Biotechnological production and applications of microbial phenylalanine ammonia lyase: A recent review

Critical Reviews in Biotechnology

Volumn 34, Issue 3, 2014, Pages 258-268

  Cui, Jian Dong ^a,b,c   Qiu, Ji Qing ^a   Fan, Xian Wei ^d   Jia, Shi Ru ^c   Tan, Zhi Lei ^c  

^a HEBEI UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

^b INSTITUTE OF PROCESS ENGINEERING   (China)

^c TIANJIN UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

^d GUANGXI UNIVERSITY   (China)

Author keywords

Activity; Applications; Biotechnological production; Microbe; Phenylalanine ammonia lyase; Purification; Stability

Indexed keywords

AMMONIA; APPLICATIONS; BACTERIA; BIOTECHNOLOGY; CATALYST ACTIVITY; CONVERGENCE OF NUMERICAL METHODS; ENZYMES; FUNGI; PURIFICATION; THERMODYNAMIC PROPERTIES;

BIOTECHNOLOGICAL APPLICATIONS; BIOTECHNOLOGICAL PRODUCTION; COMMERCIAL SOURCES; MICROBE; NEW APPLICATIONS; PHENYLALANINE AMMONIA-LYASE; PHYSIOLOGICAL ROLES; TRANS-CINNAMIC ACID;

AMINO ACIDS;

AMMONIA; CINNAMIC ACID; MICROBIAL ENZYME; PHENYLALANINE; PHENYLALANINE AMMONIA LYASE;

BIOTECHNOLOGY; CATABOLISM; CYANOBACTERIUM; DEAMINATION; ENZYME MECHANISM; FUNGUS; NONHUMAN; PRIORITY JOURNAL; REVIEW; STREPTOMYCES; BACTERIA; ISOLATION AND PURIFICATION; METABOLISM; MICROBIOLOGY; PROCEDURES;

BACTERIA; FUNGI; INDUSTRIAL MICROBIOLOGY; PHENYLALANINE AMMONIA-LYASE;

EID: 84906234873     PISSN: 07388551     EISSN: 15497801     Source Type: Journal    
DOI: 10.3109/07388551.2013.791660     Document Type: Review

References (128)

1. Abell CW, Hodgins DS, Stith WJ. (1973). An in vitro evaluation of the chemotherapeutic potency of phenylalanine ammonia lyase. Cancer Res, 33, 2529-32.
2. Abell CW, Stith WJ, Hodgins DS. (1972). The effects of phenylalanine ammonia-lyase on leukemic lymphocytes in vitro. Cancer Res, 32, 285-90.
3. Adachi Q, Matsushita K, Shinagawa E, Ameyama M. (1990). Crystallization and properties of L-phenylalanine ammonia lyase from Rhodosporidium toruloides. Agric Biol Chem, 54, 2839-43.
4. Allwood EG, Davies DR, Gerrish C, et al. (1999). Phosphorylation of phenylalanine ammonia-lyase: evidence for a novel protein kinase and identification of the phosphorylated residue. FEBS Lett, 457, 47-52.
5. Anson JG, Gilbert HJ, Oram JD, Minton NP. (1987). Complete nucleotide sequence of the Rhodosporidium toruloides gene coding for phenylalanine ammonia-lyase. Gene, 58, 189-99.
6. Ates S, Doǧan NS. (2010). Properties of immobilized phenylalanine ammonia lyase and investigation of its use for the prediagnosis of phenylketonuria. Turk J Biochem, 35, 58-62.
7. Aydas SB, Ozturk S, Ashm B. (2013). Phenylalanine ammonia lyase enzyme activity and antioxidant properties of some cyanobacteria isolates. Food Chem, 136, 164-9.
8. Aytar BS, Bakir U. (2008). Preparation of cross-linked tyrosinase aggregates. Process Biochem, 43, 125-31.
9. Barratt ES, adams PM, Poffenbarger PL, et al. (1976). Effects of rapid depletion of phenylalanine and tyrosine on sleep and behavior. Pharmacol Biochem Behav, 5, 47-53.
10. Bartsch S, Bornscheuer UT. (2010). Mutational analysis of phenylalanine ammonia lyase to improve reactions rates for various substrates. Protein Eng Des Sel, 23, 929-33.
11. Bazukian IL, Vardanian AE, Ambartsumian AA, et al. (2009). Catalytic properties of Rhodotorula aurantiaca KM-1 phenylalanine ammonialyase. Prikl Biokhim Mikrobiol, 45, 23-7.
12. Bazukyan IL, Hambardzumyan AA, Vardanyan AE. (2006). Phenylalanine ammonia lyase of Rhodotorula aurantiaca: purification and primary characteristics. In: Zaikov GE, ed. Biocatalysis and Biocatalytic Technology. New York: Nova Science Publishers Inc., 9-21.
13. Bernards MA, Ellis BE. (1991). Phenylalanine ammonia-lyase from tomato cell cultures inoculated with Verticillium albo-atrum. Plant Physiol, 97, 1494-500.
14. Berner M, Krug D, Bihlmaier C, et al. (2006). Genes and enzymes involved in caffeic acid biosynthesis in the actinomycete Saccharotrix espanaensis. J Bacteriol, 188, 2666-73.
15. Bolwell GP. (1992). A role for phosphorylation in the down-regulation of phenylalanine ammonia-lyase in suspension-cultured cells of french bean. Phytochemistry, 31, 4081-86.
16. Bourget L, Chang TMS. (1985). Phenylalanine ammonia lyase immobilized in semipermeable microcapsule for enzyme replacement in phenylketonuria. FEBS Lett, 180, 5-8.
17. Bourget L, Chang TMS. (1986). Phenylalanine ammonia-lyase immobilized in microcapsules for the depletion of phenylalanine in plasma in phenylketonuric rat model. Biochim Biophys Acta, 883, 432-8.
18. Calabrese JC, Jordan DB, Boodhoo A, et al. (2004). Crystal structure of phenylalanine ammonia lyase: multiple helix dipoles implicated in catalysis. Biochemistry, 43, 11403-16.
19. Camm EL, Towers GHN. (1973). Review article: phenylalanine ammonia lyase. Phytochemistry, 12, 961-73.
20. Chesters C, Wilding M, Goodall M, Mickefield J. (2012). Thermal bifunctionality of bacterial phenylalanine aminomutase and ammonia lyase enzymes. Angew Chem Int Ed Engl, 124, 4420-24.
21. Cramer CL, Edwards K, Dron M, et al. (1989). Phenylalanine ammonialyase gene organization and structure. Plant Mol Biol, 12, 367-83.
22. Cui JD, Huang H, Qiao CS, Jia ShR. (2007). Stability of phenylalanine ammonia lyase of recombinant Escherichia coli and conversion of trans-cinnamic acids. Chem React Eng Tech, 23, 326-31.
23. Cui JD, Jia ShR, Sun AiY. (2008). Influence of amino acids, organic solvents and surfactants for phenylalanine ammonia lyase activity in recombinant Escherichia coli. Lett Appl Microbial, 46, 631-5.
24. Cui JD, Li Y. (2009). Optimal culture condition for the production of phenyalanine ammonia lyase from E. coli. Korean J Chem Eng, 26, 444-8.
25. Cui JD, Zhang S, Sun LM. (2012). Cross-linked enzyme aggregates of phenylalanine ammonia lyase: novel biocatalysts for synthesis of L-phenylalanine. Appl Biochem Biotechnol, 167, 835-44.
26. D'Cunha GB. (2005). Enrichment of phenylalanine ammonia lyase activity of Rhodotorula yeast. Enzyme Microb Technol, 36, 498-502.
27. D'Cunha GB, Satyanarayan V, Nair PM. (1996a). Stabilization of phenylalanine ammonia lyase containing Rhodotorula glutinis cells for the continuous synthesis of L-phenylalanine methyl ester. Enzyme Microb Technol, 19, 421-7.
28. D'Cunha GB, Satyanarayan V, Nair PM. (1996b). Purification of phenylalanine ammonia lyase from Rhodotorula glutinis. Phytochemistry, 42, 17-20.
29. Decleire M, Cat WDe, Huynh Van N. (1987). Comparison of various permeabilization treatments on Kluyveromyces by determining in situ b-galactosidase activity. Enzyme Microb Technol, 5, 300-2.
30. Ding X, Wu M, Cen P. (1994). Studies on the induction of L-phenylalanine ammonia lyase (PAL) in Rhodotorula glutinis and transformation of phenylalanine from trans-cinnamic acid. Wei Sheng Wu Xue Bao, 34, 137-42.
31. El-Batal AI. (2002a). Optimization of reaction conditions and stabilization of phenylalanine ammonia lyase-containing Rhodotorula glutinis cells during bioconversion of trans-cinnamic acid to L-phenylalanine. Acta Microbiol Pol, 51, 139-52.
32. El-Batal AI. (2002b). Continuous production of L-phenylalanine by Rhodotorula glutinis immobilized cells using a column reactor. Acta Microbiol Pol, 51, 153-69.
33. EI-Batal AI, Abo-State MA, Shihab A. (2000). Phenylalanine ammonia lyase production by gamma irradiated and analog-resistant mutants of Rhodotorula glutinis. Acta Microbiol Pol, 49, 51-61.
34. Emes AV, Vining LC. (1970). Partial purification and properties of Lphenylalanine ammonia-lyase from Streptomyces verticillatus. Can J Biochem, 48, 613-22.
35. Evans CT, Choma C, PetersonW, Misawa M. (1987a). Effect of glycerol, polyethylene glycol and glutaraldehyde on stability of phenylalanine ammonia-lyase activity in yeast. J Ind Microbiol Biot, 2, 53-8.
36. Evans CT, Conrad D, Hanna K, et al. (1987b). Novel stabilization of phenylalanine ammonia lyase catalyst during bioconversion of trans-cinnamic acid to L-phenylalanine. Appl Microbiol Biotechnol, 25, 399-405.
37. Evans CT, Hanna K, Payne Ch, et al. (1987c). Biotransformation of trans-cinnamic acid to L-phenylalanine: optimization of reaction conditions using whole yeast cells. Enzyme Microb Technol, 9, 417-21.
38. Faulkner JDB, Anson JG, Tuite MF. (1994). High-level expression of the phenylalanine ammonia lyase-encoding gene from Rhodosporidium toruloides in Saccharomyces cerevisiae and Escherichia coli using a bifunctional expression system. Gene, 143, 13-20.
39. Filpula D, Strausberg RL, Vaslet CA, et al. (1988). Nucleotide sequence of gene for phenylalanine ammonia-lyase from Rhodotorula rubra. Nucleic Acids Res, 16, 11381.
40. Fiske MJ, Kane JF. (1984). Regulation of phenylalanine biosynthesis in Rhodotorula glutinis. J Bacteriol, 160, 676-81.
41. Fritz RR, Hodgins DS, Abell CW. (1976). Phenylalanine ammonia lyase: induction and purification from yeast and clearance in mammals. J Biol Chem, 251, 4646-50.
42. Gámez A, Sarkissian CN, Wang L, et al. (2005). Development of pegylated forms of recombinant Rhodosporidium toruloides phenylalanine ammonia-lyase for the treatment of classical phenylketonuria. Mol Ther, 11, 986-9.
43. Gámez A, Wang L, Sarkissian CN, et al. (2007). Structure-based epitope and PEGylation sites mapping of phenylalanine ammonia-lyase for enzyme substitution treatment of phenylketonuria. Mol Genet Metab, 91, 325-34.
44. Gilbert HJ, Clarke IN, Stephenson JR, Tully M. (1985). Molecular cloning of the phenylalanine ammonia lyase gene from Rhodosporidium toruloides in Escherichia coli K-12. J Bacteriol, 161, 314-20.
45. Gilbert HJ, Stephenson JR, Tully M. (1983). Control of synthesis of functional mRNA coding for phenylalanine ammonia-lyase from Rhodosporidium toruloides. J Bacteriol, 153, 1147-54.
46. Gilbert HJ, Tully M. (1982). Synthesis and degradation of phenylalanine ammonia-lyase of Rhodosporidium toruloides. J Bacteriol, 150, 498-505.
47. Gloge A, Zoń J, Kövári A, et al. (2000). Phenylalanine ammonia-lyase: the use of its broad substrate specificity for mechanistic investigations and biocatalysis-synthesis of L-aryl alanines. Chemistry, 15, 3386-90.
48. Gough S, Deshpande M, Scher M, Rosazza JPN. (2001). Permeabilization of Pichia pastoris for glycolate oxidase activity. Biotechnol Lett, 18, 1535-37.
49. Gubica T, Pełka A, Pełka K, et al. (2011). The influence of cyclo malto oligosaccharides (cyclodextrins) on the enzymatic decomposition of L-phenylalanine catalyzed by phenylalanine ammonia-lyase. Carbohyd Res, 346, 1855-59.
50. Guo J, Wang MH. (2009). Characterization of the phenylalanine ammonia-lyase gene (SlPAL5) from tomato (Solanum lycopersicum L.). Mol Biol Rep, 36, 1579-85.
51. Habibi-Moini S, D'mello AP. (2001). Evaluation of possible reasons for the low phenylalanine ammonia lyase activity in cellulose nitrate membrane microcapsules. Int J Pharm, 215, 185-96.
52. Havir EA, Hanson KR. (1968). L-phenylalanine ammonia lyase. II. Mechanism and kinetic properties of the enzyme from potato tubers. Biochemistry, 7, 1904-14.
53. Havir EA, Hanson KR. (1973). L-phenylalanine ammonia-lyase (maize and potato); evidence that the enzyme is composed of four subunits. Biochemistry, 12, 1583-91.
54. Havir EA, Hanson KR. (1975). L-phenylalanine ammonia lyase (maize, potato, and Rhodotorula glutinis). Studies of the prosthetic group with nitromethane, Biochemistry, 14, 1620-26.
55. Hodgins DS. (1971). Yeast phenylalanine ammonia lyase: purification, properties, and the identification of catalytically essential dehydroalanine. J Biol Chem, 246, 2977-85.
56. Hyun MW, Yun YH, Kim JY, Kim SH. (2011). Fungal and plant phenylalanine ammonia lyase. Mycobiology, 39, 257-65.
57. Jia ShR, Cui JD, Li Y, Sun AiY. (2008). Production of L-phenylalanine from trans-cinnamic acids by high-level expression of phenylalanine ammonia lyase gene from Rhodosporidium toruloides in Escherichia coli. Biochem Eng J, 42, 193-7.
58. Jiang H, Wood KV, Morgan JA. (2005). Metabolic engineering of the phenylpropanoid pathway in Saccharomyces cerevisiae. Appl Environ Microbiol, 71, 2962-69.
59. Jones DH. (1984). Phenylalanine ammonia-lyase: regulation of its induction, and its role in plant development. Phytochemistry, 23, 1349-59.
60. Joos HJ, Hahlbrock K. (1992). Phenylalanine ammonia-lyase in potato (Solanum tuberosum L). Eur J Biochem, 204, 621-9.
61. Kalghatgi K, Horvath C, Ambrus CM. (1980). Multitubular reactors with immobilized L-phenylalanine ammonia-lyase for use in extracorporeal shunts. Res Commun Chem Pathol Pharmacol, 27, 551-61.
62. Kalghatgi KK, Rao PVS. (1975). Microbial L-phenylalanine ammonialyase: purification, subunit structure and kinetic properties of the enzyme from Rhizoctonia solani. Biochem J, 149, 65-72.
63. Kim W, Erlandsen H, Surendran S, et al. (2004). Trends in enzyme therapy for phenylketonuria. Mol Ther, 10, 220-4.
64. Kim SH, Kronstad JW, Ellis BE. (1996). Purification and characterization of phenylalanine ammonia-lyase from Ustilago maydis. Phytochemistry, 43, 351-7.
65. Kim SH, Virmani D, Wake K, et al. (2001). Cloning and disruption of a phenylalanine ammonia lyase gene from Ustilago maydis. Curr Genet, 40, 40-8.
66. Klausner A. (1985). Building for success in phenylalanine. Nat Biotechnol, 3, 301-7.
67. Klibanov AM. (2001). Improving enzymes by using them in organic solvents. Nature, 409, 241-6.
68. Kumar A, Ellis BE. (2001). The phenylalanine ammonia-lyase gene family in raspberry, Structure, expression, and evolution. Plant Physiol, 127, 230-9.
69. Kyndt JA, Meyer TE, Cusanovich MA, et al. (2002). Characterization of a bacterial tyrosine ammonia lyase, a biosynthetic enzyme for the photoactive yellow protein. FEBS Lett, 512, 240-4.
70. Liang XW, Dron M, Cramer CL, et al. (1989). Differential regulation of phenylalanine ammonia-lyase genes during plant development and by environmental cues. J Biol Chem, 264, 14486-92.
71. Langer B, Rother D, Retey J. (1997). Identification of essential amino acids in phenylalanine ammonia lyase by site-directed mutagenesis. Biochemistry, 36, 10867-71.
72. Levy HL. (1999). Phenylketonuria: old disease, new approach to treatment. Proc Natl Acad Sci USA, 96, 1811-13.
73. Liu J, Jia X, Zhang J, et al. (2002). Study on a novel strategy to treatment of phenylketonuria. Artif Cells Blood Substit Immobil Biotechnol, 30, 243-57.
74. Lois R, Dietrich A, Hahlbrock K, 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, 1641-8.
75. Louie GV, Bowman ME, Moffitt MC, et al. (2006). Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases. Chem Biol, 13, 1327-38.
76. MacDonald MJ, D'Cunha GB. (2007). A modern view of phenylalanine ammonia lyase. Biochem Cell Biol, 85, 273-82.
77. Marusich WC, Jensen RA, Zamir LO. (1981). Induction of L-phenylalanine ammonia-lyase during utilization of phenylalanine as carbon or nitrogen source in Rhodotorula glutinis. J Bacteriol, 146, 1013-9.
78. Mateo C, Palomo JM, Langen LM, et al. (2004). A new, mild crosslinking methodology to prepare cross-linked enzyme aggregates. Biotechnol Bioeng, 15, 273-6.
79. McKegney GR, Butland SL, Theilmann D, Ellis BE. (1996). Expression of poplar phenylalanine ammonia lyase in insect cell cultures. Phytochemistry, 41, 1259-63.
80. Minami E, Ozeki Y, Matsuoka N, Tanaka Y. (1989). Structure and some characterization of the gene for phenylalanine ammonia lyase from ice plants. Eur J Biochem, 185, 19-25.
81. Moffitt MC, Louie GV, Bowman ME, et al. (2007). Discovery of two cyanobacterial phenylalanine ammonia lyases: kinetic and structural characterization. Biochemistry, 46, 1004-12.
82. Monge RI, Lara M, Lopez-Munguia A. (1995). Purification and stabilization of phenylalanine ammonia lyase from Sporidiobolus pararoseus. Biotechnol Tech, 9, 423-8.
83. Nagalakshmi V, Pai JS. (1994). Permeabilization of Escherichia coli cells for enhanced penicillin acylase activity. Biotechnol Tech, 6, 431-4.
84. Nakamichi K, Yamada NS, Chibata I. (1983). Induction and stabilization of L-phenylalanine ammonia lyase activity in Rhodotorula glutinis. Eur J Appl Microbiol Biotechnol, 18, 158-62.
85. Nehls U, Ecke M, Hampp R. (1999). Sugar-and nitrogen-dependent regulation of an Amanita muscaria phenylalanine ammonium lyase gene. J Bacteriol, 181, 1931-3.
86. Noda S, Miyazaki T, Miyoshi T, et al. (2011). Cinnamic acid production using Streptomyces lividans expressing phenylalanine ammonia lyase. J Ind Microbiol Biotechnol, 38, 643-8.
87. Ogata K, Uchiyama K, Yamada H. (1966). Microbial formation of cinnanic acid from phenylalanine. Agric Biol Chem, 30, 311-2.
88. Orndorff SA, Costantino N, Stewart D. (1988). Strain improvement of Rhodotorula graminis for production of a novel L-phenylalanine ammonia-lyase. Appl Environ Microbiol, 54, 996-1002.
89. Orum H, Rasmussen OF. (1992). Expression in E. coli of the gene encoding phenylalanine ammonia lyase from Rhodosporidium toruloides. Appl Microbiol Biotechnol, 36, 745-8.
90. Paizs C, Tosa MI, Bencze LC, et al. (2011). 2-Amino-3-(5-phenylfuran-2- yl) propionic acids and 5-phenylfuran-2-yl acrylic acids are novel substrates of phenylalanine ammonia-lyase. Heterocycles, 82, 1217-28.
91. Parkhurst JR, Hodgins DS. (1972). Yeast phenylalanine ammonia lyase. Properties of the enzyme from Sporobolomyces pararoseus and its catalytic site. Arch Biochem Biophys, 152, 597-605.
92. Pedersen H, Horvath C, Ambrus CM. (1978). Preparation of immobilized L-phenylalanine ammonia-lyase in tubular form for depletion of L-phenylalanine. Res Commun Chem Pathol Pharmacol, 20, 559-69.
93. Pridham JB, Woodhead S. (1974). Multimolecular forms of phenylalanine-ammonia lyase in Alternaria. Biochem Soc Trans, 2, 1070-2.
94. Quinn AJ, Pickup MJ, D'Cunha GB. (2011). Enzyme activity evaluation of organic solvent-treated phenylalanine ammonia lyase. Biotechnol Prog, 27, 1554-60.
95. Ree DG, Jones DH. (1996). Stability of L-phenylalanine ammonia lyase in aqueous solution and as the solid state in air and organic solvents. Enzyme Microb Tech, 19, 282-8.
96. Ree DG, Jones DH. (1997). Activity of L-phenylalanine ammonia lyase in organic solvents. Biochim Biophys Acta, 1338, 121-6.
97. Rosler J, Krekel F, Amrhein N. (1997). Maize phenylalanine ammonia lyase has tyrosine ammonia-lyase activity. Plant Physiol, 113, 175-9.
98. Santiago R, Armas RDe, Legaz ME, Vicente C. (2009). Changes in phenolic acids content, phenylalanine ammonia-lyase and peroxidase activities in sugarcane leaves induced by elicitors isolated from Xanthomonas albilineans. Australas Plant Pathol, 38, 357-65.
99. Sarkissian CN, Boulais DM, McDonald JD, Scriver CR. (2000). A heteroallelic mutant mouse model: a new orthologue for human hyperphenylalaninemia. Mol Genet Metab, 69, 188-94.
100. Sarkissian CN, Kang TS, Gámez A, et al. (2011). Evaluation of orally administered PEGylated phenylalanine ammonia lyase in mice for the treatment of Phenylketonuria. Mol Genet Metab, 104, 249-54.
101. Sarkissian CN, Shao ZhQ, Françoise B, et al. (1999). A different approach to treatment of phenylketonuria: phenylalanine degradation with recombinant phenylalanine ammonia lyase. Proc Natl Acad Sci USA, 96, 2339-44.
102. Shah RM, D'mello AP. (2008). Strategies to maximize the encapsulation efficiency of phenylalanine ammonia lyase in microcapsules. Int J Pharm, 356, 61-8.
103. Sheldon RA. (2007). Cross-linked enzyme aggregates (CLEAs): stable and recyclable biocatalysts. Biochem Soc Trans, 35, 1583-7.
104. Sikora LA, Marzluf GA. (1982). Regulation of L-phenylalanine ammonia lyase by L-phenylalanine and nitrogen in Neurosporo Crassa. J Bacteriol, 150, 1287-92.
105. Stith WJ, Hodgins DS, Abell CW. (1973). Effects of phenylalanine ammonia-lyase and phenylalanine deprivation on murine leukemic lymphoblasts in vitro. Cancer Res, 33, 966-71.
106. Su Y, Li N, Liang ZhQ. (2007). Stabilization of phenylalanine ammonia lyase activity in the yeast. Chem Nat Compd+, 43, 639-40.
107. Takaç S, Akay B, Özdamar TH. (1995). Bioconversion of trans-cinnamic acid to L-phenylalanine by L-phenylalanine ammonia-lyase of Rhodotorula glutinis: parameters and kinetics. Enzyme Microb Technol, 17, 445-52.
108. Vannelli T, Qi WW, Sweigard J, et al. (2007a). Production of p-hydroxycinnamic acid from glucose in Saccharomyces cerevisiae and Escherichia coli by expression of heterologous genes from plants and fungi. Metab Eng, 9, 142-51.
109. Vannelli T, Xue ZhX, Breinig S, Qi WW. (2007b). Sariaslanie F. S, Functional expression in Escherichia coli of the tyrosine-inducible tyrosine ammonia-lyase enzyme from yeast Trichosporon cutaneum for production of p-hydroxycinnamic acid. Enzyme Microb Technol, 41, 413-22.
110. Vaslet CA, Strausberg RL, Sykes A, et al. (1988). cDNA and genomic cloning of yeast phenylalanine ammonia lyase reveal genomic intron deletions. Nucleic Acids Res, 16, 11382.
111. Wall MJ, Quinn AJ, D'Cunha GB. (2008). Manganese (Mn2+)-dependent storage stabilization of Rhodotorula glutinis phenylalanine ammonia lyase activity. J Agric Food Chem, 56, 894-902.
112. Wanner LA, Li G, Ware D, et al. (1995). The phenylalanine ammonialyase gene family in Arabidopsis thaliana. Plant Mol Biol, 27, 327-38.
113. Wang L, Gamez A, Archer H, et al. (2008). Structural and biochemical characterization of the therapeutic Anabaena variabilis phenylalanine ammonia lyase. J Mol Biol, 380, 623-35.
114. Wang L, Gamez A, Sarkissian CN, et al. (2005a). Structure-based chemical modification strategy for enzyme replacement treatment of phenylketonuria. Mol Genet Metab, 86, 134-40.
115. Wang Zh, Chen YZh, Zhang S, Zhou Zh. (2005b). Investigation of a phenylalanine-biosensor system for phenylketonuria detection. Proceeding of the 2005 IEEE, Engineering in Medicine and Biology 27th Annual Conference, Shang Hai, 9, 1913-16.
116. Watanabe SK, Hemandez-Velazco G, Iturbe-Chinas F, Lopez-Mungia A. (1992). Phenylalanine ammonia lyase from Sporidiobolus pararoseus and Rhodosporidium toruloides: application for phenylalanine and tyrosine deamination. World J Microbiol Biotechnol, 8, 406-10.
117. Whetten RW, Sederoff RR. (1992). Phenylalanine ammonia lyase from loblolly pine: purification of the enzyme and isolation of complementary DNA clones. Plant Physiol, 98, 380-6.
118. Wick JF, Willis JE. (1982). Phenylalanine-dependent de novo synthesis of phenylalanine ammonia-lyase from Rhodotorula glutinis. Arch Biochem Biophys, 216, 385-91.
119. Wieder KJ, Palczuk NC, Van EsT, Davis F. (1979). Some properties of polyethylene glycol: phenylalanine ammonia lyase adducts. J Biol Chem, 254, 12579-87.
120. Williams JS, Thomas M, Clarke DJ. (2005). The gene stlA encodes a phenylalanine ammonia-lyase that is involved in the production of a stilbene antibiotic in Photorhabdus luminescens TT01. Microbiology, 151, 2543-50.
121. Woolf LI, Griffiths R, Moncrieff A, et al. (2004). The dietary treatment of phenylketonuria. Arch Dis Child, 33, 31-45.
122. Xiang LK, Moore BS. (2005). Biochemical characterization of a prokaryotic phenylalanine ammonia lyase. J Bacteriol, 187, 4286-9.
123. Yamada S, Nabe K, Izuo N, et al. (1981). Production of L-phenylalanine from trans-cinnamic acid with R. glutinis containing L-phenylalanine ammonia lyase activity. Appl Environ Microbiol, 42, 773-8.
124. Yue H, Yuan Q, Wang W. (2007a). Enhancement of L-phenylalanine production by b-cyclodextrin. J Food Eng, 3, 878-84.
125. Yue HY, Yuan QP, Wang W. (2007b). Purification of phenylalanine ammonia-lyase in PEG1000/Na2SO4 aqueous two-phase system by a two-step extraction. Biochem Eng J, 37, 231-37.
126. Zaks A, Kilbanov AM. (1988). The effect of water on enzyme action in organic media. J Biol Chem, 263, 8017-21.
127. Zhang B, Cui JD, Zhao GX, Jia ShR. (2010). Modeling and optimization of phenylalanine ammonia lyase stabilization in recombinant Escherichia coli for the continuous synthesis of L-phenylalanine on the statistical based experimental designs. J Agric Food Chem, 58, 2795-800.
128. Zhu YX, Liao SY, Ye J, Zhang H. (2012). Cloning and characterization of a novel tyrosine ammonia lyase-encoding gene involved in bagremycins biosynthesis in Streptomyces sp. Biotechnol Lett, 34, 269-74.