메뉴 건너뛰기




Volumn 46, Issue 6, 2006, Pages 435-443

Acyl-CoA oxidase activity from Beauveria bassiana, an entomopathogenic fungus

Author keywords

[No Author keywords available]

Indexed keywords

ACYL COENZYME A OXIDASE; ALKANE; AMITROLE; ENZYME INHIBITOR;

EID: 33845620688     PISSN: 0233111X     EISSN: 15214028     Source Type: Journal    
DOI: 10.1002/jobm.200610136     Document Type: Article
Times cited : (3)

References (30)
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgramquantities of protein utilizing the principle of protein-dye binding
    • BRADFORD, M. M., 1976. A rapid and sensitive method for the quantitation of microgramquantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0024999831 scopus 로고
    • Separate peroxisomal oxidases for fatty Acyl-CoA and Trihydroxycoprostanoyl-CoA in human liver
    • CASTEELS, M., XHEPERS, L., VAN VELDHOVEN, P. P., EYSSEN, H. J. and MANNAERTS, G. P., 1990. Separate peroxisomal oxidases for fatty Acyl-CoA and Trihydroxycoprostanoyl-CoA in human liver. J. Lipid Res., 31, 1865-1872.
    • (1990) J. Lipid Res. , vol.31 , pp. 1865-1872
    • Casteels, M.1    Xhepers, L.2    Van Veldhoven, P.P.3    Eyssen, H.J.4    Mannaerts, G.P.5
  • 4
    • 0001253638 scopus 로고    scopus 로고
    • Biochemical interaction between entomopathogenous fungi and their insect host like hydrocarbons
    • CRESPO, R., JUÁREZ, M. P. and CAFFERATA, L. F. R., 2000. Biochemical interaction between entomopathogenous fungi and their insect host like hydrocarbons. Mycologia, 92, 528-536.
    • (2000) Mycologia , vol.92 , pp. 528-536
    • Crespo, R.1    Juárez, M.P.2    Cafferata, L.F.R.3
  • 6
    • 0034034085 scopus 로고    scopus 로고
    • Purification and characterization of a novel pumpkin short-chain acyl coenzyme A oxidase with structural similarity to acyl coenzyme A dehydrogenases
    • DE BELLIS, L., GONZALI, S., ALPI, A., HAYASHI, H., HAYASHI, M. and NISHMURA, M., 2000. Purification and characterization of a novel pumpkin short-chain acyl coenzyme A oxidase with structural similarity to acyl coenzyme A dehydrogenases. Plant Physiol., 123, 327-334.
    • (2000) Plant Physiol. , vol.123 , pp. 327-334
    • De Bellis, L.1    Gonzali, S.2    Alpi, A.3    Hayashi, H.4    Hayashi, M.5    Nishmura, M.6
  • 7
    • 0038122825 scopus 로고    scopus 로고
    • In silico prediction of the peroxisoma proteome in fungi, plants and animals
    • EMANUELSSON, O., ELOFSSON, A., VON HEIJNE, G. and CRISTOBAL, S., 2003. In silico prediction of the peroxisoma proteome in fungi, plants and animals. J. Mol. Biol., 330, 443-456.
    • (2003) J. Mol. Biol. , vol.330 , pp. 443-456
    • Emanuelsson, O.1    Elofsson, A.2    Von Heijne, G.3    Cristobal, S.4
  • 9
    • 0031571137 scopus 로고    scopus 로고
    • Inhibition of acyl-CoA oxidase by phenol and its implication in measurement of the enzyme activity via the peroxidase-coupled assay system
    • GOPALAN, K. V. and SRIVASTAVA, D. K., 1997. Inhibition of acyl-CoA oxidase by phenol and its implication in measurement of the enzyme activity via the peroxidase-coupled assay system. Anal. Biochem., 250, 44-50.
    • (1997) Anal. Biochem. , vol.250 , pp. 44-50
    • Gopalan, K.V.1    Srivastava, D.K.2
  • 10
    • 0035313687 scopus 로고    scopus 로고
    • Potential failsafe mechanisms against the spread and introgression of transgenic hypervirulent biocontrol fungi
    • GRESEEL, J., 2001. Potential failsafe mechanisms against the spread and introgression of transgenic hypervirulent biocontrol fungi. Trens Biotech., 19, 149-154.
    • (2001) Trens Biotech. , vol.19 , pp. 149-154
    • Greseel, J.1
  • 11
    • 0033617449 scopus 로고    scopus 로고
    • A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant peroxisomes
    • HAYASHI, H., DE BELLIS, L., CIURLI, A., KONDO, M., HAYASHI, M. and NISHIMURA, M., 1999. A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant peroxisomes. J. Biol. Chem., 274, 12715-12721.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12715-12721
    • Hayashi, H.1    De Bellis, L.2    Ciurli, A.3    Kondo, M.4    Hayashi, M.5    Nishimura, M.6
  • 12
    • 0028891564 scopus 로고
    • Regulation of acyl-CoA oxidases in maize seedlings
    • HOOKS, M. A, BODE, K. and COUEE, I., 1995. Regulation of acyl-CoA oxidases in maize seedlings. Phytochemistry, 40, 657-660.
    • (1995) Phytochemistry , vol.40 , pp. 657-660
    • Hooks, M.A.1    Bode, K.2    Couee, I.3
  • 13
    • 0028188245 scopus 로고
    • Hydrocarbons biosynthesis in T. infestans eggs
    • JUÁREZ, M. P., 1994. Hydrocarbons biosynthesis in T. infestans eggs. Arch. Insect Biochem. Phisiol., 25, 193-206.
    • (1994) Arch. Insect Biochem. Phisiol. , vol.25 , pp. 193-206
    • Juárez, M.P.1
  • 14
    • 33751229676 scopus 로고    scopus 로고
    • Mycoinsecticides against Chagas disease vectors: Biochemistry involved in insect host hydrocarbon degradation
    • (MASCOMA, S., ed.), Monduzzi Bologna
    • JUÁREZ, M. P., PEDRINI, N. and CRESPO, R., 2004. Mycoinsecticides against Chagas disease vectors: Biochemistry involved in insect host hydrocarbon degradation. In: Multidisciplinary for Parasites, Vectors and Parasitic Diseases (MASCOMA, S., ed.), pp. 137-142. Monduzzi Bologna.
    • (2004) Multidisciplinary for Parasites, Vectors and Parasitic Diseases , pp. 137-142
    • Juárez, M.P.1    Pedrini, N.2    Crespo, R.3
  • 15
    • 0027159789 scopus 로고
    • Fatty acid degradation in plant peroxisomes: Function and biosynthesis of the enzymes involved
    • KIND, H., 1993. Fatty acid degradation in plant peroxisomes: function and biosynthesis of the enzymes involved. Biochemie, 75, 225-230.
    • (1993) Biochemie , vol.75 , pp. 225-230
    • Kind, H.1
  • 17
    • 0034547929 scopus 로고    scopus 로고
    • Purification and characterization of the recombinant form of acyl-CoA oxidase 3 from the yeast Yarrowia lipolytica
    • LUO, Y. S., WANG, H. J., GOPALAN, K. V., SRIVASTAVA, D. K., NICAUD, J. M. and CHARDOT, T., 2000. Purification and characterization of the recombinant form of acyl-CoA oxidase 3 from the yeast Yarrowia lipolytica. Arch. Biochem.Biophis., 384, 1-8.
    • (2000) Arch. Biochem.Biophis. , vol.384 , pp. 1-8
    • Luo, Y.S.1    Wang, H.J.2    Gopalan, K.V.3    Srivastava, D.K.4    Nicaud, J.M.5    Chardot, T.6
  • 18
    • 18844467907 scopus 로고    scopus 로고
    • Acyl-CoA oxidase, a key step for lipid accumulation in the yeast Yarrowia lipolytica
    • MLICKOVA, K., LUO, Y., D'ANDREA, S., PEC, P., CHARDOT, T. and NICAUD, J. M., 2004. Acyl-CoA oxidase, a key step for lipid accumulation in the yeast Yarrowia lipolytica. J. Mol. Catal. B, 28, 81-85.
    • (2004) J. Mol. Catal. B , vol.28 , pp. 81-85
    • Mlickova, K.1    Luo, Y.2    D'Andrea, S.3    Pec, P.4    Chardot, T.5    Nicaud, J.M.6
  • 19
    • 0031214717 scopus 로고    scopus 로고
    • Entomopathogenous fungi degrade epicuticular hydrocarbons of T. infestans
    • NAPOLITANO, R. and JUAREZ, M. P., 1997. Entomopathogenous fungi degrade epicuticular hydrocarbons of T. infestans. Arch. Biochem. Biophys., 344, 208-214.
    • (1997) Arch. Biochem. Biophys. , vol.344 , pp. 208-214
    • Napolitano, R.1    Juarez, M.P.2
  • 20
    • 0025784439 scopus 로고
    • Determination of Candida tropicalis Acyl-Co A oxidase isozyme function by sequential gene disruption
    • PICATAGGIO, S., DEANDA, K. and MIELENZ, J., 1991. Determination of Candida tropicalis Acyl-Co A oxidase isozyme function by sequential gene disruption. Mol. Cell. Biol., 11, 4333-4339.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4333-4339
    • Picataggio, S.1    Deanda, K.2    Mielenz, J.3
  • 21
    • 0025257335 scopus 로고
    • Presence of three acyl-CoA oxidases in rat liver peroxisomes. An inducible fatty acyl-CoA oxidase, a noninducible fatty acyl-CoA oxidase, and a noninducible trihydroxycoprostanoyl-CoA oxidase
    • SCHEPERS, L., VAN VELDHOVEN, P. P., CASTEELS, M., EYSSEN, H. J. and MANNAERTS, G. P., 1990. Presence of three acyl-CoA oxidases in rat liver peroxisomes. An inducible fatty acyl-CoA oxidase, a noninducible fatty acyl-CoA oxidase, and a noninducible trihydroxycoprostanoyl-CoA oxidase. J. Biol. Chem., 265, 5242-5246.
    • (1990) J. Biol. Chem. , vol.265 , pp. 5242-5246
    • Schepers, L.1    Van Veldhoven, P.P.2    Casteels, M.3    Eyssen, H.J.4    Mannaerts, G.P.5
  • 22
    • 0021809385 scopus 로고
    • A sensitive spectrophotometric assay for peroxisomal Acyl-CoA oxidase
    • SMALL, G. M., BURDETT, K. and CONNOCK, M. J., 1985. A sensitive spectrophotometric assay for peroxisomal Acyl-CoA oxidase. Biochem. J., 227, 205-210.
    • (1985) Biochem. J. , vol.227 , pp. 205-210
    • Small, G.M.1    Burdett, K.2    Connock, M.J.3
  • 23
    • 0038324369 scopus 로고    scopus 로고
    • Identification and cloning of two forms of liver peroxisomal fatty Acyl-CoA oxidase from the koala (Phascolarctos cinereus)
    • THI NGO, S. N., MCKINNON, R. A. and STUPANS, I., 2003. Identification and cloning of two forms of liver peroxisomal fatty Acyl-CoA oxidase from the koala (Phascolarctos cinereus). Gene, 309, 91-99.
    • (2003) Gene , vol.309 , pp. 91-99
    • Thi Ngo, S.N.1    Mckinnon, R.A.2    Stupans, I.3
  • 24
    • 0001746640 scopus 로고
    • Peroximal localization of enzymes related to fatty acid β-oxidation in an n-alkane grown yeast, Candida tropicalis
    • UEDA, M., YAMANOI, K., MORIKAWA, T., OKADA, H. and TANAKA, A., 1985. Peroximal localization of enzymes related to fatty acid β-oxidation in an n-alkane grown yeast, Candida tropicalis. Agric. Biol. Chem., 49, 1821-1828.
    • (1985) Agric. Biol. Chem. , vol.49 , pp. 1821-1828
    • Ueda, M.1    Yamanoi, K.2    Morikawa, T.3    Okada, H.4    Tanaka, A.5
  • 25
    • 0026348109 scopus 로고
    • Mitochondrial and peroxisomal β-oxidation of the branched chain fatty acid 2-methylpalmitate in rar liver
    • VANHOVE, G., VAN VELDHOVEN, P. P., VANHOUTTE, F., PARMENTIER, G., EYSSEN, H. and MANNAERTS, G. P., 1991. Mitochondrial and peroxisomal β-oxidation of the branched chain fatty acid 2-methylpalmitate in rar liver. J. Biol. Chem., 266, 24670-24675.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24670-24675
    • Vanhove, G.1    Van Veldhoven, P.P.2    Vanhoutte, F.3    Parmentier, G.4    Eyssen, H.5    Mannaerts, G.P.6
  • 27
    • 0026668028 scopus 로고
    • Substrate specificities of rat liver peroxisomal Acyl-CoA oxidases: Palmitoyl-CoA oxidase (Inducible Acyl-CoA oxidase), Pristanoyl-CoA oxidase (Non-inducible acyl-CoA oxidase), and trihydroxycoprostanoyl-CoA oxidase
    • VAN VELDHOVEN, P. P., VANHOVE, G., ASSSELBERGHS, S., EYSSEN, H. J. and MANNAERTS, G. P., 1992. Substrate specificities of rat liver peroxisomal Acyl-CoA oxidases: Palmitoyl-CoA oxidase (Inducible Acyl-CoA oxidase), Pristanoyl-CoA oxidase (Non-inducible acyl-CoA oxidase), and trihydroxycoprostanoyl-CoA oxidase. J. Biol. Chem., 267, 20065-20074.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20065-20074
    • Van Veldhoven, P.P.1    Vanhove, G.2    Assselberghs, S.3    Eyssen, H.J.4    Mannaerts, G.P.5
  • 28
    • 0034956657 scopus 로고    scopus 로고
    • Further insights into peroxisomal lipid breakdown via α- and β-oxidation
    • VAN VELDHOVEN, P. P., CASTEELS, M., MANNAERTS, G. P. and BAES, M., 2001. Further insights into peroxisomal lipid breakdown via α- and β-oxidation. Bioch. Soc. Trans., 29, 292-298.
    • (2001) Bioch. Soc. Trans. , vol.29 , pp. 292-298
    • Van Veldhoven, P.P.1    Casteels, M.2    Mannaerts, G.P.3    Baes, M.4
  • 29
    • 0025757048 scopus 로고
    • The reductive half-reaction in Acyl- CoA oxidase from Candida tropicalis: Interaction with acyl CoA analogues and an unusual thioesterase activity
    • WANG, R. and THORPE, C., 1991. The reductive half-reaction in Acyl- CoA oxidase from Candida tropicalis: Interaction with acyl CoA analogues and an unusual thioesterase activity. Arch. Bioch. Biophys., 286, 504-510.
    • (1991) Arch. Bioch. Biophys. , vol.286 , pp. 504-510
    • Wang, R.1    Thorpe, C.2
  • 30
    • 0037319801 scopus 로고    scopus 로고
    • A new type of a multifunctional β-oxidation enzyme in Euglena
    • WINKLER, U., SAFTEL, W. and STABENAU, H., 2003. A new type of a multifunctional β-oxidation enzyme in Euglena. Plant Physiol., 131, 753-762.
    • (2003) Plant Physiol. , vol.131 , pp. 753-762
    • Winkler, U.1    Saftel, W.2    Stabenau, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.