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Volumn 9, Issue 11, 2004, Pages 515-517

Carotenoid hydroxylation - P450 finally!

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EID: 6944227962     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tplants.2004.09.001     Document Type: Short Survey
Times cited : (27)

References (24)
  • 1
    • 0003357909 scopus 로고    scopus 로고
    • Cytochromes P450
    • C.R. Somerville E.M., Meyerowitz 10.1199/tab.0028
    • D. Werck-Reichhart Cytochromes P450 C.R. Somerville E.M., Meyerowitz The Arabidopsis Book 2002 10.1199/tab.0028 (www.aspb.org)
    • (2002) The Arabidopsis Book
    • Werck-Reichhart, D.1
  • 4
    • 4344702728 scopus 로고    scopus 로고
    • Progress in understanding the origin and functions of carotenoid hydroxylases in plants
    • L. Tian, and D. DellaPenna Progress in understanding the origin and functions of carotenoid hydroxylases in plants Arch. Biochem. Biophys. 430 2004 22 29
    • (2004) Arch. Biochem. Biophys. , vol.430 , pp. 22-29
    • Tian, L.1    Dellapenna, D.2
  • 5
    • 0001887923 scopus 로고    scopus 로고
    • Overview of carotenoid biosynthesis
    • G. Briton Birkhäuser*et al.
    • G. Britton Overview of carotenoid biosynthesis G. Briton Carotenoids: Biosynthesis and Metabolism 1998 Birkhäuser 13 147
    • (1998) Carotenoids: Biosynthesis and Metabolism , pp. 13-147
    • Britton, G.1
  • 6
    • 0029784478 scopus 로고    scopus 로고
    • Cloning and functional analysis of the β-carotene hydroxylase of Arabidopsis thaliana
    • Z. Sun Cloning and functional analysis of the β-carotene hydroxylase of Arabidopsis thaliana J. Biol. Chem. 271 1996 24349 24352
    • (1996) J. Biol. Chem. , vol.271 , pp. 24349-24352
    • Sun, Z.1
  • 7
    • 0032557139 scopus 로고    scopus 로고
    • Xanthophyll biosynthesis: Molecular and functional characterization of carotenoid hydroxylases from pepper fruits (Capsicum annuum L.)
    • F. Bouvier Xanthophyll biosynthesis: molecular and functional characterization of carotenoid hydroxylases from pepper fruits (Capsicum annuum L.) Biochim. Biophys. Acta 1391 1998 320 328
    • (1998) Biochim. Biophys. Acta , vol.1391 , pp. 320-328
    • Bouvier, F.1
  • 9
    • 0035984372 scopus 로고    scopus 로고
    • Expression of a bacterial carotene hydroxylase gene (crtZ) enhances UV tolerance in tobacco
    • T. Gotz Expression of a bacterial carotene hydroxylase gene (crtZ) enhances UV tolerance in tobacco Plant Mol. Biol. 50 2002 129 142
    • (2002) Plant Mol. Biol. , vol.50 , pp. 129-142
    • Gotz, T.1
  • 10
    • 0037062998 scopus 로고    scopus 로고
    • Overexpression of β-carotene hydroxylase enhances stress tolerance in Arabidopsis
    • P.A. Davison Overexpression of β-carotene hydroxylase enhances stress tolerance in Arabidopsis Nature 418 2002 203 206
    • (2002) Nature , vol.418 , pp. 203-206
    • Davison, P.A.1
  • 11
    • 0346458625 scopus 로고    scopus 로고
    • The Arabidopsis LUT1 locus encodes a member of the cytochrome P450 family that is required for carotenoid ε-ring hydroxylation activity
    • L. Tian The Arabidopsis LUT1 locus encodes a member of the cytochrome P450 family that is required for carotenoid ε-ring hydroxylation activity Proc. Natl. Acad. Sci. U. S. A. 101 2004 402 407
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 402-407
    • Tian, L.1
  • 12
    • 0030249497 scopus 로고    scopus 로고
    • Arabidopsis carotenoid mutants demonstrate that lutein is not essential for photosynthesis in higher plants
    • B. Pogson Arabidopsis carotenoid mutants demonstrate that lutein is not essential for photosynthesis in higher plants Plant Cell 8 1996 1627 1639
    • (1996) Plant Cell , vol.8 , pp. 1627-1639
    • Pogson, B.1
  • 13
    • 0034813551 scopus 로고    scopus 로고
    • Characterization of a second carotenoid β-hydroxylase gene from Arabidopsis and its relationship to the LUT1 locus
    • L. Tian, and D. DellaPenna Characterization of a second carotenoid β-hydroxylase gene from Arabidopsis and its relationship to the LUT1 locus Plant Mol. Biol. 47 2001 379 388
    • (2001) Plant Mol. Biol. , vol.47 , pp. 379-388
    • Tian, L.1    Dellapenna, D.2
  • 14
    • 0035144016 scopus 로고    scopus 로고
    • Tomato allene oxide synthase and fatty acid hydroperoxide lyase, two cytochrome P450s involved in oxylipin metabolism, are targeted to different membranes of chloroplast envelope
    • J.E. Froehlich Tomato allene oxide synthase and fatty acid hydroperoxide lyase, two cytochrome P450s involved in oxylipin metabolism, are targeted to different membranes of chloroplast envelope Plant Physiol. 125 2001 306 317
    • (2001) Plant Physiol. , vol.125 , pp. 306-317
    • Froehlich, J.E.1
  • 15
    • 0034836395 scopus 로고    scopus 로고
    • Localization of CYP86B1 in the outer envelope of chloroplasts
    • C.J. Watson Localization of CYP86B1 in the outer envelope of chloroplasts Plant Cell Physiol. 42 2001 873 878
    • (2001) Plant Cell Physiol. , vol.42 , pp. 873-878
    • Watson, C.J.1
  • 16
    • 3042607977 scopus 로고    scopus 로고
    • CYP175A1 from Thermus thermophilus HB27, the first β-carotene hydroxylase of the P450 superfamily
    • F. Blasco CYP175A1 from Thermus thermophilus HB27, the first β-carotene hydroxylase of the P450 superfamily Appl. Microbiol. Biotechnol. 64 2004 671 674
    • (2004) Appl. Microbiol. Biotechnol. , vol.64 , pp. 671-674
    • Blasco, F.1
  • 17
    • 0007440158 scopus 로고
    • The stereochemistry of hydroxylation of the carotenoid lutein in Calendula officinalis
    • B.V. Milborrow The stereochemistry of hydroxylation of the carotenoid lutein in Calendula officinalis Phytochemistry 21 1982 2853 2857
    • (1982) Phytochemistry , vol.21 , pp. 2853-2857
    • Milborrow, B.V.1
  • 18
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • O. Emanuelsson Predicting subcellular localization of proteins based on their N-terminal amino acid sequence J. Mol. Biol. 300 2000 1005 1016
    • (2000) J. Mol. Biol. , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1
  • 19
    • 0033593034 scopus 로고    scopus 로고
    • BAS1: A gene regulating brassinosteroid levels and light responsiveness in Arabidopsis
    • M.M. Neff BAS1: A gene regulating brassinosteroid levels and light responsiveness in Arabidopsis Proc. Natl. Acad. Sci. U. S. A. 96 1999 15316 15323
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 15316-15323
    • Neff, M.M.1
  • 20
    • 0032562078 scopus 로고    scopus 로고
    • CYP86A1 from Arabidopsis thaliana encodes a cytochrome P450-dependent fatty acid omega-hydroxylase
    • I. Benveniste CYP86A1 from Arabidopsis thaliana encodes a cytochrome P450-dependent fatty acid omega-hydroxylase Biochem. Biophys. Res. Commun. 243 1998 688 693
    • (1998) Biochem. Biophys. Res. Commun. , vol.243 , pp. 688-693
    • Benveniste, I.1
  • 21
    • 0035859901 scopus 로고    scopus 로고
    • Functional analysis of the LACERATA gene of Arabidopsis provides evidence for different roles of fatty acid omega-hydroxylation in development
    • K. Wellesen Functional analysis of the LACERATA gene of Arabidopsis provides evidence for different roles of fatty acid omega-hydroxylation in development Proc. Natl. Acad. Sci. U. S. A. 98 2001 9694 9699
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 9694-9699
    • Wellesen, K.1
  • 22
    • 0031105483 scopus 로고    scopus 로고
    • Isolation of a cDNA and a genomic clone encoding cinnamate 4-hydroxylase from Arabidopsis and its expression manner in planta
    • M. Mizutani Isolation of a cDNA and a genomic clone encoding cinnamate 4-hydroxylase from Arabidopsis and its expression manner in planta Plant Physiol. 113 1997 755 763
    • (1997) Plant Physiol. , vol.113 , pp. 755-763
    • Mizutani, M.1
  • 23
    • 0033621061 scopus 로고    scopus 로고
    • New routes for lignin biosynthesis defined by biochemical characterization of recombinant ferulate 5-hydroxylase, a multifunctional cytochrome P450-dependent monooxygenase
    • J.M. Humphreys New routes for lignin biosynthesis defined by biochemical characterization of recombinant ferulate 5-hydroxylase, a multifunctional cytochrome P450-dependent monooxygenase Proc. Natl. Acad. Sci. U. S. A. 96 1999 10045 10050
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 10045-10050
    • Humphreys, J.M.1
  • 24
    • 2342459125 scopus 로고    scopus 로고
    • The Arabidopsis cytochrome P450 CYP707A encodes ABA 8′- hydroxylases: Key enzymes in ABA catabolism
    • T. Kushiro The Arabidopsis cytochrome P450 CYP707A encodes ABA 8′-hydroxylases: key enzymes in ABA catabolism EMBO J. 23 2004 1647 1656
    • (2004) EMBO J. , vol.23 , pp. 1647-1656
    • Kushiro, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.