10.1039/b506159h
    • Celik A, Flitsch SL, Turner NJ (2005) Efficient terpene hydroxylation catalysts based upon P450 enzymes derived from actinomycetes. Org Biomol Chem 3:2930-2934 (Pubitemid 41239069)
    • (2005) Organic and Biomolecular Chemistry , vol.3 , Issue.16 , pp. 2930-2934
    • Celik, A.1    Flitsch, S.L.2    Turner, N.J.3
  • 9
    • 80052489875 scopus 로고    scopus 로고
    • Insecticidal compounds from the essential oil of Chinese medicinal herb Atractylodes chinensis
    • doi:10.1002/ps.2180
    • Chu SS, Jiang GH, Liu ZL (2011) Insecticidal compounds from the essential oil of Chinese medicinal herb Atractylodes chinensis. Pest Manag Sci. doi:10.1002/ps.2180
    • (2011) Pest Manag Sci
    • Chu, S.S.1    Jiang, G.H.2    Liu, Z.L.3
  • 10
    • 33344479001 scopus 로고    scopus 로고
    • A novel approach to the efficient oxygenation of hydrocarbons under mild conditions. Superior oxo transfer selectivity using dioxiranes
    • Curci R, D'Accolti L, Fusco C (2006) A novel approach to the efficient oxygenation of hydrocarbons under mild conditions. Superior oxo transfer selectivity using dioxiranes. Acc Chem Res 39:1-9
    • (2006) Acc Chem Res , vol.39 , pp. 1-9
    • Curci, R.1    D'Accolti, L.2    Fusco, C.3
  • 12
    • 34247271338 scopus 로고    scopus 로고
    • Pharmaceutical and therapeutic potentials of essential oils and their individual volatile constituents: A review
    • Edris AE (2007) Pharmaceutical and therapeutic potentials of essential oils and their individual volatile constituents: a review. Phytother Res 21:308-323
    • (2007) Phytother Res , vol.21 , pp. 308-323
    • Edris, A.E.1
  • 13
    • 70350417516 scopus 로고    scopus 로고
    • Genome mining in Sorangium cellulosum so ce56: Identification and characterization of the homologous electron transfer proteins of a myxobacterial cytochrome P450
    • Ewen KM, Hannemann F, Khatri Y, Perlova O, Kappl R, Krug D, Hüttermann J, Müller R, Bernhardt R (2009) Genome mining in Sorangium cellulosum So ce56: identification and characterization of the homologous electron transfer proteins of a myxobacterial cytochrome P450. J Biol Chem 284:28590-28598
    • (2009) J Biol Chem , vol.284 , pp. 28590-28598
    • Ewen, K.M.1    Hannemann, F.2    Khatri, Y.3    Perlova, O.4    Kappl, R.5    Krug, D.6    Hüttermann, J.7    Müller, R.8    Bernhardt, R.9
  • 15
    • 33751310527 scopus 로고    scopus 로고
    • Natural sesquiterpenoids
    • Fraga BM (2006) Natural sesquiterpenoids. Nat Prod Rep 23:943-972
    • (2006) Nat Prod Rep , vol.23 , pp. 943-972
    • Fraga, B.M.1
  • 16
    • 27744468958 scopus 로고    scopus 로고
    • Biotransformation of citrus aromatics nootkatone and valencene by microorganisms
    • DOI 10.1248/cpb.53.1423
    • Furusawa M, Hashimoto T, Noma Y, Asakawa Y (2005) Biotransformation of citrus aromatics nootkatone and valencene by microorganisms. Chem Pharm Bull (Tokyo) 53:1423-1429 (Pubitemid 41634210)
    • (2005) Chemical and Pharmaceutical Bulletin , vol.53 , Issue.11 , pp. 1423-1429
    • Furusawa, M.1    Hashimoto, T.2    Noma, Y.3    Asakawa, Y.4
  • 17
    • 84861999999 scopus 로고    scopus 로고
    • Sphaeranthus indicus Linn.: A phytopharmacological review
    • Galani VJ, Patel BG, Rana DG (2010) Sphaeranthus indicus Linn.: a phytopharmacological review. Int J Ayurveda Res 1:247-253
    • (2010) Int J Ayurveda Res , vol.1 , pp. 247-253
    • Galani, V.J.1    Patel, B.G.2    Rana, D.G.3
  • 20
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • DOI 10.1002/elps.1150181505
    • Guex N, Peitsch MC (1997) SWISS-MODEL and the Swiss- PdbViewer: an environment for comparative protein modelling. Electrophoresis 18:2714-2723 (Pubitemid 28059943)
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 22
    • 33645969261 scopus 로고    scopus 로고
    • Biotransformation of sesquiterpenoids having α-, β-unsaturated carbonyl groups with cultured plant cells of Marchantia polymorpha
    • Hegazy M-EF, Kuwata C, Matsushima A, Ahmed AA, Hirata T (2006) Biotransformation of sesquiterpenoids having α-, β-unsaturated carbonyl groups with cultured plant cells of Marchantia polymorpha. J Mol Catalysis B: Enzymatic 39:13-17
    • (2006) J Mol Catalysis B: Enzymatic , vol.39 , pp. 13-17
    • Hegazy, M.-E.F.1    Kuwata, C.2    Matsushima, A.3    Ahmed, A.A.4    Hirata, T.5
  • 23
    • 33947716119 scopus 로고    scopus 로고
    • Software news and update a semiempirical free energy force field with charge-based desolvation
    • DOI 10.1002/jcc.20634
    • Huey R, Morris GM, Olson AJ, Goodsell DS (2007) A semiempirical free energy force field with charge-based desolvation. J Comput Chem 28:1145-1152 (Pubitemid 46506716)
    • (2007) Journal of Computational Chemistry , vol.28 , Issue.6 , pp. 1145-1152
    • Huey, R.1    Morris, G.M.2    Olson, A.J.3    Goodsell, D.S.4
  • 24
    • 0026088577 scopus 로고
    • The high-spin/low-spin equilibrium in cytochrome P-450-a new method for determination of the high-spin content
    • Jung C, Ristau O, Rein H (1991) The high-spin/low-spin equilibrium in cytochrome P-450-a new method for determination of the high-spin content. Biochim Biophys Acta 1076:130-136
    • (1991) Biochim Biophys Acta , vol.1076 , pp. 130-136
    • Jung, C.1    Ristau, O.2    Rein, H.3
  • 27
    • 79957576732 scopus 로고    scopus 로고
    • Investigation of cytochromes P450 in myxobacteria: Excavation of cytochromes P450 from the genome of Sorangium cellulosum so ce56
    • Khatri Y, Hannemann F, Perlova O, Müller R, Bernhardt R (2011) Investigation of cytochromes P450 in myxobacteria: excavation of cytochromes P450 from the genome of Sorangium cellulosum So ce56. FEBS Lett 585:1506-1513
    • (2011) FEBS Lett , vol.585 , pp. 1506-1513
    • Khatri, Y.1    Hannemann, F.2    Perlova, O.3    Müller, R.4    Bernhardt, R.5
  • 28
    • 0029017924 scopus 로고
    • Fed-batch biotransformation of β-ionone by Aspergillus niger
    • Larroche C, Creuly C, Gros JB (1995) Fed-batch biotransformation of β-ionone by Aspergillus niger. Appl Microbiol Biotechnol 43:222-227
    • (1995) Appl Microbiol Biotechnol , vol.43 , pp. 222-227
    • Larroche, C.1    Creuly, C.2    Gros, J.B.3
  • 29
    • 0035958915 scopus 로고    scopus 로고
    • Folding requirements are different between sterol 14alpha-demethylase (CYP51) from Mycobacterium tuberculosis and human or fungal orthologs
    • Lepesheva GI, Podust LM, Bellamine A, Waterman MR (2001) Folding requirements are different between sterol 14alpha-demethylase (CYP51) from Mycobacterium tuberculosis and human or fungal orthologs. J Biol Chem 276:28413-28420
    • (2001) J Biol Chem , vol.276 , pp. 28413-28420
    • Lepesheva, G.I.1    Podust, L.M.2    Bellamine, A.3    Waterman, M.R.4
  • 30
    • 37049123301 scopus 로고
    • Carotenoids and related compounds. Part XXVIII. Syntheses of zeaxanthin, β-cryptoxanthin, and zeinoxanthin (α-cryptoxanthin)
    • Loeber DE, Russell SW, Toube TP, Weedon BCL, Diment J (1971) Carotenoids and related compounds. Part XXVIII. Syntheses of zeaxanthin, β-cryptoxanthin, and zeinoxanthin (α-cryptoxanthin). J Chem Soc C:404-408
    • (1971) J Chem Soc , vol.C , pp. 404-408
    • Loeber, D.E.1    Russell, S.W.2    Toube, T.P.3    Weedon, B.C.L.4    Diment, J.5
  • 31
    • 79951567094 scopus 로고    scopus 로고
    • Spectroscopic features of cytochrome P450 reaction intermediates
    • Luthra A, Denisov IG, Sligar SG (2011) Spectroscopic features of cytochrome P450 reaction intermediates. Arch Biochem Biophys 507:26-35
    • (2011) Arch Biochem Biophys , vol.507 , pp. 26-35
    • Luthra, A.1    Denisov, I.G.2    Sligar, S.G.3
  • 34
    • 0033858087 scopus 로고    scopus 로고
    • Insecticidal sesquiterpene from Alpinia oxyphylla against Drosophila melanogaster
    • Miyazawa M, Nakamura Y, Ishikawa Y (2000) Insecticidal sesquiterpene from Alpinia oxyphylla against Drosophila melanogaster. J Agric Food Chem 48:3639-3641
    • (2000) J Agric Food Chem , vol.48 , pp. 3639-3641
    • Miyazawa, M.1    Nakamura, Y.2    Ishikawa, Y.3
  • 36
    • 0028205462 scopus 로고
    • Structural and enzymological analysis of the interaction of isolated domains of cytochrome P-450 BM3
    • DOI 10.1016/0014-5793(94)80609-8
    • Munro AW, Lindsay JG, Coggins JR, Kelly SM, Price NC (1994) Structural and enzymological analysis of the interaction of isolated domains of cytochrome P-450 BM3. FEBS Lett 343:70-74 (Pubitemid 24123949)
    • (1994) FEBS Letters , vol.343 , Issue.1 , pp. 70-74
    • Munro, A.W.1
  • 37
    • 77954916370 scopus 로고    scopus 로고
    • Nootkatone, a characteristic constituent of grapefruit, stimulates energy metabolism and prevents diet-induced obesity by activating AMPK
    • Murase T, Misawa K, Haramizu S, Minegishi Y, Hase T (2010) Nootkatone, a characteristic constituent of grapefruit, stimulates energy metabolism and prevents diet-induced obesity by activating AMPK. Am J Physiol Endocrinol Metab 299:266-275
    • (2010) Am J Physiol Endocrinol Metab , vol.299 , pp. 266-275
    • Murase, T.1    Misawa, K.2    Haramizu, S.3    Minegishi, Y.4    Hase, T.5
  • 38
    • 0031860811 scopus 로고    scopus 로고
    • Chaperone coexpression plasmids: Differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli
    • Nishihara K, Kanemori M, Kitagawa M, Yanagi H, Yura T (1998) Chaperone coexpression plasmids:differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli. Appl Environ Microbiol 64:1694-1699 (Pubitemid 28234771)
    • (1998) Applied and Environmental Microbiology , vol.64 , Issue.5 , pp. 1694-1699
    • Nishihara, K.1    Kanemori, M.2    Kitagawa, M.3    Yanagi, H.4    Yura, T.5
  • 39
    • 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
  • 40
    • 47649104479 scopus 로고    scopus 로고
    • Mechanism and role of covalent heme binding in the CYP4 family of P450 enzymes and the mammalian peroxidases
    • Ortiz de Montellano PR (2008) Mechanism and role of covalent heme binding in the CYP4 family of P450 enzymes and the mammalian peroxidases. Drug Metab Rev 40:405-426
    • (2008) Drug Metab Rev , vol.40 , pp. 405-426
    • Ortiz De Montellano, P.R.1
  • 42
    • 0022919721 scopus 로고
    • Crystal structure of substrate-free Pseudomonas putida cytochrome P-450
    • DOI 10.1021/bi00366a049
    • Poulos TL, Finzel BC, Howard AJ (1986) Crystal structure of substrate-free Pseudomonas putida cytochrome P-450. Biochemistry 25:5314-5322 (Pubitemid 17016546)
    • (1986) Biochemistry , vol.25 , Issue.18 , pp. 5314-5322
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 43
    • 0023645035 scopus 로고
    • High-resolution crystal structure of cytochrome P450cam
    • Poulos TL, Finzel BC, Howard AJ (1987) High-resolution crystal structure of cytochrome P450cam. J Mol Biol 195:687-700
    • (1987) J Mol Biol , vol.195 , pp. 687-700
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 44
    • 33749534302 scopus 로고    scopus 로고
    • Pentalenolactone biosynthesis. Molecular cloning and assignment of biochemical function to PtlI, a cytochrome P450 of Streptomyces avermitilis
    • DOI 10.1021/ja0639214
    • Quaderer R, Omura S, Ikeda H, Cane DE (2006) Pentalenolactone biosynthesis. Molecular cloning and assignment of biochemical function to PTLI, a cytochrome P450 of Streptomyces avermitilis. J Am Chem Soc 128:13036-13037 (Pubitemid 44527659)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.40 , pp. 13036-13037
    • Quaderer, R.1    Omura, S.2    Ikeda, H.3    Cane, D.E.4
  • 45
    • 0027326717 scopus 로고
    • Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's
    • Ravichandran KG, Boddupalli SS, Hasemann CA, Peterson JA, Deisenhofer J (1993) Crystal structure of hemoprotein domain of P450BM-3, a prototype formicrosomal P450's. Science 261:731-736 (Pubitemid 23278388)
    • (1993) Science , vol.261 , Issue.5122 , pp. 731-736
    • Ravichandran, K.G.1    Boddupalli, S.S.2    Hasemann, C.A.3    Peterson, J.A.4    Deisenhofer, J.5
  • 46
    • 0033397980 scopus 로고    scopus 로고
    • Python: A programming language for software integration and development
    • Sanner MF (1999) Python: a programming language for software integration and development. J Mol Graph Model 17:57-61
    • (1999) J Mol Graph Model , vol.17 , pp. 57-61
    • Sanner, M.F.1
  • 49
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • DOI 10.1093/nar/gkg520
    • Schwede T, Kopp J, Guex N, Peitsch MC (2003) SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res 31:3381-3385 (Pubitemid 37442164)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 54
    • 65949116191 scopus 로고    scopus 로고
    • Myxobacteria - 'microbial factories' for the production of bioactive secondary metabolites
    • Wenzel SC, Müller R (2009) Myxobacteria - 'microbial factories' for the production of bioactive secondary metabolites. Mol Biosyst 5:567-574
    • (2009) Mol Biosyst , vol.5 , pp. 567-574
    • Wenzel, S.C.1    Müller, R.2
  • 55
    • 0018699952 scopus 로고
    • The kinetics of reversible tight-binding inhibition
    • Williams JW, Morrison JF (1979) The kinetics of reversible tight-binding inhibition. Methods Enzymol 63:437-467
    • (1979) Methods Enzymol , vol.63 , pp. 437-467
    • Williams, J.W.1    Morrison, J.F.2
  • 56
    • 43749088055 scopus 로고    scopus 로고
    • Biosynthesis of the sesquiterpene antibiotic albaflavenone in Streptomyces coelicolor A3(2)
    • Zhao B, Lin X, Lei L, Lamb DC, Kelly SL, Waterman MR, Cane DE (2008) Biosynthesis of the sesquiterpene antibiotic albaflavenone in Streptomyces coelicolor A3(2). J Biol Chem 283:8183-8189
    • (2008) J Biol Chem , vol.283 , pp. 8183-8189
    • Zhao, B.1    Lin, X.2    Lei, L.3    Lamb, D.C.4    Kelly, S.L.5    Waterman, M.R.6    Cane, D.E.7
  • 57
    • 0034984281 scopus 로고    scopus 로고
    • Nootkatone is a repellent for Formosan subterranean termite (Coptotermes formosanus)
    • DOI 10.1023/A:1010301308649
    • Zhu BC, Henderson G, Chen F, Maistrello L, Laine RA (2001) Nootkatone is a repellent for Formosan subterranean termite (Coptotermes formosanus). J Chem Ecol 27:523-531 (Pubitemid 32554187)
    • (2001) Journal of Chemical Ecology , vol.27 , Issue.3 , pp. 523-531
    • Zhu, B.C.R.1    Henderson, G.2    Chen, F.3    Maistrello, L.4    Laine, R.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.