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Volumn 25, Issue 9, 2015, Pages 1417-1424

Homology modeling and in vitro analysis for characterization of Streptomyces peucetius CYP157C4

Author keywords

7 ethoxycoumarin; Cytochrome P450; Homology modeling; In vitro assay; Streptomyces peucetius

Indexed keywords

7 ETHOXYCOUMARIN; CYTOCHROME P450; 7-ETHOXYCOUMARIN; COUMARIN DERIVATIVE;

EID: 84941921713     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.1504.04057     Document Type: Article
Times cited : (6)

References (33)
  • 2
    • 33745911122 scopus 로고    scopus 로고
    • Class dependent sequence alignment strategy improves the structural and functional modeling of P450s
    • Baudry J, Rupasinghe S, Schuler MA. 2006. Class dependent sequence alignment strategy improves the structural and functional modeling of P450s. Protein Eng. Des. Selec. 19: 345-353.
    • (2006) Protein Eng. Des. Selec , vol.19 , pp. 345-353
    • Baudry, J.1    Rupasinghe, S.2    Schuler, M.A.3
  • 3
    • 0028794689 scopus 로고    scopus 로고
    • Cytochrome P450: Structure, function, and generation of reactive oxygen species
    • Bernhardt R. 1996. Cytochrome P450: structure, function, and generation of reactive oxygen species. Rev. Physiol. Biochem. Pharmacol. 127: 137-221.
    • (1996) Rev. Physiol. Biochem. Pharmacol , vol.127 , pp. 137-221
    • Bernhardt, R.1
  • 4
    • 84862212859 scopus 로고    scopus 로고
    • Homology modeling and docking studies of Streptomyces peucetius CYP147F1 as limonene hydroxylase
    • Bhattarai S, Liou K, Oh TJ. 2012. Homology modeling and docking studies of Streptomyces peucetius CYP147F1 as limonene hydroxylase. J. Microbiol. Biotechnol. 22: 917-922.
    • (2012) J. Microbiol. Biotechnol , vol.22 , pp. 917-922
    • Bhattarai, S.1    Liou, K.2    Oh, T.J.3
  • 6
    • 84941891135 scopus 로고    scopus 로고
    • Discovery Studio 3.5, Accelrys Inc., San Diego, CA, USA
    • Discovery Studio 3.5. 2012. Accelrys Inc., San Diego, CA, USA. Available from http://www.accelrys.com.
    • (2012)
  • 8
    • 0030575194 scopus 로고    scopus 로고
    • Site-directed mutagenesis of human prostacyclin synthase: Alteration of Cys441 of the Cys pocket, and Glu347 and Arg350 of the ExxR motif
    • Hatae T, Hara S, Yokoyama C, Yabuki T, Inoue H, Ullrich V, Tanabe T. 1996. Site-directed mutagenesis of human prostacyclin synthase: alteration of Cys441 of the Cys pocket, and Glu347 and Arg350 of the ExxR motif. FEBS Lett. 389: 268-272.
    • (1996) FEBS Lett , vol.389 , pp. 268-272
    • Hatae, T.1    Hara, S.2    Yokoyama, C.3    Yabuki, T.4    Inoue, H.5    Ullrich, V.6    Tanabe, T.7
  • 9
    • 0026542989 scopus 로고
    • Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences
    • Gotoh O. 1992. Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences. J. Biol. Chem. 267: 83-90.
    • (1992) J. Biol. Chem , vol.267 , pp. 83-90
    • Gotoh, O.1
  • 10
    • 0025895757 scopus 로고
    • Reactions and significance of cytochrome P-450 enzymes
    • Guengerich FP. 1991. Reactions and significance of cytochrome P-450 enzymes. J. Biol. Chem. 266: 10019-10022.
    • (1991) J. Biol. Chem , vol.266 , pp. 10019-10022
    • Guengerich, F.P.1
  • 16
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes: 1. Evidence for its hemoprotein nature
    • Omura T, Sato R. 1964. The carbon monoxide-binding pigment of liver microsomes: 1. 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
  • 19
    • 14844346830 scopus 로고    scopus 로고
    • Cytochrome P450 structure, mechanism, and biochemistry
    • In Ortiz de Montellano PR, Voss De JJ (eds.), Kluwer Academic/PlenumPublishers, NY
    • Ortiz de Montellano PR. 2004. Cytochrome P450 structure, mechanism, and biochemistry, pp. 183-247. In Ortiz de Montellano PR, Voss De JJ (eds.). Substrate Oxidation by Cytochrome P450 Enzymes. Kluwer Academic/PlenumPublishers, NY.
    • (2004) Substrate Oxidation by Cytochrome P450 Enzymes , pp. 183-247
    • De Ortiz Montellano, P.R.1
  • 20
    • 0025257597 scopus 로고
    • Putidaredoxin reductase and putidaredoxin: Cloning, sequence determination, and heterologous expression of the proteins
    • Peterson JA, Lorence MC, Amarneh B. 1990. Putidaredoxin reductase and putidaredoxin: cloning, sequence determination, and heterologous expression of the proteins. J. Biol. Chem. 265: 6066-6073.
    • (1990) J. Biol. Chem , vol.265 , pp. 6066-6073
    • Peterson, J.A.1    Lorence, M.C.2    Amarneh, B.3
  • 22
    • 33750992460 scopus 로고    scopus 로고
    • The cytochrome P450 gene family CYP157 does not contain EXXR in the K-helix reducing the absolute conserved P450 residues to a single cysteine
    • Rupasinghe S, Schuler MA, Kagawa N, Yuan H, Lei L, Zhao B, et al. 2006. The cytochrome P450 gene family CYP157 does not contain EXXR in the K-helix reducing the absolute conserved P450 residues to a single cysteine. FEBS Lett. 580: 6338-6342.
    • (2006) FEBS Lett , vol.580 , pp. 6338-6342
    • Rupasinghe, S.1    Schuler, M.A.2    Kagawa, N.3    Yuan, H.4    Lei, L.5    Zhao, B.6
  • 25
    • 33748750539 scopus 로고    scopus 로고
    • The struc tural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae
    • Sherman DH, Shengying L, Yermalitskaya LV, Kim Y, Smith JA, Waterman MR, Podust LM. 2006. The struc tural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae. J. Biol. Chem. 281: 26289-26297.
    • (2006) J. Biol. Chem , vol.281 , pp. 26289-26297
    • Sherman, D.H.1    Shengying, L.2    Yermalitskaya, L.V.3    Kim, Y.4    Smith, J.A.5    Waterman, M.R.6    Podust, L.M.7
  • 26
    • 0025755694 scopus 로고
    • Probing the role of lysines and arginines in the catalytic function of cytochrome P450d by site-directed mutagenesis. Interaction with NADPH-cytochrome P450 reductase
    • Shimizu T, Tateishi T, Hatano M, Fujii-Kuriyama Y. 1991. Probing the role of lysines and arginines in the catalytic function of cytochrome P450d by site-directed mutagenesis. Interaction with NADPH-cytochrome P450 reductase. J. Biol. Chem. 266: 3372-3375.
    • (1991) J. Biol. Chem , vol.266 , pp. 3372-3375
    • Shimizu, T.1    Tateishi, T.2    Hatano, M.3    Fujii-Kuriyama, Y.4
  • 27
    • 44649165683 scopus 로고    scopus 로고
    • Cytoc hrome P450 (CYP105F2) from Streptomyces peucetius and its activity with oleandomycin
    • Shrestha P, Oh TJ, Liou K, Sohng J K. 2008. Cytoc hrome P450 (CYP105F2) from Streptomyces peucetius and its activity with oleandomycin. Appl. Microbiol. Biotechnol. 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
  • 28
    • 77649188866 scopus 로고    scopus 로고
    • Characterization of CYP166B1 and its electron transfer system in Streptomyces peucetius var. Caesius ATCC27952
    • Shrestha P, Oh TJ, Niraula NP, Liou K, Yoo JC, Sohng JK. 2010. Characterization of CYP166B1 and its electron transfer system in Streptomyces peucetius var. caesius ATCC27952. Enzyme Microb. Technol. 46: 372-377.
    • (2010) Enzyme Microb. Technol , vol.46 , pp. 372-377
    • Shrestha, P.1    Oh, T.J.2    Niraula, N.P.3    Liou, K.4    Yoo, J.C.5    Sohng, J.K.6
  • 29
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • Sippl MJ. 1993. Recognition of errors in three-dimensional structures of proteins. Proteins 17: 355-362.
    • (1993) Proteins , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 30
    • 84941885018 scopus 로고    scopus 로고
    • The ExPASy (Expert ProteinAnalysis System)proteomics server of the
    • The ExPASy (Expert ProteinAnalysis System) proteomics server of the Swiss Institute of Bioinformatics (SIB). Available at http://ca.expasy.org.
    • Swiss Institute of Bioinformatics (SIB)1
  • 31
    • 31844447468 scopus 로고    scopus 로고
    • Oxidative activities of heterologously expressed CYP107B1 and CYP105D1 in whole-cell biotransformation using Streptomyces lividans TK24
    • Ueno M, Yamashita M, Hashimoto M, Hino M, Fujie A. 2005. Oxidative activities of heterologously expressed CYP107B1 and CYP105D1 in whole-cell biotransformation using Streptomyces lividans TK24. J. Biosci. Bioeng. 100: 567-572.
    • (2005) J. Biosci. Bioeng , vol.100 , pp. 567-572
    • Ueno, M.1    Yamashita, M.2    Hashimoto, M.3    Hino, M.4    Fujie, A.5
  • 32
    • 49249117096 scopus 로고    scopus 로고
    • Bioconversion of small molecules by cytochrome P450 species expressed in Escherichia coli
    • Uno T, Okamoto S, Masuda S, Itoh A, Uno Y, Nakamura M, et al. 2008. Bioconversion of small molecules by cytochrome P450 species expressed in Escherichia coli. Biotechnol. Appl. Biochem. 50: 165-171.
    • (2008) Biotechnol. Appl. Biochem , vol.50 , pp. 165-171
    • Uno, T.1    Okamoto, S.2    Masuda, S.3    Itoh, A.4    Uno, Y.5    Nakamura, M.6
  • 33
    • 0037212102 scopus 로고    scopus 로고
    • LigandFit: A novel method for the shape-directed rapid doc king of ligands to protein active sites
    • Venkatachalam CM, Jiang X, Oldeld T, Waldman M. 2003. LigandFit: a novel method for the shape-directed rapid doc king of ligands to protein active sites. J. Mol. Graph. Model. 21: 289-307.
    • (2003) J. Mol. Graph. Model , vol.21 , pp. 289-307
    • Venkatachalam, C.M.1    Jiang, X.2    Oldeld, T.3    Waldman, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.