메뉴 건너뛰기




Volumn 48, Issue 2, 2011, Pages 181-186

Hydrogen peroxide-mediated dealkylation of 7-ethoxycoumarin by cytochrome P450 (CYP107AJ1) from Streptomyces peucetius ATCC27952

Author keywords

7 Ethoxycoumarin; Cytochrome P450; Homology modeling; Peroxygenase; Streptomyces peucetius

Indexed keywords

7-ETHOXYCOUMARIN; CYTOCHROME P450; HOMOLOGY MODELING; PEROXYGENASE; STREPTOMYCES PEUCETIUS;

EID: 78650806324     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2010.10.001     Document Type: Article
Times cited : (16)

References (31)
  • 1
    • 0023739721 scopus 로고
    • Role of cytochrome P-450 in hydrocarbon formation from xenobiotic and lipid hydroperoxides
    • Coon M.J., Vaz A.D. Role of cytochrome P-450 in hydrocarbon formation from xenobiotic and lipid hydroperoxides. Prog Clin Biol Res 1988, 274:497-507.
    • (1988) Prog Clin Biol Res , vol.274 , pp. 497-507
    • Coon, M.J.1    Vaz, A.D.2
  • 2
    • 0034973773 scopus 로고    scopus 로고
    • Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity
    • Guengerich F.P. Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity. Chem Res Toxicol 2001, 14:611-650.
    • (2001) Chem Res Toxicol , vol.14 , pp. 611-650
    • Guengerich, F.P.1
  • 5
    • 0037646516 scopus 로고    scopus 로고
    • Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. Crystallographic, spectroscopic, and mutational studies
    • Lee D.S., Yamada A., Sugimoto H., Matsunaga I., Ogura H., Ichihara K., et al. Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. Crystallographic, spectroscopic, and mutational studies. J Biol Chem 2003, 278:9761-9767.
    • (2003) J Biol Chem , vol.278 , pp. 9761-9767
    • Lee, D.S.1    Yamada, A.2    Sugimoto, H.3    Matsunaga, I.4    Ogura, H.5    Ichihara, K.6
  • 6
    • 13844255406 scopus 로고    scopus 로고
    • Reaction of haem containing proteins and enzymes with hydroperoxides: the radical view
    • Svistunenko D.A. Reaction of haem containing proteins and enzymes with hydroperoxides: the radical view. Biochem Biophys Acta 2005, 1707:127-155.
    • (2005) Biochem Biophys Acta , vol.1707 , pp. 127-155
    • Svistunenko, D.A.1
  • 7
    • 10444284194 scopus 로고    scopus 로고
    • Nitric oxide reductase (P450nor) from Fusarium oxysporum
    • Daiber A., Shoun H., Ullrich V. Nitric oxide reductase (P450nor) from Fusarium oxysporum. J Inorg Biochem 2005, 99:185-193.
    • (2005) J Inorg Biochem , vol.99 , pp. 185-193
    • Daiber, A.1    Shoun, H.2    Ullrich, V.3
  • 8
    • 0029940449 scopus 로고    scopus 로고
    • Direct involvement of hydrogen peroxide in bacterial alpha-hydroxylation of fatty acid
    • Matsunaga I., Yamada M., Kusunose E., Nishiuchi Y., Yano I., Ichihara K. Direct involvement of hydrogen peroxide in bacterial alpha-hydroxylation of fatty acid. FEBS Lett 1996, 386:252-254.
    • (1996) FEBS Lett , vol.386 , pp. 252-254
    • Matsunaga, I.1    Yamada, M.2    Kusunose, E.3    Nishiuchi, Y.4    Yano, I.5    Ichihara, K.6
  • 9
    • 0037202185 scopus 로고    scopus 로고
    • CYP119 plus a Sulfolobus tokodaii strain 7 ferredoxin and 2-oxoacid: ferredoxin oxidoreductase constitute a high-temperature cytochrome P450 catalytic system
    • Puchkaev A.V., Wakagi T., Ortiz de Montellano P.R. CYP119 plus a Sulfolobus tokodaii strain 7 ferredoxin and 2-oxoacid: ferredoxin oxidoreductase constitute a high-temperature cytochrome P450 catalytic system. J Am Chem Soc 2002, 124:12682-12683.
    • (2002) J Am Chem Soc , vol.124 , pp. 12682-12683
    • Puchkaev, A.V.1    Wakagi, T.2    Ortiz de Montellano, P.R.3
  • 10
    • 4744343779 scopus 로고    scopus 로고
    • Thermodynamic and biophysical characterization of cytochrome P450 BioI from Bacillus subtilis
    • Lawson R.J., Leys D., Sutcliffe M.J., Kemp C.A., Cheesman M.R., Smith S.J., et al. Thermodynamic and biophysical characterization of cytochrome P450 BioI from Bacillus subtilis. Biochemistry 2004, 43:12410-12426.
    • (2004) Biochemistry , vol.43 , pp. 12410-12426
    • Lawson, R.J.1    Leys, D.2    Sutcliffe, M.J.3    Kemp, C.A.4    Cheesman, M.R.5    Smith, S.J.6
  • 11
    • 0033578095 scopus 로고    scopus 로고
    • Laboratory evolution of peroxide-mediated cytochrome P450 hydroxylation
    • Joo H., Lin Z., Arnold F.H. Laboratory evolution of peroxide-mediated cytochrome P450 hydroxylation. Nature 1999, 399:670-673.
    • (1999) Nature , vol.399 , pp. 670-673
    • Joo, H.1    Lin, Z.2    Arnold, F.H.3
  • 12
    • 0043269709 scopus 로고    scopus 로고
    • A self-sufficient peroxide-driven hydroxylation biocatalyst
    • Cirino P.C., Arnold F.H. A self-sufficient peroxide-driven hydroxylation biocatalyst. Angew Chem Int Ed Engl 2003, 42:3299-3301.
    • (2003) Angew Chem Int Ed Engl , vol.42 , pp. 3299-3301
    • Cirino, P.C.1    Arnold, F.H.2
  • 13
    • 33745425331 scopus 로고    scopus 로고
    • Replacement of natural cofactors by selected hydrogen peroxide donors or organic peroxides results in improved activity for CYP3A4 and CYP2D6
    • Chefson A., Zhao J., Auclair K. Replacement of natural cofactors by selected hydrogen peroxide donors or organic peroxides results in improved activity for CYP3A4 and CYP2D6. Chembiochem 2006, 7:916-919.
    • (2006) Chembiochem , vol.7 , pp. 916-919
    • Chefson, A.1    Zhao, J.2    Auclair, K.3
  • 14
    • 33751542716 scopus 로고    scopus 로고
    • Engineering of cytochrome P450 3A4 for enhanced peroxide-mediated substrate oxidation using directed evolution and site-directed mutagenesis
    • Kumar S., Liu H., Halpert J.R. Engineering of cytochrome P450 3A4 for enhanced peroxide-mediated substrate oxidation using directed evolution and site-directed mutagenesis. Drug Metab Dispos 2006, 34:1958-1965.
    • (2006) Drug Metab Dispos , vol.34 , pp. 1958-1965
    • Kumar, S.1    Liu, H.2    Halpert, J.R.3
  • 17
    • 31844447468 scopus 로고    scopus 로고
    • Oxidative activities of heterologously expressed CYP107B1 and CYP105D1 in whole-cell biotransformation using Streptomyces lividans TK24
    • Ueno M., Midori Y., Michizane H., Motohiro H., Fujie A. Oxidative activities of heterologously expressed CYP107B1 and CYP105D1 in whole-cell biotransformation using Streptomyces lividans TK24. J Biosci Bioeng 2005, 100:567-572.
    • (2005) J Biosci Bioeng , vol.100 , pp. 567-572
    • Ueno, M.1    Midori, Y.2    Michizane, H.3    Motohiro, H.4    Fujie, A.5
  • 18
    • 44649165683 scopus 로고    scopus 로고
    • Cytochrome P450 (CYP105F2) from Streptomyces peucetius and its activity with oleandomycin
    • Shrestha P., Oh T.-J., Liou K., Sohng J.K. Cytochrome P450 (CYP105F2) from Streptomyces peucetius and its activity with oleandomycin. Appl Microbiol Biotechnol 2008, 79:555-562.
    • (2008) Appl Microbiol Biotechnol , vol.79 , pp. 555-562
    • Shrestha, P.1    Oh, T.-J.2    Liou, K.3    Sohng, J.K.4
  • 19
    • 49249117096 scopus 로고    scopus 로고
    • Bioconversion of small molecules by cytochrome P450 species expressed in Escherichia coli
    • Uno T., Sota O., Satoko M., Atsushi I., Yuichi U., Masahiko N., et al. Bioconversion of small molecules by cytochrome P450 species expressed in Escherichia coli. Biotechnol Appl Biochem 2008, 50:165-171.
    • (2008) Biotechnol Appl Biochem , vol.50 , pp. 165-171
    • Uno, T.1    Sota, O.2    Satoko, M.3    Atsushi, I.4    Yuichi, U.5    Masahiko, N.6
  • 20
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali A., Blundell T.L. Comparative protein modeling by satisfaction of spatial restraints. Mol Biol 1993, 234:779-815.
    • (1993) Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 21
    • 0037212102 scopus 로고    scopus 로고
    • LigandFit: a novel method for the shape-directed rapid docking of ligands to protein active sites
    • Venkatachalam C.M., Jiang X., Oldfield T., Waldman M. LigandFit: a novel method for the shape-directed rapid docking of ligands to protein active sites. J Mol Graph Model 2003, 21:289-307.
    • (2003) J Mol Graph Model , vol.21 , pp. 289-307
    • Venkatachalam, C.M.1    Jiang, X.2    Oldfield, T.3    Waldman, M.4
  • 25
    • 64549133456 scopus 로고    scopus 로고
    • Identification and functional characterization of an afsR homolog regulatory gene from Streptomyces venezuelae ATCC 15439
    • Maharjan S., Oh T.-J., Lee H.C., Sohng J.K. Identification and functional characterization of an afsR homolog regulatory gene from Streptomyces venezuelae ATCC 15439. J Microbiol Biotechnol 2009, 19:121-127.
    • (2009) J Microbiol Biotechnol , vol.19 , pp. 121-127
    • Maharjan, S.1    Oh, T.-J.2    Lee, H.C.3    Sohng, J.K.4
  • 26
    • 0037228761 scopus 로고    scopus 로고
    • Enhanced heterologous expression of two Streptomyces griseolus cytochrome P450s and Streptomyces coelicolor ferredoxin reductase as potentially efficient hydroxylation catalysts
    • Hussain H.A., Ward J.M. Enhanced heterologous expression of two Streptomyces griseolus cytochrome P450s and Streptomyces coelicolor ferredoxin reductase as potentially efficient hydroxylation catalysts. Appl Environ Microbiol 2003, 69:373-382.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 373-382
    • Hussain, H.A.1    Ward, J.M.2
  • 27
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes I. Evidence for its hemoprotein nature
    • Omura T., Sato R. The carbon monoxide-binding pigment of liver microsomes I. Evidence for its hemoprotein nature. J Biol Chem 1964, 239:2370-2378.
    • (1964) J Biol Chem , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 29
    • 65549169871 scopus 로고    scopus 로고
    • Screening for cytochrome p450 reactivity by harnessing catalase as reporter enzyme
    • Rabe K.S., Spengler M., Erkelenz M., Müller J., Gandubert V.J., Hayen H., et al. Screening for cytochrome p450 reactivity by harnessing catalase as reporter enzyme. ChemBioChem 2009, 10:751-757.
    • (2009) ChemBioChem , vol.10 , pp. 751-757
    • Rabe, K.S.1    Spengler, M.2    Erkelenz, M.3    Müller, J.4    Gandubert, V.J.5    Hayen, H.6
  • 30
    • 33748750539 scopus 로고    scopus 로고
    • The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae
    • Sherman D.H., Li S., Yermalitskaya L.V., Kim Y., Smith J.A., Waterman M.R., et al. The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae. J Biol Chem 2006, 281:26289-26297.
    • (2006) J Biol Chem , vol.281 , pp. 26289-26297
    • Sherman, D.H.1    Li, S.2    Yermalitskaya, L.V.3    Kim, Y.4    Smith, J.A.5    Waterman, M.R.6
  • 31
    • 0029876059 scopus 로고    scopus 로고
    • The catalytic mechanism of cytochrome P450 BM3 involves a 6Å movement of the bound substrate on reduction
    • Modi S., Sutcliffe M.J., Primrose W.U., Lian L.Y., Roberts G.C. The catalytic mechanism of cytochrome P450 BM3 involves a 6Å movement of the bound substrate on reduction. Nat Struct Biol 1996, 3:414-417.
    • (1996) Nat Struct Biol , vol.3 , pp. 414-417
    • Modi, S.1    Sutcliffe, M.J.2    Primrose, W.U.3    Lian, L.Y.4    Roberts, G.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.