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Volumn 91, Issue , 2013, Pages 140-147

Molecular cloning and catalytic activity of a membrane-bound prenyl diphosphate phosphatase from Croton stellatopilosus Ohba

Author keywords

Acyclic diterpenoids; Croton stellatopilosus; Euphorbiaceae; Geranylgeraniol; Molecular cloning; Plaunotol biosynthesis; Prenyl diphosphate phosphatase

Indexed keywords

TRANSFERASE;

EID: 84878941422     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2012.09.010     Document Type: Article
Times cited : (6)

References (34)
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 59149106049 scopus 로고    scopus 로고
    • Phosphatidic acid phosphatase, a key enzyme in the regulation of lipid synthesis
    • G.M. Carman, and G.S. Han Phosphatidic acid phosphatase, a key enzyme in the regulation of lipid synthesis J. Biol. Chem. 284 2009 2593 2597
    • (2009) J. Biol. Chem. , vol.284 , pp. 2593-2597
    • Carman, G.M.1    Han, G.S.2
  • 5
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites
    • O. Emanuelsson, H. Nielsen, and G. von Heijne ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites Protein Sci. 8 1999 978 984 (Pubitemid 29211735)
    • (1999) Protein Science , vol.8 , Issue.5 , pp. 978-984
    • Emanuelsson, O.1    Nielsen, H.2    Von Heijne, G.3
  • 6
    • 0037266613 scopus 로고    scopus 로고
    • Traumatic resin defense in Norway spruce (Picea abies): Methyl jasmonate-induced terpene synthase gene expression, and cDNA cloning and functional characterization of (+)-3-carene synthase
    • DOI 10.1023/A:1020714403780
    • J. Faeldt, D. Martin, B. Miller, S. Rawat, and J. Bohlmann Traumatic resin defense in Norway spruce (Picea abies): Methyl jasmonate-induced terpene synthase gene expression, and cDNA cloning and functional characterization of (+)-3-carene synthase Plant Mol. Biol. 51 2003 119 133 (Pubitemid 36198770)
    • (2003) Plant Molecular Biology , vol.51 , Issue.1 , pp. 119-133
    • Faldt, J.1    Martin, D.2    Miller, B.3    Rawat, S.4    Bohlmann, J.5
  • 7
    • 0033591216 scopus 로고    scopus 로고
    • The LPP1 and DPP1 gene products account for most of the isoprenoid phosphate phosphatase activities in Saccharomyces cerevisiae
    • A. Faulkner, X. Chen, J. Rush, B. Horazdovsky, C.J. Waechter, G.M. Carman, and P.C. Sternweis The LPP1 and DPP1 gene products account for most of the isoprenoid phosphate phosphatase activities in Saccharomyces cerevisiae J. Biol. Chem. 274 1999 14831 14837
    • (1999) J. Biol. Chem. , vol.274 , pp. 14831-14837
    • Faulkner, A.1    Chen, X.2    Rush, J.3    Horazdovsky, B.4    Waechter, C.J.5    Carman, G.M.6    Sternweis, P.C.7
  • 10
    • 0031826040 scopus 로고    scopus 로고
    • SOSUI: Classification and secondary structure prediction system for membrane proteins
    • T. Hirokawa, S. Boon-Chieng, and S. Mitaku SOSUI: Classification and secondary structure prediction system for membrane proteins Bioinformatics 14 1998 378 379 (Pubitemid 28393805)
    • (1998) Bioinformatics , vol.14 , Issue.4 , pp. 378-379
    • Hirokawa, T.1    Boon-Chieng, S.2    Mitaku, S.3
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural protein during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural protein during the assembly of the head of bacteriophage T4 Nature 227 1970 280 285
    • (1970) Nature , vol.227 , pp. 280-285
    • Laemmli, U.K.1
  • 14
    • 0034822927 scopus 로고    scopus 로고
    • Partial characterization of farnesyl and geranylgeranyl diphosphatases induced in rice seedlings by UV-C irradiation
    • J. Nah, S.J. Song, and K. Back Partial characterization of farnesyl and geranylgeranyl diphosphatases induced in rice seedlings by UV-C irradiation Plant Cell Physiol. 42 2001 864 867 (Pubitemid 32897209)
    • (2001) Plant and Cell Physiology , vol.42 , Issue.8 , pp. 864-867
    • Nah, J.1    Song, S.-J.2    Back, K.3
  • 15
    • 35349014055 scopus 로고    scopus 로고
    • Plastidic phosphatidic acid phosphatases identified in a distinct subfamily of lipid phosphate phosphatases with prokaryotic origin
    • DOI 10.1074/jbc.M704385200
    • Y. Nakamura, M. Tsuchiya, and H. Ohta Plastidic phosphatidic acid phosphatases identified in a distinct subfamily of lipid phosphate phosphatases with prokaryotic origin J. Biol. Chem. 282 2007 29013 29021 (Pubitemid 47606041)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.39 , pp. 29013-29021
    • Nakamura, Y.1    Tsuchiya, M.2    Ohta, H.3
  • 16
    • 27744560923 scopus 로고    scopus 로고
    • Geranylgeraniol formation in Croton stellatopilosus proceeds via successive monodephosphorylations of geranylgeranyl diphosphate
    • DOI 10.1016/j.tetlet.2005.10.048, PII S0040403905022653
    • N. Nualkaew, W. De-Eknamkul, T.M. Kutchan, and M.H. Zenk Geranylgeraniol formation in Croton stellatopilosus proceeds via successive monodephosphorylations of geranylgeranyl diphosphate Tetrahedron Lett. 46 2005 8727 8731 (Pubitemid 41617362)
    • (2005) Tetrahedron Letters , vol.46 , Issue.50 , pp. 8727-8731
    • Nualkaew, N.1    De-Eknamkul, W.2    Kutchan, T.M.3    Zenk, M.H.4
  • 17
    • 33747407026 scopus 로고    scopus 로고
    • Membrane-bound geranylgeranyl diphosphate phosphatases: Purification and characterization from Croton stellatopilosus leaves
    • DOI 10.1016/j.phytochem.2005.12.014, PII S0031942205007107
    • N. Nualkaew, W. De-Eknamkul, T.M. Kutchan, and M.H. Zenk Membrane-bound geranylgeranyl diphosphate phosphatases: Purification and characterization from Croton stellatopilosus leaves Phytochemistry 67 2006 1613 1620 (Pubitemid 44251218)
    • (2006) Phytochemistry , vol.67 , Issue.15 , pp. 1613-1620
    • Nualkaew, N.1    De-Eknamkul, W.2    Kutchan, T.M.3    Zenk, M.H.4
  • 18
    • 0018117277 scopus 로고
    • Isolation and structure of antipeptic ulcer diterpene from Thai medicinal plant
    • A. Ogiso, E. Kitazawa, M. Kurabayashi, A. Sato, S. Takahashi, H. Noguchi, H. Kuwano, S. Kobayashi, and H. Mishima Isolation and structure of antipeptic ulcer diterpene from Thai medicinal plant Chem. Pharm. Bull. 26 1978 3117 3123 (Pubitemid 9050300)
    • (1978) Chemical and Pharmaceutical Bulletin , vol.26 , Issue.10 , pp. 3117-3123
    • Ogiso, A.1    Kitazawa, E.2    Kurabayashi, M.3
  • 19
  • 21
    • 0001111218 scopus 로고
    • Terpenoids and an apocarotenoid from seeds of Bixa orellana
    • G. Pattenden, and I.J.O. Jondiko Terpenoids and an apocarotenoid from seeds of Bixa orellana Phytochemistry 28 1989 3159 3162
    • (1989) Phytochemistry , vol.28 , pp. 3159-3162
    • Pattenden, G.1    Jondiko, I.J.O.2
  • 22
    • 0003703945 scopus 로고
    • Hydrolysis of allylic phosphates by enzymes from the flavedo of Citrus sinensis
    • L.M. Perez, G. Taucher, and O. Cori Hydrolysis of allylic phosphates by enzymes from the flavedo of Citrus sinensis Phytochemistry 19 1980 183 187
    • (1980) Phytochemistry , vol.19 , pp. 183-187
    • Perez, L.M.1    Taucher, G.2    Cori, O.3
  • 23
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: Discriminating signal peptides from transmembrane regions
    • T.N. Petersen, S. Brunak, G. von Heijne, and H. Nielsen SignalP 4.0: Discriminating signal peptides from transmembrane regions Nat. Methods 8 2011 785 786
    • (2011) Nat. Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 26
    • 0035350689 scopus 로고    scopus 로고
    • Protein targeting by the twin-arginine translocation pathway
    • DOI 10.1038/35073038
    • C. Robinson, and A. Bolhuis Reviews: Protein targeting by the twin-arginine translocation pathway Nat. Rev. 2 2001 350 356 (Pubitemid 33674047)
    • (2001) Nature Reviews Molecular Cell Biology , vol.2 , Issue.5 , pp. 350-356
    • Robinson, C.1    Bolhuis, A.2
  • 27
    • 0042928465 scopus 로고    scopus 로고
    • An Escherichia coli twin-arginine signal peptide switches between helical and unstructured conformations depending on the hydrophobicity of the environment
    • DOI 10.1046/j.1432-1033.2003.03710.x
    • M. San Miguel, R. Marrington, P.M. Rodger, A. Rodger, and C. Robinson An Escherichia coli twin-arginine signal peptide switches between helical and unstructured conformations depending on the hydrophobicity of the environment Eur. J. Biochem. 270 2003 3345 3352 (Pubitemid 37011628)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.16 , pp. 3345-3352
    • San Miguel, M.1    Marrington, R.2    Rodger, P.M.3    Rodger, A.4    Robinson, C.5
  • 28
    • 33645759682 scopus 로고    scopus 로고
    • Localization of plaunotol in the leaf of croton stellatopilosus Ohba
    • DOI 10.2306/scienceasia1513-1874.2006.32.017
    • W. Sitthithaworn, B. Potduang, and W. De-Eknamkul Localization of plaunotol in the leaf of Croton stelatopilosus Ohba ScienceAsia 32 2006 17 20 (Pubitemid 43555392)
    • (2006) ScienceAsia , vol.32 , Issue.1 , pp. 17-20
    • Sitthlthawom, W.1    Potduang, B.2    De-Eknamkul, W.3
  • 29
    • 75149166956 scopus 로고    scopus 로고
    • Cloning and expression of 1-deoxy-d-xylulose 5-phosphate synthase cDNA from Croton stellatopilosus and expression of 2C-methyl-d-erythritol phosphate synthase and geranylgeranyl diphosphate synthase, key enzymes of plaunotol biosynthesis
    • W. Sitthithaworn, J. Wungsintaweekul, T. Sirisuntipong, T. Charoonratana, Y. Ebizuka, and W. De-Eknamkul Cloning and expression of 1-deoxy-d-xylulose 5-phosphate synthase cDNA from Croton stellatopilosus and expression of 2C-methyl-d-erythritol phosphate synthase and geranylgeranyl diphosphate synthase, key enzymes of plaunotol biosynthesis J. Plant Physiol. 167 2010 292 300
    • (2010) J. Plant Physiol. , vol.167 , pp. 292-300
    • Sitthithaworn, W.1    Wungsintaweekul, J.2    Sirisuntipong, T.3    Charoonratana, T.4    Ebizuka, Y.5    De-Eknamkul, W.6
  • 30
    • 0031048876 scopus 로고    scopus 로고
    • Identification of a novel phosphatase sequence motif
    • J. Stukey, and G.M. Carmen Identification of a novel phosphatase sequence motif Protein Sci. 6 1997 469 472 (Pubitemid 27079942)
    • (1997) Protein Science , vol.6 , Issue.2 , pp. 469-472
    • Stukey, J.1    Carman, G.M.2
  • 31
    • 0032051857 scopus 로고    scopus 로고
    • Geranylgeraniol-18-hydroxylase: The last enzyme on the plaunotol biosynthetic pathway in Croton sublyratus
    • DOI 10.1016/S0031-9422(97)00743-7, PII S0031942297007437
    • P. Tansakul, and W. De-Eknamkul Geranylgeraniol-18-hydroxylase: The last enzyme on the plaunotol biosynthetic pathway in Croton sublyratus Phytochemistry 47 1998 1241 1246 (Pubitemid 28232506)
    • (1998) Phytochemistry , vol.47 , Issue.7 , pp. 1241-1246
    • Tansakul, P.1    De-Eknamkul, W.2
  • 33
    • 0033517850 scopus 로고    scopus 로고
    • Mutagenesis of the phosphatase sequence motif in diacylglycerol pyrophosphate phosphatase from Saccharomyces cerevisiae
    • D.A. Toke, M.L. McClintick, and G.M. Carman Mutagenesis of the phosphatase sequence motif in diacylglycerol pyrophosphate phosphatase from Saccharomyces cerevisiae Biochemistry 38 1999 14606 14613
    • (1999) Biochemistry , vol.38 , pp. 14606-14613
    • Toke, D.A.1    McClintick, M.L.2    Carman, G.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.