메뉴 건너뛰기




Volumn 380, Issue 1, 2004, Pages 121-130

Catalytic reaction of cytokinin dehydrogenase: Preference for quinones as electron acceptors

Author keywords

Cytokinin; Cytokinin dehydrogenase (cytokinin oxidase); Flavoprotein; Plant hormone metabolism; Quinone

Indexed keywords

BIODEGRADATION; CATALYSIS; ELECTRONS; ENZYMES; PHYSIOLOGY;

EID: 2642524422     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031813     Document Type: Article
Times cited : (67)

References (42)
  • 2
    • 0036071642 scopus 로고    scopus 로고
    • New insights into the functions of cytokinins in plant development
    • Schmülling, T. (2002) New insights into the functions of cytokinins in plant development. J. Plant Growth Regul. 21, 40-49
    • (2002) J. Plant Growth Regul. , vol.21 , pp. 40-49
    • Schmülling, T.1
  • 3
    • 0027947902 scopus 로고
    • Cytokinin oxidase: Biochemical features and physiological significance
    • Hare, P. D. and van Staden, J. (1994) Cytokinin oxidase: biochemical features and physiological significance. Physiol. Plant. 91, 128-136
    • (1994) Physiol. Plant. , vol.91 , pp. 128-136
    • Hare, P.D.1    Van Staden, J.2
  • 4
    • 0034832289 scopus 로고    scopus 로고
    • Cytokinin oxidase or dehydrogenase? Mechanism of the cytokinin degradation in plants
    • Galuszka, P., Frébort, I., Šebela, M., Sauer, P., Jacobsen, S. and Peč, P. (2001) Cytokinin oxidase or dehydrogenase? Mechanism of the cytokinin degradation in plants. Eur. J. Biochem. 268, 450-461
    • (2001) Eur. J. Biochem. , vol.268 , pp. 450-461
    • Galuszka, P.1    Frébort, I.2    Šebela, M.3    Sauer, P.4    Jacobsen, S.5    Peč, P.6
  • 6
    • 0141457619 scopus 로고    scopus 로고
    • Rate enhancement of cytokinin oxidase/dehydrogenase using 2,6-dichloroindophenol as an electron acceptor
    • Laskey, J. G., Patterson, P., Bilyeu, K. D. and Morris, R. O. (2003) Rate enhancement of cytokinin oxidase/dehydrogenase using 2,6-dichloroindophenol as an electron acceptor. Plant Growth Regul. 40, 189-196
    • (2003) Plant Growth Regul. , vol.40 , pp. 189-196
    • Laskey, J.G.1    Patterson, P.2    Bilyeu, K.D.3    Morris, R.O.4
  • 8
    • 0034461290 scopus 로고    scopus 로고
    • Degradation of cytokinins by cytokinin oxidases in plants
    • Galuszka, P., Frébort, I., Šebela, M. and Peč, P. (2000) Degradation of cytokinins by cytokinin oxidases in plants. Plant Growth Reg. 32, 315-327
    • (2000) Plant Growth Reg. , vol.32 , pp. 315-327
    • Galuszka, P.1    Frébort, I.2    Šebela, M.3    Peč, P.4
  • 10
    • 0040370514 scopus 로고    scopus 로고
    • Cytokinin oxidase from Zea mays: Purification, cDNA cloning and expression in moss protoplasts
    • Houba-Herin, N., Pethe, C., d'Alayer, J. and Laloue, M. (1999) Cytokinin oxidase from Zea mays: purification, cDNA cloning and expression in moss protoplasts. Plant J. 17, 615-626
    • (1999) Plant J. , vol.17 , pp. 615-626
    • Houba-Herin, N.1    Pethe, C.2    D'Alayer, J.3    Laloue, M.4
  • 12
    • 0345445907 scopus 로고    scopus 로고
    • Cytokinin-deficienf transgenic Arabidopsis plants show multiple developmental alterations indicating opposite functions of cytokinins in the regulation of shoot and root meristem activity
    • Werner, T., Motyka, V., Laucou, V., Smets, R., van Onckelen, H. and Schmülling, T. (2003) Cytokinin-deficienf transgenic Arabidopsis plants show multiple developmental alterations indicating opposite functions of cytokinins in the regulation of shoot and root meristem activity. Plant Cell 15, 1-20
    • (2003) Plant Cell , vol.15 , pp. 1-20
    • Werner, T.1    Motyka, V.2    Laucou, V.3    Smets, R.4    Van Onckelen, H.5    Schmülling, T.6
  • 13
    • 0036718725 scopus 로고    scopus 로고
    • Isolation and characterization of the orchid cytokinin oxidase DSCKX1 promoter
    • Yang, S. H., Yu, H. and Goh, C. J. (2002) Isolation and characterization of the orchid cytokinin oxidase DSCKX1 promoter. J. Exp. Bot. 53, 1899-1907
    • (2002) J. Exp. Bot. , vol.53 , pp. 1899-1907
    • Yang, S.H.1    Yu, H.2    Goh, C.J.3
  • 14
    • 0037278822 scopus 로고    scopus 로고
    • Functional characterisation of a cytokinin oxidase gene DSCKX1 in Dendrobium orchid
    • Yang, S. H., Yu, H. and Goh, C. J. (2003) Functional characterisation of a cytokinin oxidase gene DSCKX1 in Dendrobium orchid. Plant. Mol. Biol. 51, 237-248
    • (2003) Plant. Mol. Biol. , vol.51 , pp. 237-248
    • Yang, S.H.1    Yu, H.2    Goh, C.J.3
  • 15
  • 16
    • 0029200625 scopus 로고
    • Cytokinin oxidase - Purification by affinity chromatography and activation by caffeic acid
    • Wang, J. and Letham, D. S. (1995) Cytokinin oxidase - purification by affinity chromatography and activation by caffeic acid. Plant Sci. 112, 161-166
    • (1995) Plant Sci. , vol.112 , pp. 161-166
    • Wang, J.1    Letham, D.S.2
  • 17
    • 0030463345 scopus 로고    scopus 로고
    • Differential pulse polarographic study of the redox centres in pea amine oxidase
    • Šebela, M., Studničková, M. and Wimmerová, M. (1996) Differential pulse polarographic study of the redox centres in pea amine oxidase, Bioelectrochem. Bioenerget. 41, 173-179
    • (1996) Bioelectrochem. Bioenerget. , vol.41 , pp. 173-179
    • Šebela, M.1    Studničková, M.2    Wimmerová, M.3
  • 18
    • 0002435359 scopus 로고
    • A simple method for the determination of redox potentials
    • Curti, B., Ronchi, S. and Zanetti, G., eds., de Gruyter, Berlin
    • Massey, V. (1991) A simple method for the determination of redox potentials. In Flavins and Flavoproteins 1990 (Curti, B., Ronchi, S. and Zanetti, G., eds.), pp. 59-66, de Gruyter, Berlin
    • (1991) Flavins and Flavoproteins 1990 , pp. 59-66
    • Massey, V.1
  • 19
    • 0023663982 scopus 로고
    • Redox properties of electron-transferring flavoprotein from Megasphaera elsdenii
    • Pace, C. P. and Stankovich, M. T. (1987) Redox properties of electron-transferring flavoprotein from Megasphaera elsdenii. Biochim. Biophys. Acta 911, 267-276
    • (1987) Biochim. Biophys. Acta , vol.911 , pp. 267-276
    • Pace, C.P.1    Stankovich, M.T.2
  • 20
    • 0035916251 scopus 로고    scopus 로고
    • Stopped-flow kinetic studies of flavin reduction in human cytochrome P450 reductase and its component domains
    • Gutierrez, A., Lian, L.-Y., Wolf, C. R., Scrutton, N. S. and Roberts, C. K. G. (2001) Stopped-flow kinetic studies of flavin reduction in human cytochrome P450 reductase and its component domains. Biochemistry 40, 1964-1975
    • (2001) Biochemistry , vol.40 , pp. 1964-1975
    • Gutierrez, A.1    Lian, L.-Y.2    Wolf, C.R.3    Scrutton, N.S.4    Roberts, C.K.G.5
  • 23
    • 2642530621 scopus 로고
    • Simultaneous determination of peroxidase and catalase activities using modified guaiacol method
    • Bratislava
    • Haviger, A., Peč, P. and Frébort, I. (1991) Simultaneous determination of peroxidase and catalase activities using modified guaiacol method. Biológia (Bratislava) 46, 337-343
    • (1991) Biológia , vol.46 , pp. 337-343
    • Haviger, A.1    Peč, P.2    Frébort, I.3
  • 24
    • 0031571165 scopus 로고    scopus 로고
    • Identification of the colored guaiacol oxidation product produced by peroxidases
    • Doerge, D. R., Divi, R. L. and Churchwell, M. I. (1997) Identification of the colored guaiacol oxidation product produced by peroxidases. Anal. Biochem. 250, 10-17
    • (1997) Anal. Biochem. , vol.250 , pp. 10-17
    • Doerge, D.R.1    Divi, R.L.2    Churchwell, M.I.3
  • 25
    • 0033544926 scopus 로고    scopus 로고
    • Covalent flavinylation is essential tor efficient redox catalysis in vanillyl-alcohol oxidase
    • Fraaije, M. W., van den Heuvel, R. H. H., van Berkel, W. J. H. and Mattevi, A. (1999) Covalent flavinylation is essential tor efficient redox catalysis in vanillyl-alcohol oxidase. J. Biol. Chem. 274, 35514-35520
    • (1999) J. Biol. Chem. , vol.274 , pp. 35514-35520
    • Fraaije, M.W.1    Van Den Heuvel, R.H.H.2    Van Berkel, W.J.H.3    Mattevi, A.4
  • 26
    • 0035839498 scopus 로고    scopus 로고
    • Oxygen access to the active site of cholesterol oxidase through a narrow channel is gated by an Arg-Glu pair
    • Coulombe, R., Yue, K. Q., Ghisla, S. and Vrielink, A. (2001) Oxygen access to the active site of cholesterol oxidase through a narrow channel is gated by an Arg-Glu pair. J. Biol. Chem. 276, 30435-30441
    • (2001) J. Biol. Chem. , vol.276 , pp. 30435-30441
    • Coulombe, R.1    Yue, K.Q.2    Ghisla, S.3    Vrielink, A.4
  • 27
    • 0002096286 scopus 로고
    • Cytokinin oxidase and the regulation of cytokinin degradation
    • Mok, D. W. S. and Mok, M. C., eds., CRC Press, Boca Raton, FL
    • Armstrong, D. J. (1994) Cytokinin oxidase and the regulation of cytokinin degradation. In Cytokinins: Chemistry, Activity and Function (Mok, D. W. S. and Mok, M. C., eds.), pp. 139-154, CRC Press, Boca Raton, FL
    • (1994) Cytokinins: Chemistry, Activity and Function , pp. 139-154
    • Armstrong, D.J.1
  • 28
    • 0013954466 scopus 로고
    • On the existence of spectrally distinct classes of flavoprotein semiquinones. A new method for the quantitative production of flavoprotein semiquinones
    • Massey, V. and Palmer, G. (1966) On the existence of spectrally distinct classes of flavoprotein semiquinones. A new method for the quantitative production of flavoprotein semiquinones. Biochemistry 5, 3181-3189
    • (1966) Biochemistry , vol.5 , pp. 3181-3189
    • Massey, V.1    Palmer, G.2
  • 29
    • 0033609440 scopus 로고    scopus 로고
    • The intraflavin hydrogen bond in human electron transfer flavoprotein modulates redox potentials and may participate in electron transfer
    • Dwyer, T. M., Mortl, S., Kemter, K., Bacher, A., Fauq, A. and Frerman, F. E. (1999) The intraflavin hydrogen bond in human electron transfer flavoprotein modulates redox potentials and may participate in electron transfer. Biochemistry 38, 9735-9745
    • (1999) Biochemistry , vol.38 , pp. 9735-9745
    • Dwyer, T.M.1    Mortl, S.2    Kemter, K.3    Bacher, A.4    Fauq, A.5    Frerman, F.E.6
  • 30
    • 0035923397 scopus 로고    scopus 로고
    • The presence of a hydrogen bond between asparagine 485 and the π system of FAD modulates the redox potential in the reaction catalyzed by cholesterol oxidase
    • Yin, Y., Sampson, N. S., Vrielink, A. and Lario, P. I. (2001) The presence of a hydrogen bond between asparagine 485 and the π system of FAD modulates the redox potential in the reaction catalyzed by cholesterol oxidase. Biochemistry 40, 13779-13787
    • (2001) Biochemistry , vol.40 , pp. 13779-13787
    • Yin, Y.1    Sampson, N.S.2    Vrielink, A.3    Lario, P.I.4
  • 31
    • 0030739371 scopus 로고    scopus 로고
    • Catalytic mechanism of the oxidative demethylation of 4-(methoxymethyl)phenol by vanillyl-alcohol oxidase
    • Fraaije, M. W. and van Berkel, W. J. H. (1997) Catalytic mechanism of the oxidative demethylation of 4-(methoxymethyl)phenol by vanillyl-alcohol oxidase. J. Biol. Chem. 272, 18111-18116
    • (1997) J. Biol. Chem. , vol.272 , pp. 18111-18116
    • Fraaije, M.W.1    Van Berkel, W.J.H.2
  • 34
    • 0033605220 scopus 로고    scopus 로고
    • Refined crystal structures of reaction centres from Rhodopseudomonas viridis in complexes with the herbicide atrazine and two chiral atrazine derivatives also lead to a new model of the bound carotenoid
    • Lancaster, C. R. and Michel, H. (1999) Refined crystal structures of reaction centres from Rhodopseudomonas viridis in complexes with the herbicide atrazine and two chiral atrazine derivatives also lead to a new model of the bound carotenoid. J. Mol. Biol. 286, 883-898
    • (1999) J. Mol. Biol. , vol.286 , pp. 883-898
    • Lancaster, C.R.1    Michel, H.2
  • 36
    • 0034161331 scopus 로고    scopus 로고
    • Flavoenzymes: Diverse catalysts with recurrent features
    • Fraaije, M. W. and Mattevi, A. (2000) Flavoenzymes: diverse catalysts with recurrent features. Trends Biochem. Sci. 25, 126-132
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 126-132
    • Fraaije, M.W.1    Mattevi, A.2
  • 37
    • 0034662927 scopus 로고    scopus 로고
    • The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme
    • Dym, O., Pratt, E. A., Ho, C. and Eisenberg, D. (2000) The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme. Proc. Natl. Acad. Sci. U.S.A. 97, 9413-9418
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 9413-9418
    • Dym, O.1    Pratt, E.A.2    Ho, C.3    Eisenberg, D.4
  • 38
    • 0029056202 scopus 로고
    • An enzyme-substrate complex involved in bacterial cell wall biosynthesis
    • Benson, T. E., Filman, D. J., Walsh, C. T. and Hogle, J. M. (1995) An enzyme-substrate complex involved in bacterial cell wall biosynthesis. Nat. Struct. Biol. 2, 644-653
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 644-653
    • Benson, T.E.1    Filman, D.J.2    Walsh, C.T.3    Hogle, J.M.4
  • 39
    • 0037025299 scopus 로고    scopus 로고
    • Structure-function relationships in flavoenzyme-dependent amine oxidations: A comparison of polyamine oxidase and monoamine oxidase
    • Binda, C., Mattevi, A. and Edmondson, D. E. (2003) Structure-function relationships in flavoenzyme-dependent amine oxidations: a comparison of polyamine oxidase and monoamine oxidase. J. Biol. Chem. 277, 23973-23976
    • (2003) J. Biol. Chem. , vol.277 , pp. 23973-23976
    • Binda, C.1    Mattevi, A.2    Edmondson, D.E.3
  • 40
    • 0029729048 scopus 로고    scopus 로고
    • Changes in cytokinin content and cytokinin oxidase activity in response to de-repression of ipt gene transcription in transgenic tobacco calli and plants
    • Motyka, V., Faiss, M., Strnad, M., Kamínek, M. and Schmülling, T. (1996) Changes in cytokinin content and cytokinin oxidase activity in response to de-repression of ipt gene transcription in transgenic tobacco calli and plants. Plant Physiol. 112, 1035-1043
    • (1996) Plant Physiol. , vol.112 , pp. 1035-1043
    • Motyka, V.1    Faiss, M.2    Strnad, M.3    Kamínek, M.4    Schmülling, T.5
  • 41
    • 0038014307 scopus 로고    scopus 로고
    • Cytokinin-induced upregulation of cytokinin oxidase activity in tobacco includes changes in enzyme glycosylation and secretion
    • Motyka, V., Vaňková, R., Čapková, R., Petrášek, J., Kamínek, M. and Schmülling, T. (2003) Cytokinin-induced upregulation of cytokinin oxidase activity in tobacco includes changes in enzyme glycosylation and secretion. Physiol. Plant. 117, 11-21
    • (2003) Physiol. Plant. , vol.117 , pp. 11-21
    • Motyka, V.1    Vaňková, R.2    Čapková, R.3    Petrášek, J.4    Kamínek, M.5    Schmülling, T.6
  • 42
    • 0037355587 scopus 로고    scopus 로고
    • Dynamics of expression and distribution of cytokinin oxidase/ dehydrogenase in developing maize kernels
    • Bilyeu, K. D., Laskey, J. G. and Morris, R. O. (2003) Dynamics of expression and distribution of cytokinin oxidase/dehydrogenase in developing maize kernels. Plant Growth Regul. 39, 195-203
    • (2003) Plant Growth Regul. , vol.39 , pp. 195-203
    • Bilyeu, K.D.1    Laskey, J.G.2    Morris, R.O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.