References
- Koukol J, Conn EE. The metabolism of aromatic compounds in higher plants. IV. Purification and properties of the phenylalanine deaminase of Hordeum vulgare. J Biol Chem 1961;236:2692-8.
- Jones DH. Phenylalanine ammonia-lyase: regulation of its induction, and its role in plant development. Phytochemistry 1984;23:1349-59. https://doi.org/10.1016/S0031-9422(00)80465-3
- Marusich WC, Jensen RA, Zamir LO. Induction of L-phenylalanine ammonia-lyase during utilization of phenylalanine as a carbon or nitrogen source in Rhodotorula glutinis. J Bacteriol 1981;146:1013-9.
- Camm EL, Towers GHN. Review article: phenylalanine ammonia lyase. Phytochemistry 1973;12:961-73. https://doi.org/10.1016/0031-9422(73)85001-0
- Jorrin J, Lopez-Valbuena R, Tena M. Purification and properties of phenylalanine ammonia-lyase from sunflower (Helianthus annuus L.) hypocotyls. Biochim Biophys Acta 1988;964:73-82. https://doi.org/10.1016/0304-4165(88)90069-4
- Czichi U, Kindl H. 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 1975;125:115-25.
- Bandoni RJ, Moore K, Subba Rao PV, Towers GH. Phenylalanine and tyrosine ammonia-lyase activity in some Basidiomycetes. Phytochemistry 1968;7:205-7. https://doi.org/10.1016/S0031-9422(00)86316-5
- Moore K, Subba Rao PV, Towers GH. Degradation of phenylalanine and tyrosine by Sporobolomyces roseus. Biochem J 1968;106:507-14. https://doi.org/10.1042/bj1060507
- Hodgins DS. Yeast phenylalanine ammonia-lyase: purification, properties, and the identification of catalytically essential dehydroalanine. J Biol Chem 1971;246:2977-85.
- Sikora LA, Marzluf GA. Regulation of L-phenylalanine ammonia-lyase by L-phenylalanine and nitrogen in Neurospora crassa. J Bacteriol 1982;150:1287-91.
- Emes AV, Vining LC. Partial purification and properties of L-phenylalanine ammonia-lyase from Streptomyces verticillatus. Can J Biochem 1970;48:613-22. https://doi.org/10.1139/o70-099
- Xiang L, Moore BS. Inactivation, complementation, and heterologous expression of encP, a novel bacterial phenylalanine ammonia-lyase gene. J Biol Chem 2002;277:32505-9. https://doi.org/10.1074/jbc.M204171200
- Young MR, Towers GH, Neish AC. Taxonomic distribution of ammonia-lyases for L-phenylalanine and L-tyrosine in relation to lignification. Can J Bot 1966;44:341-9. https://doi.org/10.1139/b66-040
- Vance CP, Bandoni RJ, Towers GHN. Further observations on phenylalanine ammonia-lyase in fungi. Phytochemistry 1975;14:1513-4. https://doi.org/10.1016/0031-9422(75)85341-6
- Nari J, Mouttet Ch, Pinna MH, Ricard J. Some physico-chemical properties of L-phenylalanine ammonia-lyase of wheat seedlings. FEBS Lett 1972;23:220-4. https://doi.org/10.1016/0014-5793(72)80346-6
- Havir EA, Hanson KR. L-phenylalanine ammonia-lyase (maize and potato); evidence that the enzyme is composed of four subunits. Biochemistry 1973;12:1583-91. https://doi.org/10.1021/bi00732a019
- Jorrin J, Dixon RA. Stress reponses in alfalfa (Medicago sativa L.). II. Purification, characterization, and induction of phenylalanine ammonia-lyase isoforms from elicitor-treated cell suspension cultures. Plant Physiol 1990;92:447-55. https://doi.org/10.1104/pp.92.2.447
- Bernards MA, Ellis BE. Phenylalanine ammonia-lyase from tomato cell cultures inoculated with Verticillium albo-atrum. Plant Physiol 1991;97:1494-500. https://doi.org/10.1104/pp.97.4.1494
- Campbell MM, Ellis BE. Fungal elicitor-mediated responses in pine cell cultures. III Purification and characterization of phenylalanine ammonia-lyase. Plant Physiol 1992;98:62-70. https://doi.org/10.1104/pp.98.1.62
- Given NK, Venis MA, Grierson D. Purification and properties of phenylalanine ammonia-lyase from strawberry fruit and its synthesis during ripening. J Plant Physiol 1988;133:31-7. https://doi.org/10.1016/S0176-1617(88)80080-4
- Pridham JB, Woodhead S. Multimolecular forms of phenylalanine-ammonia lyase in Alternaria. Biochem Soc Trans 1974;2:1070-2. https://doi.org/10.1042/bst0021070
- Kalghatgi KK, Subba Rao PV. Microbial L-phenylalanine ammonia-lyase: purification, subunit structure and kinetic properties of the enzyme from Rhizoctonia solani. Biochem J 1975;149:65-72. https://doi.org/10.1042/bj1490065
- Hanson KR, Havir EA. Phenylalanine ammonia-lyase. In: Stumpf PK, Conn EE, editors. Biochemistry of plants: a comprehensive treatise. Vol. 7. New York: Academic Press; 1981. p. 577-625.
- Schomburg D, Salzmann M. Enzyme handbook 1. Class 4: lyases, phenylalanine ammonia-lyase. Berlin, Heidelberg: Springer-Verlag; 1990.
- Hao Z, Charles DJ, Yu L, Simon JE. Purification and characterization of a phenylalanine ammonia-lyase from Ocimum basilicum. Phytochemistry 1996;43:735-9. https://doi.org/10.1016/0031-9422(96)00168-9
- Kim SH, Kronstad JW, Ellis BE. Purification and characterization of phenylalanine ammonia-lyase from Ustilago maydis. Phytochemistry 1996;43:351-7. https://doi.org/10.1016/0031-9422(96)00282-8
- Neumann G, Schwemmle B. Flavonoids from Oenothera seedlings: identification and extranuclear control of their biosynthesis. J Plant Physiol 1993;142:135-43. https://doi.org/10.1016/S0176-1617(11)80953-3
- Adachi O, Matsushita K, Shinagawa E, Ameyama M. Crystallization and properties of L-phenylalanine ammonia-lyase from Rhodosporidium toruloides. Agric Biol Chem 1990;54:2839-43. https://doi.org/10.1271/bbb1961.54.2839
- Dahiya JS. Isolation and chalacterization of phenylalanine ammonia-lyase enzyme from the fungus Leptosphaeria maculans. Indian J Exp Biol 1993;31:874-7.
- Bolwell GP, Rodgers MW. L-Phenylalanine ammonia-lyase from French bean (Phaseolus vulgaris L.): characterization and differential expression of antigenic multiple Mr forms. Biochem J 1991;279(Pt 1):231-6. https://doi.org/10.1042/bj2790231
- McKegney GR, Butland SL, Theilmann D, Ellis BE. Expression of poplar phenylalanine ammonia-lyase in insect cell cultures. Phytochemistry 1996;41:1259-63. https://doi.org/10.1016/0031-9422(95)00677-X
- Dubery IA, Smit F. Phenylalanine ammonia-lyase from cotton (Gossypium hirsutum) hypocotyls: properties of the enzyme induced by a Verticillium dahliae phytotoxin. Biochim Biophys Acta 1994;1207:24-30. https://doi.org/10.1016/0167-4838(94)90047-7
- D'Cunha GB, Satyanarayan V, Nair PM. Purification of phenylalanine ammonia lyase from Rhodotorula glutinis. Phytochemistry 1996;42:17-20. https://doi.org/10.1016/0031-9422(95)00914-0
- Gowri G, Paiva NL, Dixon RA. Stress responses in alfalfa (Medicago sativa L.) 12. Sequence analysis of phenylalanine ammonia-lyase (PAL) cDNA clones and appearance of PAL transcripts in elicitor-treated cell cultures and developing plants. Plant Mol Biol 1991;17:415-29. https://doi.org/10.1007/BF00040636
- Havir EA. L-phenylalanine ammonia-lyase: binding of polysaccharide by the enzyme from maize. Plant Sci Lett 1979;16:297-304. https://doi.org/10.1016/0304-4211(79)90042-7
- Shaw NM, Bolwell GP, Smith C. Wound-induced phenylalanine ammonia-lyase in potato (Solanum tuberosum) tuber discs: significance of glycosylation and immunolocalization of enzyme subunits. Biochem J 1990;267:163-70. https://doi.org/10.1042/bj2670163
- Cramer CL, Edwards K, Dron M, Liang X, Dildine SL, Bolwell GP, Dixon RA, Lamb CJ, Schuch W. Phenylalanine ammonia-lyase gene organization and structure. Plant Mol Biol 1989;12:367-83. https://doi.org/10.1007/BF00017577
- Lois R, Dietrich A, Hahlbrock K, Schulz W. A phenylalanine ammonia-lyase gene from parsley: structure, regulation, and identification of elicitor and light responsive cis-acting elements. EMBO J 1989;8:1641-8.
- Orum H, Rasmussen OF. Expression in E. coli of the gene encoding phenylalanine ammonia-lyase from Rhodosporidium toruloides. Appl Microbiol Biotechnol 1992;36:745-7.
- Schulz W, Eiben HG, Hahlbrock K. Expression in Escherichia coli of catalytically active phenylalanine ammonia-lyase from parsley. FEBS Lett 1989;258:335-8. https://doi.org/10.1016/0014-5793(89)81687-4
- Appert C, Logemann E, Hahlbrock K, Schmid J, Amrhein N. Structural and catalytic properties of the four phenylalanine ammonia-lyase isoenzymes from parsley (Petroselinum crispum Nym.). Eur J Biochem 1994;225:491-9. https://doi.org/10.1111/j.1432-1033.1994.00491.x
- Calabrese JC, Jordan DB, Boodhoo A, Sariaslani S, Vannelli T. Crystal structure of phenylalanine ammonia lyase: multiple helix dipoles implicated in catalysis. Biochemistry 2004;43:11403-16. https://doi.org/10.1021/bi049053+
- Hanson KR, Havir EA. The enzymic elimination of ammonia. In: Boyer PD, editor. The enzymes. New York: Academic Press; 1972. p. 75-166.
- Hanson KR, Havir EA. L-Phenylalanine ammonia-lyase. IV. Evidence that the prosthetic group contains a dehydroalanyl residue and mechanism of action. Arch Biochem Biophys 1970;141:1-17. https://doi.org/10.1016/0003-9861(70)90100-1
- Schuster B, Retey J. The mechanism of action of phenylalanine ammonia-lyase: the role of prosthetic dehydroalanine. Proc Natl Acad Sci U S A 1995;92:8433-7. https://doi.org/10.1073/pnas.92.18.8433
- Banerjee S, Hansen JN. Structure and expression of a gene encoding the precursor of subtilin, a small protein antibiotic. J Biol Chem 1988;263:9508-14.
- Ohmiya Y, Hayashi H, Kondo T, Kondo Y. Location of dehydroalanine residues in the amino acid sequence of bovine thyroglobulin: identification of "donor" tyrosine sites for hormonogenesis in thyroglobulin. J Biol Chem 1990;265:9066-71.
- Recsei PA, Snell EE. Pyruvoyl enzymes. Annu Rev Biochem 1984;53:357-87. https://doi.org/10.1146/annurev.bi.53.070184.002041
- Taylor RG, Lambert MA, Sexsmith E, Sadler SJ, Ray PN, Mahuran DJ, McInnes RR. Cloning and expression of rat histidase: homology of two bacterial histidases and four phenylalanine ammonia-lyases. J Biol Chem 1990;265:18192-9.
- Neish AC. Biosynthetic pathways of aromatic compounds. Annu Rev Plant Physiol 1960;11:55-80. https://doi.org/10.1146/annurev.pp.11.060160.000415
- Parkhurst JR, Hodgins DS. Phenylalanine and tyrosine ammonia-lyase activity in Sporobolomyces pararoseus. Phytochemistry 1971;10:2997-3000. https://doi.org/10.1016/S0031-9422(00)97341-2
- Scott DA, Hammond PM, Brearley GM, Price CP. Identification by high-performance liquid chromatography of tyrosine ammonia-lyase activity in purified fractions of Pheseolus vulgaris phenylalanine ammonia-lyase. J Chromatogr 1992;573:309-12. https://doi.org/10.1016/0378-4347(92)80134-C
- Jangaard NO. The characterization of phenylalanine ammonia-lyase from several plant species. Phytochemistry 1974;13:1765-8. https://doi.org/10.1016/0031-9422(74)85086-7
- ROsler J, Krekel F, Amrhein N, Schmid J. Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity. Plant Physiol 1997;113:175-9. https://doi.org/10.1104/pp.113.1.175
- Nari J, Mouttet C, Fouchier F, Ricard J. Subunit interactions in enzyme catalysis. Eur J Biochem 1974;41:499-515. https://doi.org/10.1111/j.1432-1033.1974.tb03291.x
- Bolwell GP, Bell JN, Cramer CL, Schuch W, Lamb CJ, Dixon RA. L-Phenylalanine ammonia-lyase from Phaseolus vulgaris: characterization and differential induction of multiple forms from elicitor-treated cell suspension cultures. Eur J Biochem 1985;149:411-9. https://doi.org/10.1111/j.1432-1033.1985.tb08941.x
- Nagai N, Kojima Y, Shimosaka M, Okazaki M. Effect of kinetin on L-phenylalanine ammonia-lyase activity in tobacco cell culture. Agric Biol Chem 1988;52:2617-9. https://doi.org/10.1271/bbb1961.52.2617
- Zon J, Amrhein N. Inhibitor of phenylalanine ammonia-lyase: 2-aminoindan-2-phosphonic acid and related compounds. Liebigs Ann Chem 1992;1992;625-8. https://doi.org/10.1002/jlac.1992199201107
- Fritz RR, Hodgins DS, Abell CW. Phenylalanine ammonia-lyase: induction and purification from yeast and clearance in mammals. J Biol Chem 1976;251:4646-50.
- Tanaka Y, Matsuoka M, Yamanoto N, Ohashi Y, Kano-Murakami Y, Ozeki Y. Structure and characterization of a cDNA clone for phenylalanine ammonia-lyase from cut-injured roots of sweet potato. Plant Physiol 1989;90:1403-7. https://doi.org/10.1104/pp.90.4.1403
- Joos HJ, Halhbrock K. Phenylalanine ammonia-lyase in potato (Solanum tuberosum L.): genomic complexity, structural comparison of two selected genes, and modes of expression. Eur J Biochem 1992;204:621-9. https://doi.org/10.1111/j.1432-1033.1992.tb16675.x
- Whetten RW, Sederoff RR. Phenylalanine ammonia-lyase from loblolly pine: purification of the enzyme and isolation of complementary DNA clones. Plant Physiol 1992;98:380-6. https://doi.org/10.1104/pp.98.1.380
- Anson JG, Gilbert HJ, Oram JD, Minton NP. Complete nucleotide sequence of the Rhodosporidium toruloides gene coding for phenylalanine ammonia-lyase. Gene 1987;58:189-99. https://doi.org/10.1016/0378-1119(87)90375-1
- Vaslet CA, Strausberg RL, Sykes A, Levy A, Filpula D. cDNA and genomic cloning of yeast phenylalanine ammonia-lyase reveal genomic intron deletions. Nucleic Acids Res 1988;16:11382. https://doi.org/10.1093/nar/16.23.11382
- Wanner LA, Li G, Ware D, Somssich IE, Davis KR. The phenylalanine ammonia-lyase gene family in Arabidopsis thaliana. Plant Mol Biol 1995;27:327-38. https://doi.org/10.1007/BF00020187
- Campbell MM. Elicited phenylpropanoid metabolism in pine cell cultures [dissertation]. Guelph: University of Guelph; 1991.
- Sederoff R, Campbell M, O'Malley D, Whetten R. Genetic regulation of lignin biosynthesis and the potential modification of wood by genetic engineering in loblolly pine. Recent Adv Phytochem 1994;28:313-55.
- Kim SH, Virmani D, Wake K, MacDonald K, Kronstad JW, Ellis BE. Cloning and disruption of a phenylalanine ammonia-lyase gene from Ustilago maydis. Curr Genet 2001;40:40-8. https://doi.org/10.1007/s002940100230
- Wat CK, Towers GH. Metabolism of the aromatic amino acids by fungi. Recent Adv Phytochem 1977;12:371-432.
- Power DM, Towers GH, Neish AC. Biosynthesis of phenolic acids by certain wood-destroying Basidiomycetes. Can J Biochem 1965;43:1397-407. https://doi.org/10.1139/o65-157
- Moore K, Subba Rao PV, Towers GH. Degradation of phenylalanine and tyrosine by Basidiomycetes. Life Sci 1967;6:2629-33. https://doi.org/10.1016/0024-3205(67)90113-0
- Uchiyama K, Kawaguchi K, Tochikura T, Ogata K. Metabolism of aromatic amino acids in microorganisms. Part III. Metabolism of cinnamic acid in Rhodotorula. Agric Biol Chem 1969;33:755-63. https://doi.org/10.1271/bbb1961.33.755
- Towers GH. Metabolism of cinnamic acid and its derivatives in Basidiomycetes. In: Harborne JB, Swain T, editors. Perspectives in phytochemistry. New York: Academic Press; 1969. p. 179-91.
- Nambudiri AM, Subba Rao PV, Bhat JV. Metabolism of aromatic compounds by an Alternaria species. Phytochemistry 1970;9:687-93. https://doi.org/10.1016/S0031-9422(00)85165-1
- Kalghatgi KK, Nambudiri AM, Bhat JV, Subba Rao PV. Degradation of L-phenylalanine by Rhizoctonia solani. Indian J Biochem Biophys 1974;11:116-8.
- Campbell IM, Gallo MA, Jones CA, La Sitis PR, Rosato LM. Role of cinnamate in benzoate production in Penicillium brevicompactum. Phytochemistry 1987;26:1413-5. https://doi.org/10.1016/S0031-9422(00)81824-5
- Griffin DH. Fungal physiology. Toronto: Wiley-Less;1994.
- Stith WJ, Hodgins DS, Abell CW. Effects of phenylalanine ammonia-lyase and phenylalanine deprivation on murine leukemic lymphoblasts in vitro. Cancer Res 1973;33:966-71.
- Abell CW, Stith WJ, Hodgins DS. The effects of phenylalanine ammonia-lyase on leukemic lymphocytes in vitro. Cancer Res 1972;32:285-90.
- Abell CW, Hodgins DS, Stith WJ. An in vitro evaluation of the chemotherapeutic potency of phenylalanine ammonia-lyase. Cancer Res 1973;33:2529-32.
- Hoskins JA, Jack G, Wade HE, Peiris RJ, Wright EC, Starr DJ, Stern J. Enzymatic control of phenylalanine intake on phenylketonuria. Lancet 1980;23:392-4.
- Sarkissian CN, Gamez A, Wang L, Charbonneau M, Fitzpatrick P, Lemontt JF, Zhao B, Vellard M, Bell SM, Henschell C, et al. Preclinical evaluation of multiple species of PEGylated recombinant phenylalanine ammonia lyase for the treatment of phenylketonuria. Proc Natl Acad Sci U S A 2008;105: 20894-9. https://doi.org/10.1073/pnas.0808421105
- Klausner A. Building for success in phenylalanine. Bio/Technology 1985;3:301-7. https://doi.org/10.1038/nbt0485-301
- Hamilton BK, Hsiao HY, Swann WE, Anderson DM, Delent JJ. Manufacture of L-amino acids with bioreactors. Trends Biotechnol 1985;3:64-8. https://doi.org/10.1016/0167-7799(85)90079-4