메뉴 건너뛰기




Volumn 127, Issue 4, 2000, Pages 659-664

Functional expression of two Arabidopsis aldehyde oxidases in the yeast Pichia pastoris

Author keywords

Aldehyde oxidase; Arabidopsis thaliana; Indole 3 acetic acid (AA); Molybdenum cofactor; Pichia pastoris

Indexed keywords

ALDEHYDE OXIDASE;

EID: 0034052745     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022654     Document Type: Article
Times cited : (37)

References (32)
  • 2
    • 0023050157 scopus 로고
    • Kinetic and inhibition studies on reduction of diphenyl sulfoxide by guinea pig liver aldehyde oxidase
    • Yoshihara, S. and Tatsumi, K. (1986) Kinetic and inhibition studies on reduction of diphenyl sulfoxide by guinea pig liver aldehyde oxidase. Arch. Biochem. Biophys. 249, 8-14
    • (1986) Arch. Biochem. Biophys. , vol.249 , pp. 8-14
    • Yoshihara, S.1    Tatsumi, K.2
  • 3
    • 0023037533 scopus 로고
    • Aldehyde oxidase from rabbit liver: Specificity toward purines and their analogs
    • Hall, W.W. and Krenitsky, T.A. (1986) Aldehyde oxidase from rabbit liver: specificity toward purines and their analogs. Arch. Biochem. Biophys. 251, 36-46
    • (1986) Arch. Biochem. Biophys. , vol.251 , pp. 36-46
    • Hall, W.W.1    Krenitsky, T.A.2
  • 4
    • 0025873907 scopus 로고
    • Kinetics and cofactor requirements for the nitroreductive metabolism of 1-nitropyrene and 3-nitrofluoranthene by rabbit liver aldehyde oxidase
    • Bauer, S.L. and Howard, P.C. (1991) Kinetics and cofactor requirements for the nitroreductive metabolism of 1-nitropyrene and 3-nitrofluoranthene by rabbit liver aldehyde oxidase. Carcinogenesis 12, 1545-1549
    • (1991) Carcinogenesis , vol.12 , pp. 1545-1549
    • Bauer, S.L.1    Howard, P.C.2
  • 5
    • 0028177106 scopus 로고
    • Epoxide reductase activity of mammalian liver cytosols and aldehyde oxidase
    • Hirao, Y., Kitamura, S., and Tatsumi, K. (1994) Epoxide reductase activity of mammalian liver cytosols and aldehyde oxidase. Carcinogenesis 15, 739-743
    • (1994) Carcinogenesis , vol.15 , pp. 739-743
    • Hirao, Y.1    Kitamura, S.2    Tatsumi, K.3
  • 6
    • 0027144768 scopus 로고
    • Retinal oxidase is identical to aldehyde oxidase
    • Tomita, S., Tsujita, M., and Ichikawa, Y. (1993) Retinal oxidase is identical to aldehyde oxidase. FEBS Lett. 336, 272-274
    • (1993) FEBS Lett. , vol.336 , pp. 272-274
    • Tomita, S.1    Tsujita, M.2    Ichikawa, Y.3
  • 7
    • 84989742281 scopus 로고
    • Metabolism of indole-3-acetaldehyde. III. Some characteristics of the aldehyde oxidase of Avena coleoptiles
    • Rajagopal, R. (1971) Metabolism of indole-3-acetaldehyde. III. Some characteristics of the aldehyde oxidase of Avena coleoptiles. Physiol. Plant. 24, 272-281
    • (1971) Physiol. Plant , vol.24 , pp. 272-281
    • Rajagopal, R.1
  • 8
    • 0001451391 scopus 로고
    • Cucumber seedling indoleacetaldehyde oxidase
    • Bower, P.J., Brown H.M., and Purves, W.K. (1978) Cucumber seedling indoleacetaldehyde oxidase. Plant Physiol. 61, 107-110
    • (1978) Plant Physiol. , vol.61 , pp. 107-110
    • Bower, P.J.1    Brown, H.M.2    Purves, W.K.3
  • 9
    • 0000236687 scopus 로고
    • An in vitro system of indole-3-acetic acid formation from tryptophan in maize (Zea mays) coleoptile extracts
    • Koshiba, T. and Matsuyama, H. (1993) An in vitro system of indole-3-acetic acid formation from tryptophan in maize (Zea mays) coleoptile extracts. Plant Physiol. 102, 1319-1324
    • (1993) Plant Physiol. , vol.102 , pp. 1319-1324
    • Koshiba, T.1    Matsuyama, H.2
  • 10
    • 0030028266 scopus 로고    scopus 로고
    • Purification and properties of flavin-and molybdenum-containing aldehyde oxidase from coleoptiles of maize
    • Koshiba, T., Saito, E., Ono, N., Yamamoto, N., and Sato, M. (1996) Purification and properties of flavin-and molybdenum-containing aldehyde oxidase from coleoptiles of maize. Plant Physiol. 110, 781-789
    • (1996) Plant Physiol. , vol.110 , pp. 781-789
    • Koshiba, T.1    Saito, E.2    Ono, N.3    Yamamoto, N.4    Sato, M.5
  • 11
    • 0031992097 scopus 로고    scopus 로고
    • Higher activity of an aldehyde oxidase in the auxin-overproducing superroot1 mutant of Arabidopsis thaliana
    • Seo, M., Akaba, S., Oritani, T., Delarue, M., Bellini, C., Caboche, M., and Koshiba, T. (1998) Higher activity of an aldehyde oxidase in the auxin-overproducing superroot1 mutant of Arabidopsis thaliana. Plant Physiol. 116, 687-693
    • (1998) Plant Physiol. , vol.116 , pp. 687-693
    • Seo, M.1    Akaba, S.2    Oritani, T.3    Delarue, M.4    Bellini, C.5    Caboche, M.6    Koshiba, T.7
  • 12
    • 0030967046 scopus 로고    scopus 로고
    • Conversion of indole-3-acetaldehyde to indole-3-acetic acid in cell-wall fraction of barley (Hordeum vulgare) seedlings
    • Tsurusaki, K., Takeda, K., and Sakurai, N. (1997) Conversion of indole-3-acetaldehyde to indole-3-acetic acid in cell-wall fraction of barley (Hordeum vulgare) seedlings. Plant Cell Physiol. 38, 268-273
    • (1997) Plant Cell Physiol. , vol.38 , pp. 268-273
    • Tsurusaki, K.1    Takeda, K.2    Sakurai, N.3
  • 13
    • 0000981896 scopus 로고
    • Reduced accumulation of ABA during water stress in a molybdenum cofactor mutant of barley
    • Walker-Simmons, M., Kudrna, D.A., and Warner, R.L. (1989) Reduced accumulation of ABA during water stress in a molybdenum cofactor mutant of barley. Plant Physiol. 90, 728-733
    • (1989) Plant Physiol. , vol.90 , pp. 728-733
    • Walker-Simmons, M.1    Kudrna, D.A.2    Warner, R.L.3
  • 14
    • 0029141442 scopus 로고
    • Molybdenum cofactor mutants, specifically impaired in xanthine dehydrogenase activity and abscisic acid biosynthesis, simultaneously overexpress nitrate reductase
    • Leydecker, M.-T., Moureaux, T., Kraepiel, Y., Schnorr, K., and Caboche, M. (1995) Molybdenum cofactor mutants, specifically impaired in xanthine dehydrogenase activity and abscisic acid biosynthesis, simultaneously overexpress nitrate reductase. Plant Physiol. 107, 1427-1431
    • (1995) Plant Physiol. , vol.107 , pp. 1427-1431
    • Leydecker, M.-T.1    Moureaux, T.2    Kraepiel, Y.3    Schnorr, K.4    Caboche, M.5
  • 15
    • 0030926247 scopus 로고    scopus 로고
    • Tomato flacca mutant is impaired in ABA aldehyde oxidase and xanthine dehydrogenase activities
    • Marin, E. and Marion-Poll, A. (1997) Tomato flacca mutant is impaired in ABA aldehyde oxidase and xanthine dehydrogenase activities. Plant Physiol. Biochem. 35, 369-372
    • (1997) Plant Physiol. Biochem. , vol.35 , pp. 369-372
    • Marin, E.1    Marion-Poll, A.2
  • 16
  • 17
    • 0032463418 scopus 로고    scopus 로고
    • Aldehyde oxidase in wild type and aba1 mutant leaves of Nicotiana plumbaginifolia
    • Akaba, S., Leydecker, M.-T., Moureaux, T., Oritani, T., and Koshiba, T. (1998) Aldehyde oxidase in wild type and aba1 mutant leaves of Nicotiana plumbaginifolia. Plant Cell Physiol. 39, 1281-1286
    • (1998) Plant Cell Physiol. , vol.39 , pp. 1281-1286
    • Akaba, S.1    Leydecker, M.-T.2    Moureaux, T.3    Oritani, T.4    Koshiba, T.5
  • 18
    • 0032791490 scopus 로고    scopus 로고
    • Aldehyde oxidase and xanthine dehydrogenase in a flacca tomato mutant with deficient abscisic acid and wilty phenotype
    • Sagi, M., Fluhr, R., and Lips, S.H. (1999) Aldehyde oxidase and xanthine dehydrogenase in a flacca tomato mutant with deficient abscisic acid and wilty phenotype. Plant Physiol. 120, 571-577
    • (1999) Plant Physiol. , vol.120 , pp. 571-577
    • Sagi, M.1    Fluhr, R.2    Lips, S.H.3
  • 19
    • 0030920524 scopus 로고    scopus 로고
    • Cloning and molecular characterization of plant aldehyde oxidase
    • Sekimoto, H., Seo, M., Dohmae, N., Takio, K., Kamiya, Y., and Koshiba, T. (1997) Cloning and molecular characterization of plant aldehyde oxidase. J. Biol. Chem. 272, 15280-15285
    • (1997) J. Biol. Chem. , vol.272 , pp. 15280-15285
    • Sekimoto, H.1    Seo, M.2    Dohmae, N.3    Takio, K.4    Kamiya, Y.5    Koshiba, T.6
  • 20
    • 15644377647 scopus 로고    scopus 로고
    • TAO1, a representative of the molybdenum cofactor containing hydroxylases from tomato
    • Ori, N., Eshed, Y., Pinto, P., Paran, I., Zamir, D., and Fluhr, R. (1997) TAO1, a representative of the molybdenum cofactor containing hydroxylases from tomato. J. Biol. Chem. 272, 1019-1025
    • (1997) J. Biol. Chem. , vol.272 , pp. 1019-1025
    • Ori, N.1    Eshed, Y.2    Pinto, P.3    Paran, I.4    Zamir, D.5    Fluhr, R.6
  • 22
    • 0345411380 scopus 로고    scopus 로고
    • Production of homo-and hetero-dimeric isozymes from two aldehyde oxidase genes of Arabidopsis thaliana
    • Akaba, S., Seo, M., Dohmae, N., Takio, K., Sekimoto, H., Kamiya, Y., Furuya, N., Komano, T., and Koshiba, T. (1999) Production of homo-and hetero-dimeric isozymes from two aldehyde oxidase genes of Arabidopsis thaliana. J. Biochem. 126, 395-401
    • (1999) J. Biochem. , vol.126 , pp. 395-401
    • Akaba, S.1    Seo, M.2    Dohmae, N.3    Takio, K.4    Sekimoto, H.5    Kamiya, Y.6    Furuya, N.7    Komano, T.8    Koshiba, T.9
  • 23
    • 0023665902 scopus 로고
    • An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs
    • Kozak, M. (1987) An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res. 15, 8125-8132
    • (1987) Nucleic Acids Res. , vol.15 , pp. 8125-8132
    • Kozak, M.1
  • 25
    • 0001431311 scopus 로고
    • Hepatic aldehyde oxidase. I. Purification and properties
    • Rajagopalan, K.V., Fridovich, I., and Handler, P. (1962) Hepatic aldehyde oxidase. I. Purification and properties. J. Biol. Chem. 237, 922-928
    • (1962) J. Biol. Chem. , vol.237 , pp. 922-928
    • Rajagopalan, K.V.1    Fridovich, I.2    Handler, P.3
  • 27
    • 0022344589 scopus 로고
    • Guinea pig liver aldehyde oxidase as a sulfoxide reductase: Its purification and characterization
    • Yoshihara, S. and Tatsumi, K. (1985) Guinea pig liver aldehyde oxidase as a sulfoxide reductase: its purification and characterization. Arch. Biochem. Biophys. 242, 213-224
    • (1985) Arch. Biochem. Biophys. , vol.242 , pp. 213-224
    • Yoshihara, S.1    Tatsumi, K.2
  • 28
    • 0032950253 scopus 로고    scopus 로고
    • Aldehyde oxidase in roots, leaves and seeds of barley (Hordeum vulgare L.)
    • Omarov, R.T., Akaba, S., Koshiba, T., and Lips, S.H. (1999) Aldehyde oxidase in roots, leaves and seeds of barley (Hordeum vulgare L.). J. Exp. Bot. 50, 63-69
    • (1999) J. Exp. Bot. , vol.50 , pp. 63-69
    • Omarov, R.T.1    Akaba, S.2    Koshiba, T.3    Lips, S.H.4
  • 29
    • 0030095876 scopus 로고    scopus 로고
    • Identification in vitro of a post-translational regulatory site in the hinge 1 region of Arabidopsis nitrate reductase
    • Su, W., Huber, S.C., and Crawford, N.M. (1996) Identification in vitro of a post-translational regulatory site in the hinge 1 region of Arabidopsis nitrate reductase. Plant Cell 8, 519-527
    • (1996) Plant Cell , vol.8 , pp. 519-527
    • Su, W.1    Huber, S.C.2    Crawford, N.M.3
  • 30
    • 0031277446 scopus 로고    scopus 로고
    • Analysis of wild-type and mutant plant nitrate reductase expressed in the methylotrophic yeast Pichia pastoris
    • Su, W., Mertens, J.A., Kanamaru, K., Campbell, W.H., and Crawford, N.M. (1997) Analysis of wild-type and mutant plant nitrate reductase expressed in the methylotrophic yeast Pichia pastoris. Plant Physiol. 115, 1135-1143
    • (1997) Plant Physiol. , vol.115 , pp. 1135-1143
    • Su, W.1    Mertens, J.A.2    Kanamaru, K.3    Campbell, W.H.4    Crawford, N.M.5
  • 31
    • 0029876533 scopus 로고    scopus 로고
    • Site-directed mutagenesis of recombinant sulfite oxidase
    • Garrett, R.M. and Rajagopalan, K.V. (1996) Site-directed mutagenesis of recombinant sulfite oxidase. J. Biol. Chem. 271, 7387-7391
    • (1996) J. Biol. Chem. , vol.271 , pp. 7387-7391
    • Garrett, R.M.1    Rajagopalan, K.V.2
  • 32
    • 0033560621 scopus 로고    scopus 로고
    • Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit and mouse livers and functional expression of recombinant mouse retinal oxidase cDNA in Escherichia coli
    • Huang, D.-Y., Furukawa, A., and Ichikawa, Y. (1999) Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit and mouse livers and functional expression of recombinant mouse retinal oxidase cDNA in Escherichia coli. Arch. Biochem. Biophys. 364, 264-272
    • (1999) Arch. Biochem. Biophys. , vol.364 , pp. 264-272
    • Huang, D.-Y.1    Furukawa, A.2    Ichikawa, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.