請用此 Handle URI 來引用此文件：
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/43245完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 李平篤 | |
| dc.contributor.author | Zhong-Yuan Zheng | en |
| dc.contributor.author | 鄭仲淵 | zh_TW |
| dc.date.accessioned | 2021-06-15T01:44:49Z | - |
| dc.date.available | 2010-07-17 | |
| dc.date.copyright | 2009-07-17 | |
| dc.date.issued | 2009 | |
| dc.date.submitted | 2009-07-09 | |
| dc.identifier.citation | Alibert, G., Ranjeva, R. and Boudet, A. (1972) Studies on enzymes catalyzing phenolic acids formation in Quercus penduculata (Ehrh.). II. Intracellular location of phenylalanine ammonia-lyase, cinnamate 4-hydroxylase and 'benzoate synthase'. Biochim Biophys Acta 279, 282-288.
Allwood, E.G., Davies, D.R., Gerrish, C. and Bolwell, G.P. (2002) Regulation of CDPKs, including identification of PAL kinase, in biotically stressed cells of French bean. Plant Mol Biol. 49, 533-44. Allwood, E.G., Davies, D.R., Gerrish, C., Ellis, B.E. and Bolwell, G.P. (1999) Phosphorylation of phenylalanine ammonia-lyase: evidence for a novel protein kinase and identification of the phosphorylated residue. FEBS Lett. 457, 47-52. Alunni, S., Cipiciani, A., Fioroni, G. and Ottavi, L. (2003) Mechanisms of inhibition of phenylalanine ammonia-lyase by phenol inhibitors and phenol/glycine synergistic inhibitors. Arch Biochem Biophys. 412, 170-5. Appert, C., Logemann, E., Hahlbrock, k., Schmid, J. and Amrhein, N. (1994) Structural and catalytic properties of the four phenylalanine ammonia-lyase isozymes from parsley (Petroselinum crispum Nym.). Eur J Biochem 225, 491-499. Appert, C., Zon, J. and Amrhein, N. (2003) Kinetic analysis of the inhibition of phenylalanine ammonia-lyase by 2-aminoindan-2-phosphonic acid and other phenylalanine analogues. Phytochemistry. 62, 415-22. Attridge, T.H., Stewart, G.R. and Smith, H. (1971) End-product inhibition of Pisum phenyl- alanine ammonia-lyase by the Pisum flavonoids. FEBS Lett. 17, 84-86. Baedeker, M. and Schulz, G.E. (1999) Overexpression of a designed 2.2 kb gene of eukaryotic phenylalanine ammonia-lyase in Escherichia coli. FEBS Lett 457, 57-60. Bate, N.J., Orr, J., Ni, W., Meromi, A., Nadler-Hassar, T., Doerner, P.W., Dixon, .A., Lamb, C.J. and Elkind, Y. (1994) Quantitative relationship between phenylalanine ammonia-lyase levels and phenylpropanoid accumulation in transgenic tobacco identifies a rate-deter- mining step in natural product synthesis. Proc. Natl. Acad. Sci. USA. 91, 7608-7612. Benoit, M.A., D'Aprano, G. and Lacroix, M. (2000) Effect of gamma-irradiation on phenyl- alanine ammonia-lyase activity, total phenolic content, and respiration of mushrooms (Agaricus bisporus). J Agric Food Chem 48, 6312-6. Bevan, M. and Northcote, D.H. (1979) The loss of morphogenetic potential and induction of phenylalanine ammonia-lyase in suspension cultures of Phaseolus vulgaris. J Cell Sci 39, 339-353. Blount, J. W., Korth, K. L., Masoud, S. A., Rasmussen, S., Lamb, C. and Dixon, R. A. (2000). Altering Expression of cinnamic acid 4-hydroxylase in transgenic plants provides evidence for a feedback loop at the entry point into the phenylpropanoid pathway. Plant Physiol. 122, 107-116. Bolwell, G.P. (1992) A role for phosphorylation in the down regulation of phenylalanine ammonia-lyase in suspension cultured cells of French bean. Phytochemistry. 31, 4081-6. Bolwell, G.P. (1999) Role of active oxygen species and NO in plant defence responses. Curr. Opin. Plant Biol. 2, 287-294. Bolwell, G.P., Bell, J.N., cramer, C.L., Schuch, w., Lamb, C.J. and Dixon, R.A. (1985) L-phenylalanine ammonia-lyase from Phaseolus vulgaris: characterization and differential induction of multiple forms from elictor-treated suspension cultures. Eur J Biochem 149, 411-419. Bolwell, G.P., Cramer, C.L., Lamb, C.J., Schuch, W. and Dixon, R.A. (1986) L-Phenyl- alanine ammonia-lyase from Phaseolus vulgaris. Modulation of the levels of active enzyme by trans- cinnamic acid. Planta 169, 97-107. Bradford, M.M. (1976) A rapid and sensitive method for the quantiation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254. Chaman, M.E., Copaja, S.V. and Argandona, V.H. (2003) Relationships between salicylic acid content, phenylalanine ammonia-lyase (PAL) activity, and resistance of barley to aphid infestation. J Agric Food Chem. 51, 2227-31. Chang, W. C. (1991) Bamboo, In:Bajaj, Y.P.S. (ed.). Biotechonology in Agriculture and Forestry, Vol 16, Tree III. P.221-237. SpringeVerlag, Berlin. Chang, W. C. (1994) Somatic embryogenesis of Bambusa oldhami, Bambusa beecheyana and Sinocalamus latiflora. In: Jain, S. Gupta, P. and Nowton, R. (eds.). Somatic Embryogenesis in Woods Plants. P. 53-65. Kluver Academic Publisher, Nertherland. Cheng, S.H, Sheen, J., Gerrish, C. and Bolwell, G.P. (2001) Molecular identification of phenylalanine ammonia-lyase as a substrate of a specific constitutively active Arabidopsis CDPK expressed in maize protoplasts. FEBS Lett. 503, 185-188. Cramer, C.L., Edwards, K., Dron, M., Liang, X., Dildine, S.L., Bolwell, G.P., Dixon, R.A., Lamb, C.J. and Schuch, W. (1989) Phenylalanine ammonia-lyase gene organization and structure. Plant Mol. Biol. 12, 367-383. Czichi, U. and Kindl, H. (1975) Formation of p-coumaric acid and o-coumaric acid from L-phenylalanine by microsomal membrane fractions from potato: Evidence of membrane- bound enzyme complexes. Planta 125, 115-125. Czichi, U., and Kindl, H. (1977) Phenylalanine ammonia-lyase and cinnamic acid hydroxy- lases as assembled consecutive enzymes on microsomal membranes of cucumber cotyledons: Cooperation and subcellular distribution. Planta 134, 133-143. Deikman, J. and Hammer, P.E. (1995) Induction of anthocyanin accumulation by cytokinins in Arabidopsis thaliana. Plant Physiol. 108, 47-57. Dieguez, M.J., Belloto, M., Afsar, K., Mittelsten Scheid, O. and Paszkowski, J. (1997) Methylation of cytosines in nonconventional methylation acceptor sites can contribute to reduced gene expression. Mol Gen Genet. 253, 581-588. Dixon, R.A. and Paiva, N.L. (1995) Stress-induced phenylpropanoid metabolism. Plant Cell 7, 1085-1097. Dixon, R.A., Browne, T. and Ward, M. (1980) Modulation of L-phenylalanine ammonia- lyase by pathway intermediates in cell suspension cultures of dwarf French bean (Phaseolus vulgaris L.). Planta 150, 279-285. Dunn, D.C., Duncan, L.W. and Romeo, J.T. (1998) Changes in arginine, PAL activity, and nematode behavior in salinity-stressed citrus. Phytochemistry 49, 413-7. Edwards, K., Cramer, C.L., Bolwell, G.P., Dixon, R.A., Schuch, W. and Lamb, C.J. (1985) Rapid transient induction of phenylalanine ammonia-lyase mRNA in elicitor-treated bean cells. Proc. Natl. Acad. Sci. USA 82, 6731-6735. El-Shora, H.M. (2002) Properties of phenylalanine ammonia-lyase from marrow cotyledons. Plant Sci. 162, 1-7. Elkind, Y., Edwards, R., Mavandad, M., Hedrick, S.A., Ribak, O., Dixon, R.A. and Lamb, C.J. (1990) Abnormal plant development and downregulation of phenylpropanoid biosynthesis in transgenic tobacco containing a heterologous phenylalanine ammonia-lyase gene. Proc. Natl. Acad. Sci. USA 87, 9057-9061. Flavell, R.B. (1994) Inactivation of gene expression in plants as a consequence of specific sequence duplication. Proc. Natl. Acad. Sci. USA 91, 3490-3496. Fukasawa-Akada, T., Kung, S., and Watson, J.C. (1996) Phenylalanine ammonia- lyase gene structure, expression, and evolution in Nicotiana. Plant Mol. Biol. 30:711-722. Given, N.K., Venis, M.A. and Grierson, D. (1988) J Plant Physiol. 133, 31-37. Gloge, A., Langer, B., Poppe, L. and Rétey, J. (1998) The behavior of substrate analogues and secondary deuterium isotope effects in the phenylalanine ammonia-lyase reaction. Arch Biochem Biophys 359, 1-7. Gloge, A., Zon, J., Kovari, A., Poppe, L. and Rétey, J. (2000) Phenylalanine ammonia-lyase: the use of its broad substrate specificity for mechanistic investigations and biocatalysis- synthesis of L-arylalanines. Chemistry 6, 3386-90. Gray-Mitsumune, M., Molitor, E., Cukovic, D., Carlson, J.E. and Douglas, C.J. (1999) Developmentally regulated patterns of expression directed by poplar PAL promoters in transgenic tobacco and poplar. Plant Mol Biol 39, 657-669. Habibi-Moini, S. and D'mello, A.P. (2001) Evaluation of possible reasons for the low phenylalanine ammonia-lyase activity in cellulose nitrate membrane microcapsules. Int J Pharm 215, 185-96 Hahlbrock, K. and Scheel, D. (1989) Physiology and molecular biology of phenylpropanoid metabolism. Annu Rev Plant Physiol Plant Mol Biol 40, 347-369. Hanson, K.R. and Havir, E.A. (1970) L-phenylalanine ammonia-lyase. IV. Evidence that the prosthetic group contains dehydroalanyl residue and mechanism of action. Arch Biochem Biophys 141, 1-17. Hanson, K.R., Havir, E.A. (1972) in ‘The Enzyme’, 3rd. Ed. (Boyer, P.D., Ed.) 7, 75-166. Hao, Z., Charles, D.J., Yu, L. and Simon, J.E. (1996) Purification and characterization of phenylalanine ammonia-lyase from Ocimum basilicum. Phytochemistry 43, 735-739. Hatton D, Smith C, Bevan M. (1996) Tissue-specific expression of the PAL3 promoter requires the interaction of two conserved cis sequences. Plant Mol Biol. 31, 393-7. Hattori, T., Nishiyawa, A. and Shimada, M. (1999) Induction of L-phenylalanine ammonia- lyase and suppression of veratryl alcohol biosynthesis by exogenously added L-phenyl- alanine in white-rot fungus Phanerochaete chrysosporium. FEMS Lett. 179, 305-309. Havir, E.A. (1979) L-Phenylalanine ammonia-lyase. Binding of polysaccharide by the enzyme from maize. Plant Sci Lett 16, 297-304. Havir, E.A., Reid, P.D. and Marsh, H.V. Jr (1971) L-phenylalanine ammonia-lyase (maize). Plant Physiol 48, 130-136. Herrmann, K.M. (1995) The shikimate pathway as an entry to aromatic secondary metabolism. Plant Physiol. 107, 7-12. Herrmann, K.M. and Weaver, L.M. (1999) The shikimate pathway. Annu. Rev. Plant Physiol. Plant Mol. Biol. 50, 473-503. Hisaminato, H., Murata, M. and Homma, S. (2001) Relationship between the enzymatic browning and phenylalanine ammonia-lyase activity of cut lettuce, and the prevention of browning by inhibitors of polyphenol biosynthesis. Biosci Biotechnol Biochem 65, 1016-21. Howles, P.A., Sewalt, V.J.H., Paiva, N.L., Elkind, Y., Bate, N.J., Lamb, C.J. and Dixon, R.A. (1996) Overexpression of L-phenylalanine ammonia-lyase in transgenic tobacco plants reveals control points for flux into phenylpropanoid biosynthesis. Plant Physiol. 112, 1617-1624. Jangaard, N.O. (1974) The characterization of phenylalanine ammonia-lyase from several plant species. Phytochemustry 13, 1765-1768. Jiménez, C.R., Huang, L., Qie, Y. and Burlingame, A.L. (1998) In-gel digestion of proteins for MALDI-MS fingerprint mapping. Current Proptocols in Protein Science 16.4.1-16.4.5. Jingzhong, L., Hua, X., Wei, H., Zhangling, Z., Jin, Z. and Qingyuan, L. (1999) Cloning and expression of phenylalanine ammonia-lyase cDNA in Escherichia coli. Chin J Biotechnol 14, 227-32. Jones, D.H. (1984) Phenylalanine ammonia-lyase: Regulation of its induction, and its role in plant development. Phytochemistry 23, 1349-1359. Jones, D.H. and Northcote, D.H. (1984) Stability of the complex formed between French bean (Phaseolus vulgaris) phenylalanine ammonia-lyase and its transition-state analog. Arch. Biochem. Biophys. 235, 167-177. Jorrin, J., Lopez-Valbuena, R. and Tena, M. (1988) Biochim Biophys. Acta. 964, 73-82. Kalghatgi, K.K. and Subba-Rao, P.V. (1975) Microbial L-phenylalanine ammonia-lyase. Purification, subunit structure and kinetic properties of the enzyme from Rhizoctonia solani. Biochem J. 149, 65-75. Kamada, Y. and Muto, S. (1994) Stimulation by fungal elicitor of inositol phospholipid turnover in tobacco suspension culture cells. Plant Cell Physiol 35,397-404. Kato, H., Wada, M., Muraya, K., Malik, K., Shiraishi, T., Ichinose, Y. and Yamada, T. (1995) Characterization of nuclear factors for the elicitor-mediated activation of the promoter of the pea phenylalanine ammonia-lyase gene 1. Plant Physiol 108, 129-139. Kato, M., Hayakawa, Y., Hyodo, H., Ikoma, Y. and Yano, M. (2000) Wound-induced ethylene synthesis and expression and formation of 1-aminocyclopropane-1-carboxylate (ACC) syn- thase, ACC oxidase, phenylalanine ammonia-lyase, and peroxidase in wounded mesocarp tissue of Cucurbita maxima. Plant Cell Physiol 41, 440-7. Kawamata, S., Shimoharai, K,, Imura, Y., Ozaki, M., Ichinose, Y., Shiraishi, T., Kunoh, H. and Yamada, T. (1997) Temporal and spatial pattern of expression of the pea phenylalanine ammonia-lyase gene1 promoter in transgenic tobacco. Plant Cell Physiol 38, 792-803. Kawaoka, A., Kaothien, P., Yoshida, K., Endo, S., Yamada, K. and Ebinuma, H. (2000) Functional analysis of tobacco LIM protein Ntlim1 involved in lignin biosynthesis. Plant J 22, 289-301. Kim, S.H., Kronstad, J.W. and Ellis, B.E. (1996) Purification and characterization of phenylalanine ammonia-lyase from Ustilago maydis. Phytochemistry 43, 351-357. Kim, S.H., Kronstad, J.W. and Ellis, B.E. (2001) Induction of phenylalanine ammonia-lyase activity by tryptophan in Ustilago maydis. Phytochemistry. 58, 849-57. Kim, S.H., Virmani, D., Wake, K., MacDonald, K., Kronstad, W. and Ellis, B.E. (2001) Cloning and disruption of phenylalanine ammonia-lyase gene from Ustilago maydis. Curr. Genet. 40, 40-48. Koukol, J. and Conn, E.E. (1961) The metabolism of aromatic compounds in higher plants. IV. Purification and properties of phenylalanine deaminase of Hordeum vulgare. J Biol Chem 236, 1692-2698. Kristensen, D.B., Imamura, K., Miyamoto, Y. and Yoshizato, K. (2000) Mass spectrometric approaches for the characterization of proteins on a hybrid quadruple time-of-flight (Q-TOF) mass spectrometer. Electrophoresis 21, 430- 439. Kubasek, W.L., Shirley, B.W., Mckillop, A., Goodman, H.M. and Briggs, W. (1992) Regulation of Flavonoid Biosynthetic Genes in Germinating Arabidopsis Seedlings. Plant Cell 4, 1229-1236. Kumar, A. and Ellis, B..E. (2001) The phenylalanine ammonia-lyase gene family in raspberry. Structure, expression, and evolution. Plant Physiol. 127, 230-9. Kyndt, J.A., Meyer, T.E., Cusanovich, M.A. and Van Beeumen, J.J. (2002) Characterization of bacterial tyrosine ammonia lyase, a biosynthetic enzyme for the photoactive yellow protein. FEBS Lett 512, 240-244. Lamb, C.J. and Dixon, R.A. (1997) The oxidative burst in plant disease resistance. Annu Rev Plant Physiol Plant Mol Biol. 48, 251-279. Langer, B., Langer, M. and Rétey, J. (2001) Methylidene-imidazole-one (MIO) from histidine and phenylalanine ammonia lyase. In Advances in Protein Chemistry, vol 58, 175-214. Edited by Klinman, J.P. and Dove, J.E., New York: Academic Press. Langer, B., Rother, D. and Rétey, J. (1997) Identification of essential amino acids in phenylalanine ammonia-lyase by site-directed mutagenesis. Biochemistry 36, 10867-71. Lee, P.D. and Su, J.C. (1970) Cytokinin activity of bamboo shoot soluble RNA. J. Chinese Agr. Chem. Soc., Sp. Iss, 54-64. Lee, S.W., Robb, J. and Nazar, R.N. (1992) Truncated phenylalanine ammonia-lyase express- ion in tomato (Lycopersicon esculentum). J Biol Chem 267, 11824- 11830. Levee V, Seguin A. (2001) Inducible expression of the heterologous PAL2 promoter from bean in white pine (Pinus strobus) transgenic cells. Tree Physiol. 21, 665-72. Lewandowicz, A., Jemielity, J., Kanska, M., Zon, J. and Paneth, P. (1999) Tritium secondary kinetic isotope effect on phenylalanine ammonia-lyase-catalyzed reaction. Arch Biochem Biophys 370, 216-21. Leyva, A., Jarillo, J.A., Salinas, J. and Martinez-Zapater, J.M. (1995) Low temperature induces the accumulation of phenylalanine ammonia-lyase and chalcone synthase mRNAs of Arabidopsis thaliana in a light-dependent manner. Plant Physiol. 108, 39-46. Lim, H.W., Park, S.S. and Lim, C.J. (1997) Purification and properties of phenylalanine ammonia-lyase from leaf mustard. Mol Cells 7, 715-20. Lim, H.W., Sa, J.H., Park, S.S. and Lim, C.J. (1998) A second form of phenylalanine ammonia-lyase from leaf mustard. Mol Cells 8, 343-9. Logemann, E., Parniske, M. and Hahlbrock, K. (1995) Modes of expression and common structural features of the complete phenylalanine ammonia-lyase gene family in parsley. Proc Natl Acad Sci USA 92, 5905-5909. Lois, R., Dietrich, A., Hahlbrock, K. and Schulz, W. (1989) A phenylalanine ammonia-lyase gene from parsley: structure, regulation and identification of elicitor and light responsive cis-acting elements. EMBO J 8, 1641-1648. Maher, E.A., Bate, N.J., Ni, W., Elkind, Y., Dixon, R.A. and Lamb, C.J. (1994) Increased disease susceptibility pf transgenic tobacco plants with suppressed levels of preformed phenylpropanoid products. Proc. Natl. Acad. Sci. USA 91, 7802-7806. Matsumoto, S., Kiriiwa, Y. and Takeda, Y. (2002) Differentiation of Japanese green tea cultivars as revealed by RFLP analysis of phenylalanine ammonia-lyase DNA Theor Appl Genet 104, 998-1002. McKegney G.R., Butland, S.L., Theilmann, D. and Ellis, B.E. (1996) Expression of poplar phenylalanine ammonia-lyase in insect cell culture. Phytochemistry 41, 1259- 1263. Meyer, P. (1996) Homology dependent gene silencing in plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 47, 23-48. Mishra, K.K. and Handa, A.K. (1998) Post-transcriptional silencing of pectin methylesterase gene in transgenic tomato fruits from impaired pre-mRNA processing. Plant J. 14, 583- 592. Morino, K., Olsen, O.A. and Shimamoto, K. (1999) Silencing of an aleurone-specific genes in transgenic rice is caused by a rearranged transgene. Plant J. 17, 275-285. Nagai, N., Kitauchi, F., Okamoto, K., Kanda, T., Shimosaka, M. and Okazaki, M. (1994) A transient increase of phenylalanine ammonia-lyase transcript in kinetin-treated tobacco callus. Biosci Biotechnol Biochem 58, 558-559. Nagai, N., Kitauchi, F., Shimosaka, M. and Okazaki, M. (1994) Cloning and sequencing of a full length cDNA coding for phenylalanine ammonia-lyase from tobacco cell culture. Plant Physiol. 104, 1091-1092. Nagai, N., Kojima, Y., Shimosaka, M. and Okazaki, M. (1988) Agric. Biol. Chem. 52, 2617-9. Nehls, U., Ecke, M. and Hampp, R. (1999) Sugar- and nitrogen-dependent regulation of an Amanita muscaria phenylalanine ammonium lyase gene. J Bacteriol 181,1931-3. Neish, A.C. (1961) Formation of m- and p-coumaric acids by enzymatic desamination of the corresponding isomers of tyrosine. Phytochemistry 41, 1259- 1263. Nugroho, L.H., Verberne, M.C. and Verpoorte, R. (2002) Activities of enzymes involved in the phenylpropanoid pathway in constitutively salicylic acid-producing tobacco plants. Plant Physiol. Biochem. 40, 755-760. Ohl, S., Hedrick, S.A., Chory, J. and Lamb, C.J. (1990) Functional properties of a phenyl- alanine ammonia-lyase promoter from Arabidopsis. Plant Cell 2, 837-848. O'Neal, D. and Keller, C.J. (1970) Partial purification and some properties of phenylalanine ammonia-lyase of tobacco (Nicotiana tabacum). Phytochemistry 9, 1373-1383. Orr, J.D., Edwards, R. and Dixon, R,A. (1993) Stress Responses in Alfalfa (Medicago sativa L.) (XIV. Changes in the Levels of Phenylpropanoid Pathway Intermediates in Relation to Regulation of L-Phenylalanine Ammonia-Lyase in Elicitor-Treated Cell-Suspension Cultures). Plant Physiol. 101, 847-856. Oufedjikh, H., Mahrouz, M., Amiot, M.J. and Lacroix, M. (2000) Effect of gamma-irradiation on phenolic compounds and phenylalanine ammonia-lyase activity during storage in relation to peel injury from peel of Citrus clementina hort. Ex. tanaka. J Agric Food Chem 48, 559-65. Ozeki, Y., Matsui, K., Sakuta, M., Matsuoka, M., Ohashi, Y., Kano-Murakami, Y., Yama- moto, N. and Tanaka, Y. (1990) Differential regulation of phenylalanine ammonia-lyase genes during anthocyanin synthesis and by transfer effect in carrot cell suspension cultures. Physiol Plant 80, 379-387. Ozeki, Y., Chikagawa, Y., Kimura, S., Soh, H.C., Maeda, K., Pornsiriwong, W., Kato, M., Akimoto, H., Oyanagi, M., Fukuda, T., Koda, T., Itoh, Y., Yamada, A., Davies, E., Ueno, H. and Takeda, J. (2003) Putative cis-elements in the promoter region of the carrot phenylalanine ammonia-lyase gene induced during anthocyanin synthesis. J Plant Res. 116, 155-9. Ozeki, Y. and Takeda, J. (1994) Regulation of phenylalanine ammonia-lyase genes in carrot suspension cultured cells. Plant Cell Tissue Organ Culture 38, 221-225. Poppe, L. (2001) Methylidene-imidazolone: a novel electrophile for substrate activation. Curr Opin in Chem Biol 5, 512-524. Pellegrini, L., Rohfritsch, O., Fritig, B. and Legrand, M. (1994) Phenylalanine ammonia-lyase in tobacco. Plant Physiol. 106, 877-886. Prutpongse, P. and Gavinlertvatana, P. (1992) In vitro micropropagation of 54 species from 15 genera of bamboo. HortScience. 27, 453-455. Rasmussen, S. and Dixon, R.A. (1999) Transgene-mediated and elicitor-induced perturbation of metabolic channeling at the entry point into the phenylpropanoid pathway. Plant Cell 11, 1537-1552. Reddy, J.T., Korth, K.L., Wesley, S.V., Howles, P.A., Rasmussen, S., Lamb, C. and Dixon, R.A. (2001) Post-transcriptional regulation of phenylalanine ammonia-lyase expression in tobacco following recovery from gene silencing. J. Biol Chem 381, 655-65. Rees, D.G. and Jones, D.H. (1997) Activity of L-phenylalanine ammonia-lyase in organic solvents. Biochim Biophys Acta 1338, 121-6. Retéy, J. (2003) Discovery and role of methylidene imidazolone, a highly electrophilic prosthetic group. Biochim Biophys Acta. 1647, 179-84. Ro, D. K., Mah, N., Ellis, B. E. and Douglas, C. J. (2001). Functional characterization and subcellular localization of poplar (Populus trichocarpa × Populus deltoides) cinnamate 4- hydroxylase. Plant Physiol. 126, 317-329. Rosler, J., Krekel, F., Amrhein, N. and Schmid, J. (1997) Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity. Plant Physiol 113, 175-9. Sanchez-Ballesta, M,T., Zacarias, L., Granell, A. and Lafuente, M.T. (2000) Accumulation of PAL transcript and PAL activity as affected by heat-conditioning and low-temperature storage and its relation to chilling sensitivity in mandarin fruits. J Agric Food Chem 48, 2726-31. Sarma, A.D. and Sharma, R. (1999) Purification and characterization of UV-B induced phenylalanine ammonia-lyase from rice seeding. Phytochemistry 50, 729- 737. Sarma, A.D., Sreelakshmi, Y. and Sharma, R. (1998) Differential expression and properties of phenylalanine ammonia-lyase isoforms in tomato leaves. Phytochemistry 49, 2233-2243. Schulz, W., Eiben, H-G. and Hahlbrock, K. (1989) Expression in Escherichia coli of catalytically active phenylalanine ammonia-lyase from parsley. FEBS Lett 258, 335-338. Schuster, B. and Rétry, J. (1995) The mechanism of action of phenylalanine ammonia-lyase: the role of prosthetic dehydroalanine. Proc Natl Acad Sci USA 92, 8433-8437. Schwede TF, Rétey J, Schulz GE. (1999) Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile. Biochemistry. 38, 5355-61. Seguin, A., Laible, G., Leyva, A., Dixon, R.A. and Lamb, C.J. (1997) Characterization of a gene encoding a DNA-binding protein that interacts in vitro with vascular specific cis elements of the phenylalanine ammonia-lyase promoter. Plant Mol Biol 35, 281-91. Seki, H., Nagasugi, Y., Ichinose, Y., Shiraishi, T. and Yamada, T. (1999) Changes in in vivo DNA-protein interactions in pea phenylalanine ammonia-lyase and chalcone synthase gene promoter induced by fungal signal molecules. Plant Cell Physiol 40, 88-95. Sewalt, V.J.H., Ni, W., Blount, J.W., Jung, H.G., Masoud, S.A., Howles, P.A., Lamb, C.J. and Dixon, R.A. (1997) Reduced lignin content and altered lignin composition in trans- genic tobacco down- regulated in expression of L-phenylalanine ammonia- lyase or cinna- mate 4-hydroxylase. Plant Physiol. 115, 41-50. Shaw, N.M., Bolwell, G.P. and Smith, C. (1990) Wound-induced phenylalanine ammonia- lyase by L-phenylalanine ammonia-lyase in potato (Solanum tuberosum) tuber discs. Biochem J 267, 163-170. Singh, S., Lewis, N.G. and Towers, G.H. (1998) Nitrogen recycling during phenylpropanoid metabolism in sweet potato tubers. J Plant Physiol. 153, 316-23. Skolaut, A. and Retéy, J. (2001) 1,4-Dihydro-l-phenylalanine-its synthesis and behavior in the phenylalanine ammonia-lyase reaction. Arch Biochem Biophys. 393, 187-91. Su, J.C. (1965) Carbohydrate metabolism in the shoots of bamboo Leleba oldhami. I preli- minary survy of soluble saccharides and sucrose-degrading enzyme. Bot. Bull. Acad. Sinica. 6, 153-159. Subramaniam, R., Reinold, S., Molitor, E.K. and Douglas, C.J. (1993) Structure, inheritance, and expression of hybrid poplar (Populus trichocarpa×Populus deltoides) phenylalanine ammonia-lyase genes. Plant Physiol 102, 71-83 Sung, H.Y., Yuan, H.F. and Su, J.C. (1971) Carbohydrate metabolism in the shoots of bamboo Leleba oldhami. IX Some properties of the pentosan synthesizing syatem. J. Chin. Agric. Chem. Soc. Sp Iss, 62-73. Takeda, J., Ozeki, Y. and Yoshida, K. (1997) Action spectrum for induction of promoter activity of phenylalanine ammonia-lyase gene by UV in carrot suspension cells. Photochem Photobiol 66, 464-70. Tanaka, Y. and Uritani, I. (1977) Purification and properties of phenylalanine ammonia-lyase in cut injured sweet potato. J. Biochem 81, 963-970. Terauchi, R. and Kahl, G. (2000) Rapid isolation of promoter sequences by TAIL-PCR: the 5'-flanking regions of Pal and Pgi genes from yams (Dioscorea). Mol Gen Genet 263, 554-60. Wanner, L.A., Li, G., Ware, D., Somssich, I.E. and Davis, K.R. (1995) The phenylalanine ammonia- lyase gene family in Arabidopsis thaliana. Plant Mol. Biol. 27, 327-338. Yamada, T., Tanaka, Y., Sriprasertsak, P., Kato, H., Hashimoto, T. and Oku, H. (1992) Phenyl- alanine ammonia-lyase genes from Pisum sativum: structure, organ-specific expression and regulation by fungal elicitor and supressor. Plant Cell Physiol 33, 715-725. Yazaki, K., Kataoka, M., Honda, G., Severin, K. and Heide, L. (1997) cDNA cloning and gene expression of phenylalanine ammonia-lyase in Lithospermum erythrorhizon. Biosci Biotechnol Biochem 61, 1995-2003. Young, M.R., Towers, G.H.N. and Neish, A.C. (1966) Taxonmic distribution of ammonia- lyases for L-phenylalanine and L-tyrosine in relation to lignification. Can J Bot 44, 341-9. Zhu, Q., Dabi, T., Beeche, A., Yamamoto, R., Lawton, M.A. and Lamb, C. (1995) Cloning and properties of a rice gene encoding phenylalanine ammonia-lyase. Plant Mol Biol. 29, 535-50. Zon, J., Amrhein, N. and Gancarz, R. (2002) Inhibitors of phenylalanine ammonia-lyase: 1-amino- benzylphosphonic acids substituted in the benzene ring. Phytochemistry. 59, 9-21. 莊榮輝 (1985) 水稻蔗糖合成之生化及免疫學研究。博士論文，國立台灣大學農業化學研究所 謝陸盛 (2003) 綠竹葉與籜苯丙胺酸裂解酶之生化學研究。碩士論文，國立台灣大學農業化學研究所 蘇玟珉 (2003) 綠竹筍苯丙胺酸裂解酶之生化學研究。碩士論文，國立台灣大學農業化學研究所 潘宏記 (2004) 大腸桿菌表現綠竹苯丙胺酸脫氨裂解酶及功能鑑定。碩士論文，國立台灣大學微生物與生化學研究所 賴偉學 (2009) 白蘆筍苯丙胺酸裂解酶之生化學研究。 碩士論文，國立台灣大學微生物與生化學研究所 | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/43245 | - |
| dc.description.abstract | 苯丙胺酸裂解 (phenylalanine ammonia-lyase, PAL EC 4.3.1.5) 是植物 phenylpropanoids 生合成之第一個酵素。此酵素催化苯丙胺酸 (phenylalanine) 經過非氧化型脫氨反應產生肉桂酸 (trans-cinnamic acid)。這個反應導致植物二級代謝產物及大量的 phenylpropanoid 衍生物生合成，包括木質素 (lignin)、黃酮素 (flavonoid) 等。
本論文以筊白筍為材料；經緩衝液粗抽、硫酸銨分劃、膠體過濾法 (Sepharacyl S-300)、疏水性作用層析法 (Phenyl-Sepharose) 及快速蛋白質液相層析法 (FPLC) 後，得到純化倍率為 110.5 倍，比活性為 53.3 nkat/mg protein。以膠體過濾法 (Superose 6, Superose 12) 測得之 PAL 原態分子量介於 290-300 kD，其次單元體分子量由 SDS-PAGE 測得約為 75 kD，因此推測筊白筍 PAL 可能為同質四元體結構。藉綠竹之 PAL 抗體進行西方點墨法顯示純化所得確實為 PAL，並將所得之 PAL 進行相關生化學研究 筊白筍與其他禾本科植物之 PAL 具有類似生化性質。苯丙胺酸裂解酶對基質 Phe 之 Km 值為筊白筍 516 μM。酵素最適反應溫度為 45℃。活化能為16.1 kcal/mol；最適反應 pH 為 8.5。鈣、鎂、錳在低濃度事會活化 PAL 活性；鈷、汞離子則會抑制。二級代謝產物，包括 trans-cinnamic acid、p-coumaric acid、ferulic acid、p-amino-benzonic acid 以及 caffeic acid，有產物回饋抑制現象。PAL 對基質 L-Phe 有專一性。酵素催化作用之活化中心具有 serine、tyrosine、histidine 等胺酸。 | zh_TW |
| dc.description.abstract | Phenylalanine ammonia-lyase (PAL, EC 4.3.1.5) is the first enzyme of the phenylpropanoid biosynthetic pathway. The enzyme catalyzes the non-oxidative deamination of phenylalanine to trans-cinnamic acid. This reaction leads to bio- synthesis of many phenylpropanoid-derived secondary metabolic products in plants, such as flavonoids and lignin.
In this study, PAL was purified from water bamboo by buffer extraction, ammonium sulfate precipitation, Sephacryl S-300, Phenyl- Sepharose, and Fast Protein Liquid Chromatography (FPLC). The purified PAL with 110.5-fold purification and specific activity of 53.3 nkat/mg protein obtained from water bamboo. Using Superose 6 and Superose 12 column (FPLC), the molecular weight of native form PAL was estimated to be 290-300 kD, the molecular weight of subunit form was determined to be 75 kD by SDS-PAGE.Using Western blot by antibody of bamboo PAL, and the results indicated that after the purification procedure the enzyme PAL had been purified. The pure enzyme was used to test biochemical properties. PAL from water bamboo is similar with Gramineae plants in biochemical properties. The Km values for L-Phe were 516.The optimum temperature and pH were 45℃ and 8.5, respectively. The activation energy was 16.1 kcal/mol. Ca2+, Mg2+, Mn2+ actived PAL activity in low concentration; Co2+, Hg2+ inhibited PAL activity. Secondary metabolites including trans-cinnamic acid, p-coumaric acid, ferulic acid, p-amino-benzonic acid, and caffeic acid with phenomena of feedback inhibition. PAL has high substrate specificity to L-phenylalanine, and the presence of seryl, tyrosyl and histidyl groups was found to be essential for enzyme catalysis. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-15T01:44:49Z (GMT). No. of bitstreams: 1 ntu-98-R96B47216-1.pdf: 2917064 bytes, checksum: 8ba4b25210d8243e7456669e00daeaaa (MD5) Previous issue date: 2009 | en |
| dc.description.tableofcontents | 目錄……………………………………………………………………………………a
縮寫表………………………………………………………………………………….i 中文摘要………………………………………………………………………………ii 英文摘要……………………………………………………………………………...iii 第一章 緒論…………………………………………………………………………..1 1.1 筊白筍……………………………………..….……………………………...1 1.2 植物的二級代謝………………………………..……………………..……..2 1.3 類苯丙胺酸路徑.……………………….…...……………………………….4 1.4 苯丙胺酸裂解酶…………..………….…..………..…………………..6 1.5 苯丙胺酸裂解酶催化機制……….………..……….………...……………...7 1.6 單子葉植物 PAL 可能具有 TAL 活性………….……………………..9 1.7 轉殖菸草中 PAL 之相關研究……………………….…………………10 1.8 苯丙胺酸裂解酶同功酶……………………………………………………12 1.9 苯丙胺酸脫氨裂解酶之調控...……………….……………………………12 1.9.1 環境與發育因子在轉錄層次上之調控……………………………12 1.9.2 磷酸化與後轉譯修飾………………………..………………………13 1.9.3 產物調控……………………………………………………………..14 1.10 實驗緣起…………………………………………………………………..14 第二章 材料與方法…………………………………………………………………15 2.1材料、藥品與儀器………………….……………………………………….15 2.1.1 材料…………………..…..…..……………………………………..15 2.1.2 藥品與儀器…………………..…………...………...………………15 2.2 蛋白質定量法………..……………….……………………………………16 2.3苯丙胺酸裂解酶活性分析………………….……………………………...17 2.4 電泳檢定系統……………………………………………………………...18 2.4.1 原態膠體電泳 (native-PAGE)……..…………………….………….19 2.4.2 SDS 膠體電泳 (SDS-PAGE)………………………………………..21 2.4.3 膠體染色法…………………………………………………………..23 2.4.3.1 CBR 染色法…………………………………………………23 2.4.3.2膠片乾燥法………………………………….……………..24 2.5 苯丙胺酸裂解酶的純化…………………………………………………...25 2.5.1 粗抽與硫酸銨分劃…………………………………………………..25 2.5.2 膠體過濾管柱層析…………………………………………………..27 2.5.3疏水性作用管柱層析………………………………………………...27 2.5.4快速蛋白質液相管柱 (FPLC) 層析….……………….…………….30 2.6蛋白質電泳轉印及相關應用…………….………………………...………32 2.6.1蛋白質轉印法………………………………………………...………32 2.6.2酵素免疫染色…………………………………………………..…..33 2.7 分子量測定……………….…..……………………………………………33 2.7.1 Superose 6 和 Superose 12 (FPLC) 膠體過濾層析……………..…33 2.7.2 SDS-PAGE……………………………………………..………….….35 2.8 酵素生化性質……………………………………………………………...35 2.8.1 酵素反應最適 pH 值…………………………………………….…35 2.8.2 最適反應溫度………………………………………………………..35 2.8.3活化能 (Activation energy, Ea)……..………………………………..35 2.8.4 熱安定性……………………………………………………………..36 2.8.5 Km 值…………………………………………………………….…..36 2.8.6 金屬離子對活性之影響……………………...……………………...36 2.8.7 二級代謝物對活性影響………...……………………………….…..36 2.8.8化學修飾劑對活性影響………………………………………….…..36 2.8.9 基質專一性………...…………………………………………….…..36 2.8.10酪胺酸脫氨裂解酶 (TAL) 活性分析法…………………………...37 第三章 結果與討論…………………………………………………………………38 3.1筊白筍苯丙胺酸裂解酶純化………………………………………..…...38 3.1.1純化步驟之流程…………………………………………………..….38 3.1.2活性測定…………………………………………………….………..39 3.1.3硫酸銨分劃…………………………………………………….....…..39 3.1.4 Sephacryl S-300 (Gel filtration)………………………………………39 3.1.5 Phenyl-Sepharose……………………………………………..……....40 3.1.6 Mono Q HR5/5 (FPLC)…...……………………………………..……40 3.1.7各純化步驟電泳分析比較………………………………………...…41 3.1.8純化表…………………………………………….…………..…….41 3.1.9 原態分子量測定……………………………………………………..41 3.2 PAL 生化性質………………………………………………………..……42 3.2.1 最適反應溫度與活化能……………………………………………42 3.2.2 熱安定性…………………………………………………………..…43 3.2.3 最適反應 pH…………………………………………………….…44 3.2.4 Km 值………………………………………………………………...44 3.2.5 金屬離子影響……………………………………………......………44 3.2.6 二級代謝物對 PAL 活性的影響……………………………….….45 3.2.7 基質專一性…………….……………...……...…………………..….45 3.2.8 化學修飾劑對活性影響………...………….….………..………..….46 第四章 結果與展望…………………………………………………………………47 4.1 筊白筍苯丙胺酸裂解酶純化………………………….…………..……....47 4.2苯丙胺酸裂解分子形式……………………….……………..…………….48 4.3筊白筍與綠竹之苯丙胺酸裂解酶生化性質比較……………….….……..48 4.4 未來展望…………………………………………………...………………50 參考文獻……………………………..……………………………….…………...…74 | |
| dc.language.iso | zh-TW | |
| dc.subject | 苯丙胺酸裂解酶 | zh_TW |
| dc.subject | Phenylalanine Ammonia-Lyase | en |
| dc.title | 筊白筍苯丙胺酸裂解酶之生化學研究 | zh_TW |
| dc.title | Biochemical Studies of Phenylalanine Ammonia-Lyase from Water Bamboo (Zizania latifolia) | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 97-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 楊健志,林棋財 | |
| dc.subject.keyword | 苯丙胺酸裂解酶, | zh_TW |
| dc.subject.keyword | Phenylalanine Ammonia-Lyase, | en |
| dc.relation.page | 81 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2009-07-10 | |
| dc.contributor.author-college | 生命科學院 | zh_TW |
| dc.contributor.author-dept | 微生物與生化學研究所 | zh_TW |
| 顯示於系所單位： | 微生物學科所 | |
文件中的檔案：
| 檔案 | 大小 | 格式 | |
|---|---|---|---|
| ntu-98-1.pdf 未授權公開取用 | 2.85 MB | Adobe PDF |
系統中的文件，除了特別指名其著作權條款之外，均受到著作權保護，並且保留所有的權利。