Synthetic and therapeutic applications of ammonia-lyases and aminomutases

Chemical Reviews

Volumn 118, Issue 1, 2018, Pages 73-118

  Parmeggiani, Fabio ^a   Weise, Nicholas J ^a   Ahmed, Syed T ^a   Turner, Nicholas J ^b  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; AMMONIA; BIOSYNTHESIS; MEDICAL APPLICATIONS;

BIOSYNTHETIC PATHWAY; FINE CHEMICALS; MEDICAL BIOTECHNOLOGY; PROTEIN FAMILY; STAND -ALONE; THERAPEUTIC APPLICATION; THERAPEUTIC TOOLS;

ENZYMES;

AMINOTRANSFERASE; AMMONIA LYASE; MUTASE; PHENYLALANINE AMMONIA LYASE;

BACTERIUM; BIOCATALYSIS; CHEMISTRY; CLASSIFICATION; ENZYME SPECIFICITY; ENZYMOLOGY; HUMAN; METABOLISM; MOLECULAR MODEL;

AMMONIA-LYASES; BACTERIA; BIOCATALYSIS; HUMANS; INTRAMOLECULAR TRANSFERASES; MODELS, MOLECULAR; PHENYLALANINE AMMONIA-LYASE; SUBSTRATE SPECIFICITY; TRANSAMINASES;

EID: 85042628559     PISSN: 00092665     EISSN: 15206890     Source Type: Journal    
DOI: 10.1021/acs.chemrev.6b00824     Document Type: Review

References (323)

1. Puthan Veetil, V.; Fibriansah, G.; Raj, H.; Thunnissen, A.-M. W. H.; Poelarends, G. J. Aspartase/Fumarase Superfamily: A Common Catalytic Strategy Involving General Base-Catalyzed Formation of a Highly Stabilized Aci-Carboxylate Intermediate. Biochemistry 2012, 51, 4237−4243.
2. Levy, C. W.; Buckley, P. A.; Sedelnikova, S.; Kato, Y.; Asano, Y.; Rice, D. W.; Baker, P. J. Insights into Enzyme Evolution Revealed by the Structure of Methylaspartate Ammonia Lyase. Structure 2002, 10, 105−113.
3. Asuncion, M.; Blankenfeldt, W.; Barlow, J. N.; Gani, D.; Naismith, J. H. The Structure of 3-Methylaspartase from Clostridium tetanomorphum Functions via the Common Enolase Chemical Step. J. Biol. Chem. 2002, 277, 8306−8311.
4. Babbitt, P. C.; Hasson, M. S.; Wedekind, J. E.; Palmer, D. R. J.; Barrett, W. C.; Reed, G. H.; Rayment, I.; Ringe, D.; Kenyon, G. L.; Gerlt, J. A. The Enolase Superfamily: A General Strategy for Enzyme-Catalyzed Abstraction of the α-Protons of Carboxylic Acids. Biochemistry 1996, 35, 16489−16501.
5. Herrmann, G.; Selmer, T.; Jessen, H. J.; Gokarn, R. R.; Selifonova, O.; Gort, S. J.; Buckel, W. Two β-Alanyl-CoA:Ammonia Lyases. FEBS J. 2005, 272, 813−821.
6. Heine, A.; Herrmann, G.; Selmer, T.; Terwesten, F.; Buckel, W.; Reuter, K. High Resolution Crystal Structure of Clostridium propionicum β-Alanyl-CoA:ammonia Lyase, a New Member of the “Hot Dog Fold” Protein Superfamily. Proteins: Struct., Funct., Genet. 2014, 82, 2041−2053.
7. Jeng, I.; Barker, H. A. Purification and Properties of L-3Aminobutyryl Coenzyme A Deaminase from a Lysine-Fermenting Clostridium. J. Biol. Chem. 1974, 249, 6578−6584.
8. Barker, H. A.; Kahn, J. M.; Chew, S. Enzymes Involved in 3,5-Diaminohexanoate Degradation by Brevibacterium sp. J. Bacteriol. 1980, 143, 1165−1170.
9. Turner, N. J. Ammonia Lyases and Aminomutases as Biocatalysts for the Synthesis of α-Amino and β-Amino Acids. Curr. Opin. Chem. Biol. 2011, 15, 234−240.
10. Heberling, M. M.; Wu, B.; Bartsch, S.; Janssen, D. B. Priming Ammonia Lyases and Aminomutases for Industrial and Therapeutic Applications. Curr. Opin. Chem. Biol. 2013, 17, 250−260.
11. Cooke, H. A.; Christianson, C. V.; Bruner, S. D. Structure and Chemistry of 4-Methylideneimidazole-5-One Containing Enzymes. Curr. Opin. Chem. Biol. 2009, 13, 460−468.
12. MacDonald, M. J.; D’Cunha, G. B. A Modern View of Phenylalanine Ammonia Lyase. Biochem. Cell Biol. 2007, 85, 273−282.
13. Kumavath, R. N.; Ramana, C. V.; Sasikala, C.; Barh, D.; Kumar, A. P.; Azevedo, V. Isolation and Characterization of L-Tryptophan Ammonia Lyase from Rubrivivax benzoatilyticus Strain JA2. Curr. Protein Pept. Sci. 2015, 16, 775−781.
14. Retey, J. Discovery and Role of Methylidene Imidazolone, a Highly Electrophilic Prosthetic Group. Biochim. Biophys. Acta, Proteins Proteomics 2003, 1647, 179−184.
15. Poppe, L.; Retey, J. Properties and Synthetic Applications of Ammonia-Lyases. Curr. Org. Chem. 2003, 7, 1297−1315.
16. Cui, J. D.; Qiu, J. Q.; Fan, X. W.; Jia, S. R.; Tan, Z. L. Biotechnological Production and Applications of Microbial Phenylalanine Ammonia Lyase: A Recent Review. Crit. Rev. Biotechnol. 2014, 34, 258−268.
17. Kong, J.-Q. Phenylalanine Ammonia-Lyase, a Key Component Used for Phenylpropanoids Production by Metabolic Engineering. RSC Adv. 2015, 5, 62587−62603.
18. Poppe, L.; Paizs, C.; Kovaćs, K.; Irimie, F. D.; Vertessy, B. G. Preparation of Unnatural Amino Acids with Ammonia-Lyases and 2,3-Aminomutases. Methods Mol. Biol. 2012, 794, 3−19.
19. Yamada, T.; Komoto, J.; Takata, Y.; Ogawa, H.; Pitot, H. C.; Takusagawa, F. Crystal Structure of Serine Dehydratase from Rat Liver. Biochemistry 2003, 42, 12854−12865.
20. 6 Enzyme from Escherichia coli. J. Biol. Chem. 1952, 198, 363−373.
21. Viola, R. E. L-Aspartase: New Tricks from an Old Enzyme. Adv. Enzymol. Relat. Areas Mol. Biol. 2006, 74, 295−341.
22. De Villiers, M.; Puthan Veetil, V.; Raj, H.; De Villiers, J.; Poelarends, G. J. Catalytic Mechanisms and Biocatalytic Applications of Aspartate and Methylaspartate Ammonia Lyases. ACS Chem. Biol. 2012, 7, 1618−1628.
23. Mizobata, T.; Kawata, Y. Aspartases: Molecular Structure, Biochemical Function and Biotechnological Applications. Industrial Enzymes: Structure, Function and Applications 2007, 549−565.
24. Nishimura, J. S.; Greenberg, D. M. Purification and Properties of L-Threonine Dehydrase of Sheep Liver. J. Biol. Chem. 1961, 236, 2684−2691.
25. Phillips, A. T.; Wood, W. A. The Mechanism of Action of 5′-Adenylic Acid-Activated Threonine Dehydrase. J. Biol. Chem. 1965, 240, 4703−4709.
26. Wada, M.; Matsumoto, T.; Nakamori, S.; Sakamoto, M.; Kataoka, M.; Liu, J.-Q.; Itoh, N.; Yamada, H.; Shimizu, S. Purification and Characterization of a Novel Enzyme, L-threo-3-Hydroxyaspartate Dehydratase, from Pseudomonas sp. T62. FEMS Microbiol. Lett. 1999, 179, 147−151.
27. Iwamoto, R.; Imanaga, Y.; Soda, K. D-Glucosaminate Dehydratase from Agrobacterium radiobacter. Physicochemical and Enzymological Properties. J. Biochem. 1982, 91, 283−289.
28. Nagasawa, T.; Tanizawa, K.; Satoda, T.; Yamada, H. Diaminopropionate Ammonia-Lyase from Salmonella typhimurium. J. Biol. Chem. 1988, 263, 958−964.
29. Cooper, A. J. L.; Meister, A. Enzymatic Conversion of O-Carbamyl-L-Serine to Pyruvate and Ammonia. Biochem. Biophys. Res. Commun. 1973, 55, 780−787.
30. Iwamoto, R.; Imanga, Y. Enzymatic Microdetermination of D-Glucosaminate with D-Glucosaminate Dehydratase. Anal. Lett. 1982, 15, 161−169.
31. Ito, T.; Takahashi, K.; Naka, T.; Hemmi, H.; Yoshimura, T. Enzymatic Assay of D-Serine Using D-Serine Dehydratase from Saccharomyces cerevisiae. Anal. Biochem. 2007, 371, 167−172.
32. Bradbeer, C. The Clostridial Fermentations of Choline and Ethanolamine. I. Preparation and Properties of Cell-Free Extracts. J. Biol. Chem. 1965, 240, 4669−4674.
33. Bradbeer, C. The Clostridial Fermentations of Choline and Ethanolamine. II. Requirment for a Cobamide Coenzyme by an Ethanolamine Deaminase. J. Biol. Chem. 1965, 240, 4675−4681.
34. 12 Analogs and Substrates. J. Biol. Chem. 2010, 285, 26484−26493.
35. 12-Dependent Isomerization (Eliminating) Reactions. Chem. Rev. 2003, 103, 2095− 2127.
36. Toraya, T. Cobalamin-Dependent Dehydratases and a Deaminase: Radical Catalysis and Reactivating Chaperones. Arch. Biochem. Biophys. 2014, 544, 40−57.
37. Costilow, R. N.; Laycock, L. Ornithine Cyclase (Deaminating). Purification of a Protein That Converts Ornthine to Proline and Definition of the Optimal Assay Conditions. J. Biol. Chem. 1971, 246, 6655−6660.
38. Muth, W. L.; Costilow, R. N. Ornithine Cyclase (Deaminating). III. Mechanism of the Conversion of Ornithine to Proline. J. Biol. Chem. 1974, 249, 7463−7467.
39. Goodman, J. L.; Wang, S.; Alam, S.; Ruzicka, F. J.; Frey, P. A.; Wedekind, J. E. Ornithine Cyclodeaminase: Structure, Mechanism of Action, and Implications for the μ-Crystallin Family. Biochemistry 2004, 43, 13883−13891.
40. Khaw, L. E.; Böhm, G. A.; Metcalfe, S.; Staunton, J.; Leadlay, P. F. Mutational Biosynthesis of Novel Rapamycins by a Strain of Streptomyces hygroscopicus NRRL 5491 Disrupted in rapL, Encoding a Putative Lysine Cyclodeaminase. J. Bacteriol. 1998, 180, 809−814.
41. Gatto, G. J.; Boyne, M. T.; Kelleher, N. L.; Walsh, C. T. Biosynthesis of Pipecolic Acid by RapL, a Lysine Cyclodeaminase Encoded in the Rapamycin Gene Cluster. J. Am. Chem. Soc. 2006, 128, 3838−3847.
42. Tsotsou, G. E.; Barbirato, F. Biochemical Characterisation of Recombinant Streptomyces pristinaespiralis L-Lysine Cyclodeaminase. Biochimie 2007, 89, 591−604.
43. Ying, H.; Wang, J.; Wang, Z.; Feng, J.; Chen, K.; Li, Y.; Ouyang, P. Enhanced Conversion of L-Lysine to L-Pipecolic Acid Using a Recombinant Escherichia coli Containing Lysine Cyclodeaminase as Whole-Cell Biocatalyst. J. Mol. Catal. B: Enzym. 2015, 117, 75−80.
44. Jensen, J. V. K.; Wendisch, V. F. Ornithine Cyclodeaminase-Based Proline Production by Corynebacterium glutamicum. Microb. Cell Fact. 2013, 12 (1), 63.
45. Wu, B.; Szymanski, W.; Heberling, M. M.; Feringa, B. L.; Janssen, D. B. Aminomutases: Mechanistic Diversity, Biotechnological Applications and Future Perspectives. Trends Biotechnol. 2011, 29, 352−362.
46. Frey, P. A.; Reed, G. H. Pyridoxal-5′-phosphate as the Catalyst for Radical Isomerization in Reactions of PLP-Dependent Aminomutases. Biochim. Biophys. Acta, Proteins Proteomics 2011, 1814, 1548− 1557.
47. Berkovitch, F.; Behshad, E.; Tang, K.; Enns, E. A.; Frey, P. A.; Drennan, C. L. A Locking Mechanism Preventing Radical Damage in the Absence of Substrate, as Revealed by the X-Ray Structure of Lysine 5,6-Aminomutase. Proc. Natl. Acad. Sci. U. S. A. 2004, 101, 15870− 15875.
48. Chen, Y.; Maity, A. N.; Frey, P. A.; Ke, S. Mechanism-Based Inhibition Reveals Transitions Between Two Conformational States in the Action of Lysine 5,6-Aminomutase: A Combination of Electron Paramagnetic Resonance Spectroscopy, Electron Nuclear Double Resonance Spectroscopy, and Density Functional Theory Study. J. Am. Chem. Soc. 2013, 135, 788−794.
49. Lo, H.; Lin, H.; Maity, A. N.; Ke, S. The Molecular Mechanism of the Open-Closed Protein Conformational Cycle Transitions and Coupled Substrate Binding, Activation and Product Release Events in Lysine 5,6-Aminomutase. Chem. Commun. 2016, 52, 6399−6402.
50. 12-Coenzyme-Dependent D-α-Lysine Mutase Complex from Clostridium sticklandii. Biochemistry 1970, 9, 4890− 4900.
51. 12 Dependent D-α-Ornithine 5,4-Aminomutase. Biochemistry 1973, 12, 2597−2604.
52. Chen, H.-P.; Wu, S.-H.; Lin, Y.-L.; Chen, C.-M.; Tsay, S.-S. Cloning, Sequencing, Heterologous Expression, Purification, and Characterization of Adenosylcobalamin-Dependent D-Ornithine Aminomutase from Clostridium sticklandii. J. Biol. Chem. 2001, 276, 44744−44750.
53. Chirpich, T. P.; Zappia, V.; Costilow, R. N.; Barker, H. A. Lysine 2,3-Aminomutase: Purification and Properties of a Pyridoxal Phosphate and S-Adenosylmethionine-Activated Enzyme. J. Biol. Chem. 1970, 245, 1778−1789.
54. Song, K. B.; Frey, P. A. Molecular Properties of Lysine-2,3Aminomutase. J. Biol. Chem. 1991, 266, 7651−7655.
55. Frey, P. A. Lysine 2,3-Aminomutase: Is Adenosylmethionine a Poor Man’s Adenosylcobalamin? FASEB J. 1993, 7, 662−670.
56. Lepore, B. W.; Ruzicka, F. J.; Frey, P. A.; Ringe, D. The X-Ray Crystal Structure of Lysine-2,3-Aminomutase from Clostridium subterminale. Proc. Natl. Acad. Sci. U. S. A. 2005, 102, 13819−13824.
57. Broderick, J. B.; Duffus, B. R.; Duschene, K. S.; Shepard, E. M. Radical S-Adenosylmethionine Enzymes. Chem. Rev. 2014, 114, 4229− 4317.
58. Moss, M.; Frey, P. A. The Role of S-Adenosylmethionine in the Lysine 2,3-Aminomutase Reaction. J. Biol. Chem. 1987, 262, 14859− 14862.
59. Behshad, E.; Ruzicka, F. J.; Mansoorabadi, S. O.; Chen, D.; Reed, G. H.; Frey, P. A. Enantiomeric Free Radicals and Enzymatic Control of Stereochemistry in a Radical Mechanism: The Case of Lysine 2,3-Aminomutases. Biochemistry 2006, 45, 12639−12646.
60. Ruzicka, F. J.; Frey, P. A. Glutamate 2,3-Aminomutase: A New Member of the Radical SAM Superfamily of Enzymes. Biochim. Biophys. Acta, Proteins Proteomics 2007, 1774, 286−296.
61. Frey, P. A.; Ruzicka, F. J. Glutamate 2,3-Aminomutase and Methods of Use Thereof. U.S. Patent US 7456271 B2, 2008.
62. Liao, H. H.; Gokarn, R. R.; Gort, S. J.; Jessen, H. J.; Selifonova, O. Alanine 2,3-Aminomutase. U.S. Patent US 7655451 B2, 2010.
63. Frey, P. A.; Ruzicka, F. J. Methods for the Preparation of β-Amino Acids. U.S. Patent US 7452701 B2, 2008.
64. Gamini Kannangara, C.; Gough, S. P. Biosynthesis of Δ-Aminolevulinate in Greening Barley Leaves: Glutamate-1-Semialdehyde Aminotransferase. Carlsberg Res. Commun. 1978, 43, 185− 194.
65. Pugh, C. E.; Harwood, J. L.; John, R. A. Mechanism of Glutamate Semialdehyde Aminotransferase: Roles of Diamino- and Dioxo-Intermediates in the Synthesis of Aminolevulinate. J. Biol. Chem. 1992, 267, 1584−1588.
66. 6-Dependent Enzyme with Asymmetry in Structure and Active Site Reactivity. Proc. Natl. Acad. Sci. U. S. A. 1997, 94, 4866−4871.
67. Contestabile, R.; Jenn, T.; Akhtar, M.; Gani, D.; John, R. A. Reactions of Glutamate 1-Semialdehyde Aminomutase with R- and S-Enantiomers of a Novel, Mechanism-Based Inhibitor, 2,3-Diamino-propyl Sulfate. Biochemistry 2000, 39, 3091−3096.
68. Campanini, B.; Bettati, S.; Di Salvo, M. L.; Mozzarelli, A.; Contestabile, R. Asymmetry of the Active Site Loop Conformation between Subunits of Glutamate-1-Semialdehyde Aminomutase in Solution. BioMed Res. Int. 2013, 2013, 353270.
69. Asano, Y.; Kato, Y.; Levy, C.; Baker, P.; Rice, D. Structure and Function of Amino Acid Ammonia-Lyases. Biocatal. Biotransform. 2004, 22, 133−140.
70. Wu, B.; Szymanski, W.; Crismaru, C. G.; Feringa, B. L.; Janssen, D. B. C-N Lyases Catalyzing Addition of Ammonia, Amines and Amides to CC and CO Bonds. Enzyme Catalysis in Organic Synthesis 2012, 749−778.
71. Poppe, L. Methylidene-Imidazolone: A Novel Electrophile for Substrate Activation. Curr. Opin. Chem. Biol. 2001, 5, 512−524.
72. Frey, P. A.; Hegeman, A. D.; Ruzicka, F. J. The Radical SAM Superfamily. Crit. Rev. Biochem. Mol. Biol. 2008, 43, 63−88.
73. Harden, A. The Chemical Action of Bacillus coli communis and Similar Organisms on Carbohydrates and Allied Compounds. J. Chem. Soc., Trans. 1901, 79, 610−628.
74. Quastel, J. H.; Woolf, B. The Equilibrium Between L-Aspartic Acid, Fumaric Acid and Ammonia in Presence of Resting Bacteria. Biochem. J. 1926, 20, 545−555.
75. Rudolph, F. B.; Fromm, H. J. The Purification and Properties of Aspartase from Escherichia coli. Arch. Biochem. Biophys. 1971, 147, 92−98.
76. Takagi, J. S.; Fukunaga, R.; Tokushige, M.; Katsuki, H. Purification, Crystallization, and Molecular Properties of Aspartase from Pseudomonas fluorescens. J. Biochem. 1984, 96, 545−552.
77. Wilkinson, J. S.; Williams, V. R. Partial Purification of Bacterial Aspartase by Starch Electrophoresis. Arch. Biochem. Biophys. 1961, 93, 80−84.
78. Singh, R. S.; Yadav, M. Single-Step Purification and Characterization of Recombinant Aspartase of Aeromonas media NFB-5. Appl. Biochem. Biotechnol. 2012, 167, 991−1001.
79. Sun, D.; Setlow, P. Cloning, Nucleotide Sequence, and Expression of the Bacillus subtilis ans Operon, Which Codes for L-Asparaginase and L-Aspartase. J. Bacteriol. 1991, 173, 3831−3845.
80. Kawata, Y.; Tamura, K.; Yano, S.; Mizobata, T.; Nagai, J.; Esaki, N.; Soda, K.; Tokushige, M.; Yumoto, N. Purification and Characterization of Thermostable Aspartase from Bacillus sp. YM55−1. Arch. Biochem. Biophys. 1999, 366, 40−46.
81. Shi, W.; Dunbar, J.; Jayasekera, M. M. K.; Viola, R. E.; Farber, G. K. The Structure of L -Aspartate Ammonia-Lyase from Escherichia coli. Biochemistry 1997, 36, 9136−9144.
82. Piatigorsky, J.; O’Brien, W. E.; Norman, B. L.; Kalumuck, K.; Wistow, G. J.; Borras, T.; Nickerson, J. M.; Wawrousek, E. F. Gene Sharing by δ-Crystallin and Argininosuccinate Lyase. Proc. Natl. Acad. Sci. U. S. A. 1988, 85, 3479−3483.
83. Simpson, A.; Bateman, O.; Driessen, H.; Lindley, P.; Moss, D.; Mylvaganam, S.; Narebor, E.; Slingsby, C. The Structure of Avian Eye Lens δ-Crystallin Reveals a New Fold for a Superfamily of Oligomeric Enzymes. Nat. Struct. Biol. 1994, 1, 724−734.
84. Fibriansah, G.; Veetil, V. P.; Poelarends, G. J.; Thunnissen, A. W. H. Structural Basis for the Catalytic Mechanism of Aspartate Ammonia Lyase. Biochemistry 2011, 50, 6053−6062.
85. Falzone, C. J.; Karsten, W. E.; Conley, J. D.; Viola, R. E. L-Aspartase from Escherichia coli: Substrate Specificity and Role of Divalent Metal Ions. Biochemistry 1988, 27, 9089−9093.
86. Yoon, M.-Y.; Thayer-Cook, K. A.; Berdis, A. J.; Karsten, W. E.; Schnackerz, K. D.; Cook, P. F. Acid-Base Chemical Mechanism of Aspartase from Hafnia alvei. Arch. Biochem. Biophys. 1995, 320, 115− 122.
87. Porter, D. J. T.; Bright, H. J. 3-Carbanionic Substrate Analogues Bind Very Tightly to Fumarase and Aspartase. J. Biol. Chem. 1980, 255, 4772−4780.
88. Ellfolk, N. Studies of Aspartase III. On the Specificity of Aspartase. Acta Chem. Scand. 1954, 8, 151−156.
89. Virtanen, A. I.; Ellfolk, N. Aspartase. Methods Enzymol. 1955, 2, 386−390.
90. Ma, L.; Yan, B.-X.; Zhao, H.-L.; Liu, W.-H.; You, D.-L.; Cheng, Y.-H. Alteration of Specificity in L-Aspartase in the Presence of Alcohol. Ann. N. Y. Acad. Sci. 1995, 750, 134−137.
91. Yumoto, N.; Okada, M.; Tokushige, M. Biospecific Inactivation of Aspartase by L-Aspartic-β-Semialdehyde. Biochem. Biophys. Res. Commun. 1982, 104, 859−866.
92. Barker, H. A.; Smyth, R. D.; Wawszkiewicz, E. J.; Lee, M. N.; Wilson, R. M. Enzymic Preparation and Characterization of an α-L-β-Methylaspartic Acid. Arch. Biochem. Biophys. 1958, 78, 468−476.
93. Barker, H. A.; Smyth, R. D.; Wilson, R. M.; Weissbach, H. The Purification and Properties of β-Methylaspartase. J. Biol. Chem. 1958, 234, 320−328.
94. Asano, Y.; Kato, Y. Occurrence of 3-Methylaspartate Ammonia-Lyase in Facultative Anaerobes and Their Application to Synthesis of 3-Substituted (S)-Aspartic Acids. Biosci., Biotechnol., Biochem. 1994, 58, 223−224.
95. Kato, Y.; Asano, Y. Purification and Properties of Crystalline 3-Methylaspartase from Two Facultative Anaerobes, Citrobacter sp. Strain YG-0504 and Morganella morganii strain YG-0601. Biosci., Biotechnol., Biochem. 1995, 59, 93−99.
96. 2H]-3-Methylaspartic Acid: Slow Substrates for a syn-Elimination Reaction Catalysed by Methylaspartase. Tetrahedron: Asymmetry 1993, 4 (6), 1141−1152.
97. Goda, S. K.; Minton, N. P.; Botting, N. P.; Gani, D. Cloning, Sequencing, and Expression in Escherichia coli of the Clostridium tetanomorphum Gene Encoding β-Methylaspartase and Characterization of the Recombinant Protein. Biochemistry 1992, 31, 10747− 10756.
98. Kato, Y.; Asano, Y. Cloning, Nucleotide Sequencing, and Expression of the 3-Methylaspartate Ammonia-Lyase Gene from Citrobacter amalonaticus Strain YG-1002. Appl. Microbiol. Biotechnol. 1998, 50, 468−474.
99. Bearne, S. L.; White, R. L.; McDonnell, J. E.; Bahrami, S.; Grønlund, J. Purification and Characterization of β-Methylaspartase from Fusobacterium varium. Mol. Cell. Biochem. 2001, 221, 117−126.
100. Raj, H.; Puthan Veetil, V.; Szymanski, W.; Dekker, F. J.; Quax, W. J.; Feringa, B. L.; Janssen, D. B.; Poelarends, G. J. Characterization of a Thermostable Methylaspartate Ammonia Lyase from Carboxydothermus hydrogenoformans. Appl. Microbiol. Biotechnol. 2012, 94, 385−397.
101. Gerlt, J. A.; Babbitt, P. C. The Enolase Superfamily: Different Reactions Catalyzed by Similar Active Sites. FASEB J. 1997, 11, A1006.
102. Bright, H. J.; Ingraham, L. L.; Lundin, R. E. The Mechanism of the Methylaspartate Ammonia-Lyase Reaction: Deuterium Exchange. Biochim. Biophys. Acta, Spec. Sect. Enzymol. Subj. 1964, 81, 576−584.
103. Raj, H.; Weiner, B.; Puthan Veetil, V.; Reis, C. R.; Quax, W. J.; Janssen, D. B.; Feringa, B. L.; Poelarends, G. J. Alteration of the Diastereoselectivity of 3-Methylaspartate Ammonia Lyase by Using Structure-Based Mutagenesis. ChemBioChem 2009, 10, 2236−2245.
104. Raj, H.; Poelarends, G. J. The Roles of Active Site Residues in the Catalytic Mechanism of Methylaspartate Ammonia-Lyase. FEBS Open Bio 2013, 3, 285−290.
105. Emiliani, G.; Fondi, M.; Fani, R.; Gribaldo, S. A Horizontal Gene Transfer at the Origin of Phenylpropanoid Metabolism: A Key Adaptation of Plants to Land. Biol. Direct 2009, 4, 7.
106. Zhang, X.; Liu, C.-J. Multifaceted Regulations of Gateway Enzyme Phenylalanine Ammonia-Lyase in the Biosynthesis of Phenylpropanoids. Mol. Plant 2015, 8, 17−27.
107. Watts, K. T.; Mijts, B. N.; Lee, P. C.; Manning, A. J.; Schmidt-Dannert, C. Discovery of a Substrate Selectivity Switch in Tyrosine Ammonia-Lyase, a Member of the Aromatic Amino Acid Lyase Family. Chem. Biol. 2006, 13, 1317−1326.
108. Hodgins, D. S. Yeast Phenylalanine Ammonia-Lyase: Purification, Properties, and the Identification of Catalytically Essential Dehydroalanine. J. Biol. Chem. 1971, 246, 2977−2985.
109. Calabrese, J. C.; Jordan, D. B.; Boodhoo, A.; Sariaslani, S.; Vannelli, T. Crystal Structure of Phenylalanine Ammonia Lyase: Multiple Helix Dipoles Implicated in Catalysis. Biochemistry 2004, 43, 11403−11416.
110. Ritter, H.; Schulz, G. E. Structural Basis for the Entrance into the Phenylpropanoid Metabolism Catalyzed by Phenylalanine Ammonia-Lyase. Plant Cell 2004, 16, 3426−3436.
111. Baedeker, M.; Schulz, G. E. Overexpression of a Designed 2.2 Kb Gene of Eukaryotic Phenylalanine Ammonia-Lyase in Escherichia Coli. FEBS Lett. 1999, 457, 57−60.
112. Moffitt, M. C.; Louie, G. V.; Bowman, M. E.; Pence, J.; Noel, J. P.; Moore, B. S. Discovery of Two Cyanobacterial Phenylalanine Ammonia Lyases: Kinetic and Structural Characterization. Biochemistry 2007, 46, 1004−1012.
113. Zhu, Y.; Liao, S.; Ye, J.; Zhang, H. Cloning and Characterization of a Novel Tyrosine Ammonia Lyase-Encoding Gene Involved in Bagremycins Biosynthesis in Streptomyces sp. Biotechnol. Lett. 2012, 34, 269−274.
114. Peterkofsky, A. The Mechanism of Action of Histidase: Amino-Enzyme Formation and Partial Reactions. J. Biol. Chem. 1962, 237, 787−795.
115. Consevage, M. W.; Phillips, A. T. Presence and Quantity of Dehydroalanine in Histidine Ammonia-Lyase from Pseudomonas putida. Biochemistry 1985, 24, 301−308.
116. Smith, T. A.; Cordelle, F. H.; Abeles, R. H. Inactivation of Histidine Deaminase by Carbonyl Reagents. Arch. Biochem. Biophys. 1967, 120, 724−725.
117. Givot, I. L.; Smith, T. A.; Abeles, R. H. Studies on the Mechanism and the Structure of the Electrophilic Center of Histidine Ammonia Lyase. J. Biol. Chem. 1969, 244, 6341−6353.
118. Hanson, K. R.; Havir, E. A. 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.
119. Langer, M.; Reck, G.; Reed, J.; Retey, J. Identification of Serine-143 as the Most Likely Precursor of Dehydroalanine in the Active Site of Histidine Ammonia-Lyase. A Study of the Overexpressed Enzyme by Site-Directed Mutagenesis. Biochemistry 1994, 33, 6462− 6467.
120. Schuster, B.; Retey, J. Serine-202 Is the Putative Precursor of the Active Site Dehydroalanine of Phenylalanine Ammonia Lyase. Site-Directed Mutagenesis Studies on the Enzyme from Parsley (Petroselinum crispum L.). FEBS Lett. 1994, 349, 252−254.
121. Schroeder, A. C.; Kumaran, S.; Hicks, L. M.; Cahoon, R. E.; Halls, C.; Yu, O.; Jez, J. M. Contributions of Conserved Serine and Tyrosine Residues to Catalysis, Ligand Binding, and Cofactor Processing in the Active Site of Tyrosine Ammonia Lyase. Phytochemistry 2008, 69, 1496−1506.
122. Langer, B.; Röther, D.; Retey, J. Identification of Essential Amino Acids in Phenylalanine Ammonia-Lyase by Site-Directed Mutagenesis. Biochemistry 1997, 36, 10867−10871.
123. Langer, M.; Lieber, A.; Retey, J. Histidine Ammonia-Lyase Mutant S143C Is Posttranslationally Converted into Fully Active
124. Wild-Type Enzyme. Evidence for Serine 143 to Be the Precursor of Active Site Dehydroalanine. Biochemistry 1994, 33, 14034−14038.
125. Schwede, T. F.; Retey, J.; Schulz, G. E. Crystal Structure of Histidine Ammonia-Lyase Revealing a Novel Polypeptide Modification as the Catalytic Electrophile. Biochemistry 1999, 38, 5355−5361.
126. Ormö, M.; Cubitt, A. B.; Kallio, K.; Gross, L. A.; Tsien, R. Y.; Remington, S. J. Crystal Structure of the Aequorea victoria Green Fluorescent Protein. Science 1996, 273, 1392−1395.
127. Reid, B. G.; Flynn, G. C. Chromophore Formation in Green Fluorescent Protein. Biochemistry 1997, 36, 6786−6791.
128. Sanchez-Murcia, P. A.; Bueren-Calabuig, J. A.; Camacho-Artacho, M.; Cortes-Cabrera, Á.; Gago, F. Stepwise Simulation of 3,5-Dihydro-5-Methylidene-4H-Imidazol-4-One (MIO) Biogenesis in Histidine Ammonia-Lyase. Biochemistry 2016, 55, 5854−5864.
129. Havir, E. A.; Hanson, K. R. L-Phenylalanine Ammonia-Lyase (Maize and Potato). Evidence That the Enzyme Is Composed of Four Subunits. Biochemistry 1973, 12, 1583−1591.
130. Pilbak, S.; Tomin, A.; Retey, J.; Poppe, L. The Essential Tyrosine-Containing Loop Conformation and the Role of the C-Terminal Multi-Helix Region in Eukaryotic Phenylalanine Ammonia-Lyases. FEBS J. 2006, 273, 1004−1019.
131. Wang, L.; Gamez, A.; Archer, H.; Abola, E. E.; Sarkissian, C. N.; Fitzpatrick, P.; Wendt, D.; Zhang, Y.; Vellard, M.; Bliesath, J.; Bell, S. M.; Lemontt, J. F.; Scriver, C. R.; Stevens, R. C. Structural and Biochemical Characterization of the Therapeutic Anabaena variabilis Phenylalanine Ammonia Lyase. J. Mol. Biol. 2008, 380, 623−635.
132. Röther, D.; Merkel, D.; Retey, J. Spectroscopic Evidence for a 4-Methylidene Imidazol-5-One in Histidine and Phenylalanine Ammonia-Lyases. Angew. Chem., Int. Ed. 2000, 39, 2462−2464.
133. Louie, G. V.; Bowman, M. E.; Moffitt, M. C.; Baiga, T. J.; Moore, B. S.; Noel, J. P. Structural Determinants and Modulation of Substrate Specificity in Phenylalanine-Tyrosine Ammonia-Lyases. Chem. Biol. 2006, 13, 1327−1338.
134. Röther, D.; Poppe, L.; Morlock, G.; Viergutz, S.; Retey, J. An Active Site Homology Model of Phenylalanine Ammonia-Lyase from Petroselinum crispum. Eur. J. Biochem. 2002, 269, 3065−3075.
135. Krug, D.; Müller, R. Discovery of Additional Members of the Tyrosine Aminomutase Enzyme Family and the Mutational Analysis of CmdF. ChemBioChem 2009, 10, 741−750.
136. Rösler, J.; Krekel, F.; Amrhein, N.; Schmid, J. Maize Phenylalanine Ammonia-Lyase Has Tyrosine Ammonia-Lyase Activity. Plant Physiol. 1997, 113, 175−179.
137. Klee, C. B. Metal Activation of Histidine Ammonia-Lyase. Metal Ion-SulfhydrylGroup Relationship. J. Biol. Chem. 1972, 247, 1398−1406.
138. Seff, A.-L.; Pilbak, S.; Silaghi-Dumitrescu, I.; Poppe, L. Computational Investigation of the Histidine Ammonia-Lyase Reaction: A Modified Loop Conformation and the Role of the Zinc(II) Ion. J. Mol. Model. 2011, 17, 1551−1563.
139. Röther, D.; Poppe, L.; Viergutz, S.; Langer, B.; Retey, J. Characterization of the Active Site of Histidine Ammonia-Lyase from Pseudomonas putida. Eur. J. Biochem. 2001, 268, 6011−6019.
140. Bartsch, S.; Bornscheuer, U. T. Mutational Analysis of Phenylalanine Ammonia Lyase to Improve Reactions Rates for Various Substrates. Protein Eng., Des. Sel. 2010, 23, 929−933.
141. Hermes, J. D.; Weiss, P. M.; Cleland, W. W. Use of Nitrogen-15 and Deuterium Isotope Effects to Determine the Chemical Mechanism of Phenylalanine Ammonia-Lyase. Biochemistry 1985, 24, 2959−2967.
142. Pilbak, S.; Farkas, Ö.; Poppe, L. Mechanism of the Tyrosine Ammonia Lyase Reaction. Tandem Nucleophilic and Electrophilic Enhancement by a Proton Transfer. Chem. - Eur. J. 2012, 18, 7793− 7802.
143. Langer, M.; Pauling, A.; Retey, J. The Role of Dehydroalanine in Catalysis by Histidine Ammonia Lyase. Angew. Chem., Int. Ed. Engl. 1995, 34, 1464−1465.
144. 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, 8433−8437.
145. Poppe, L.; Retey, J. Friedel-Crafts-Type Mechanism for the Enzymatic Elimination of Ammonia from Histidine and Phenylalanine. Angew. Chem., Int. Ed. 2005, 44, 3668−3688.
146. Baedeker, M.; Schulz, G. E. Structures of Two Histidine Ammonia-Lyase Modifications and Implications for the Catalytic Mechanism. Eur. J. Biochem. 2002, 269, 1790−1797.
147. Rettig, M.; Sigrist, A.; Retey, J. Mimicking the Reaction of Phenylalanine Ammonia Lyase by a Synthetic Model. Helv. Chim. Acta 2000, 83, 2246−2265.
148. Pinto, G. P.; Ribeiro, A. J. M.; Ramos, M. J.; Fernandes, P. A.; Toscano, M.; Russo, N. New Insights in the Catalytic Mechanism of Tyrosine Ammonia-Lyase given by QM/MM and QM Cluster Models. Arch. Biochem. Biophys. 2015, 582, 107−115.
149. Strange, P. G.; Staunton, J.; Wiltshire, H. R.; Battersby, A. R.; Hanson, K. R.; Havir, E. A. Studies of Enzyme-Mediated Reactions. Part II. Stereochemistry of the Elimination of Ammonia from L-Tyrosine Catalysed by the Enzyme Form Maize. J. Chem. Soc., Perkin Trans. 1 1972, 2364−2372.
150. Weiser, D.; Bencze, L. C.; Banoćzi, G.; Ender, F.; Kiss, R.; Kokai, E.; Szilagyi, A.; Vertessy, B. G.; Farkas, Ö.; Paizs, C.; Poppe, L. Phenylalanine Ammonia-Lyase-Catalyzed Deamination of an Acyclic Amino Acid: Enzyme Mechanistic Studies Aided by a Novel Microreactor Filled with Magnetic Nanoparticles. ChemBioChem 2015, 16, 2283−2288.
151. Zon, J.; Amrhein, N. Inhibitors of Phenylalanine Ammonia-Lyase: 2-Aminoindan-2-Phosphonic Acid and Related Compounds. Liebigs Ann. Chem. 1992, 1992, 625−628.
152. Gloge, A.; Zon, J.; Kövari, Á.; Poppe, L.; Retey, J. Phenylalanine Ammonia-Lyase: The Use of Its Broad Substrate Specificity for Mechanistic Investigations and Biocatalysis. Synthesis of L-Arylalanines. Chem. - Eur. J. 2000, 6, 3386−3390.
153. Klee, C. B.; Kirk, K. L.; Cohen, L. A. 4-Nitro-L-Histidine as a Substrate for Histidine Ammonia-Lyase: The Role of β-Hydrogen Acidity in the Rate-Limiting Step. Biochem. Biophys. Res. Commun. 1979, 87, 343−348.
154. Tosa, M. I.; Brem, J.; Mantu, A.; Irimie, F. D.; Paizs, C.; Retey, J. The Interaction of Nitrophenylalanines with Wild Type and Mutant 4-Methylideneimidazole-5-One-Less Phenylalanine Ammonia Lyase. ChemCatChem 2013, 5, 779−783.
155. Lovelock, S. L.; Lloyd, R. C.; Turner, N. J. Phenylalanine Ammonia Lyase Catalyzed Synthesis of Amino Acids by an MIO-Cofactor Independent Pathway. Angew. Chem., Int. Ed. 2014, 53, 4652−4656.
156. Parmeggiani, F.; Lovelock, S. L.; Weise, N. J.; Ahmed, S. T.; Turner, N. J. Synthesis of D- and L-Phenylalanine Derivatives by Phenylalanine Ammonia Lyases: A Multienzymatic Cascade Process. Angew. Chem., Int. Ed. 2015, 54, 4608−4611.
157. Christenson, S. D.; Liu, W.; Toney, M. D.; Shen, B. A Novel 4-Methylideneimidazole-5-One-Containing Tyrosine Aminomutase in Enediyne Antitumor Antibiotic C-1027 Biosynthesis. J. Am. Chem. Soc. 2003, 125, 6062−6063.
158. Christenson, S. D.; Wu, W.; Spies, M. A.; Shen, B.; Toney, M. D. Kinetic Analysis of the 4-Methylideneimidazole-5-One-Containing Tyrosine Aminomutase in Enediyne Antitumor Antibiotic C-1027 Biosynthesis. Biochemistry 2003, 42, 12708−12718.
159. Christianson, C. V.; Montavon, T. J.; Van Lanen, S. G.; Shen, B.; Bruner, S. D. The Structure of L-Tyrosine 2,3-Aminomutase from the C-1027 Enediyne Antitumor Antibiotic Biosynthetic Pathway. Biochemistry 2007, 46, 7205−7214.
160. Van Lanen, S. G.; Oh, T.; Liu, W.; Wendt-Pienkowski, E.; Shen, B. Characterization of the Maduropeptin Biosynthetic Gene Cluster from Actinomadura madurae ATCC 39144 Supporting a Unifying Paradigm for Enediyne Biosynthesis. J. Am. Chem. Soc. 2007, 129, 13082−13094.
161. Huang, S.-X.; Lohman, J. R.; Huang, T.; Shen, B. A New Member of the 4-Methylideneimidazole-5-One-Containing Aminomutase Family from the Enediyne Kedarcidin Biosynthetic Pathway. Proc. Natl. Acad. Sci. U. S. A. 2013, 110, 8069−8074.
162. Rachid, S.; Krug, D.; Kunze, B.; Kochems, I.; Scharfe, M.; Zabriskie, T. M.; Blöcker, H.; Müller, R. Molecular and Biochemical Studies of Chondramide Formation. Highly Cytotoxic Natural Products from Chondromyces crocatus Cm c5. Chem. Biol. 2006, 13, 667−681.
163. Rachid, S.; Krug, D.; Weissman, K. J.; Müller, R. Biosynthesis of (R)-β-Tyrosine and Its Incorporation into the Highly Cytotoxic Chondramides Produced by Chondromyces crocatus. J. Biol. Chem. 2007, 282, 21810−21817.
164. Wanninayake, U.; Walker, K. D. A Bacterial Tyrosine Aminomutase Proceeds through Retention or Inversion of Stereochemistry to Catalyze Its Isomerization Reaction. J. Am. Chem. Soc. 2013, 135, 11193−11204.
165. Spiteller, P.; Rüth, M.; Von Nussbaum, F.; Steglich, W. Detection of a 2,3-Aminomutase in the Mushroom Cortinarius violaceus. Angew. Chem., Int. Ed. 2000, 39, 2754−2756.
166. Yan, J.; Aboshi, T.; Teraishi, M.; Strickler, S. R.; Spindel, J. E.; Tung, C.-W.; Takata, R.; Matsumoto, F.; Maesaka, Y.; McCouch, S. R.; Okumoto, Y.; Mori, N.; Jander, G. The Tyrosine Aminomutase TAM1 Is Required for β-Tyrosine Biosynthesis in Rice. Plant Cell 2015, 27, 1265−1278.
167. Walter, T.; King, Z.; Walker, K. D. A Tyrosine Aminomutase from Rice (Oryza sativa) Isomerizes (S)-α- to (R)-β-Tyrosine with Unique High Enantioselectivity and Retention of Configuration. Biochemistry 2016, 55, 1−4.
168. Walter, T.; Wijewardena, D.; Walker, K. D. Mutation of Aryl Binding Pocket Residues Results in an Unexpected Activity Switch in an Oryza sativa Tyrosine Aminomutase. Biochemistry 2016, 55, 3497− 3503.
169. Bartsch, S.; Bornscheuer, U. T. A Single Residue Influences the Reaction Mechanism of Ammonia Lyases and Mutases. Angew. Chem., Int. Ed. 2009, 48, 3362−3365.
170. Walker, K. D.; Klettke, K.; Akiyama, T.; Croteau, R. Cloning, Heterologous Expression, and Characterization of a Phenylalanine Aminomutase Involved in Taxol Biosynthesis. J. Biol. Chem. 2004, 279, 53947−53954.
171. Feng, L.; Wanninayake, U.; Strom, S.; Geiger, J.; Walker, K. D. Mechanistic, Mutational, and Structural Evaluation of a Taxus Phenylalanine Aminomutase. Biochemistry 2011, 50, 2919−2930.
172. Steele, C. L.; Chen, Y.; Dougherty, B. A.; Li, W.; Hofstead, S.; Lam, K. S.; Xing, Z.; Chiang, S.-J. Purification, Cloning, and Functional Expression of Phenylalanine Aminomutase: The First Committed Step in Taxol Side-Chain Biosynthesis. Arch. Biochem. Biophys. 2005, 438, 1−10.
173. Amos, L. A.; Löwe, J. How Taxol® Stabilises Microtubule Structure. Chem. Biol. 1999, 6, R65−R69.
174. Roopa, G.; Madhusudhan, M. C.; Sunil, K. C. R.; Lisa, N.; Calvin, R.; Poornima, R.; Zeinab, N.; Kini, K. R.; Prakash, H. S.; Geetha, N. Identification of Taxol-Producing Endophytic Fungi Isolated from Salacia oblonga through Genomic Mining Approach. J. Genet. Eng. Biotechnol. 2015, 13, 119−127.
175. Walker, K. D.; Floss, H. G. Detection of a Phenylalanine Aminomutase in Cell-Free Extracts of Taxus brevifolia and Preliminary Characterization of Its Reaction. J. Am. Chem. Soc. 1998, 120, 5333− 5334.
176. Mutatu, W.; Klettke, K. L.; Foster, C.; Walker, K. D. Unusual Mechanism for an Aminomutase Rearrangement: Retention of Configuration at the Migration Termini. Biochemistry 2007, 46, 9785−9794.
177. Wybenga, G. G.; Szymanski, W.; Wu, B.; Feringa, B. L.; Janssen, D. B.; Dijkstra, B. W. Structural Investigations into the Stereochemistry and Activity of a Phenylalanine-2,3-Aminomutase from Taxus chinensis. Biochemistry 2014, 53, 3187−3198.
178. Ratnayake, N. D.; Wanninayake, U.; Geiger, J. H.; Walker, K. D. Stereochemistry and Mechanism of a Microbial Phenylalanine Aminomutase. J. Am. Chem. Soc. 2011, 133, 8531−8533.
179. Wu, B.; Szymanski, W.; Wybenga, G. G.; Heberling, M. M.; Bartsch, S.; De Wildeman, S.; Poelarends, G. J.; Feringa, B. L.; Dijkstra, B. W.; Janssen, D. B. Mechanism-Inspired Engineering of Phenylalanine Aminomutase for Enhanced β-Regioselective Asymmetric Amination of Cinnamates. Angew. Chem., Int. Ed. 2012, 51, 482−486.
180. Wang, K.; Hou, Q.; Liu, Y. Insight into the Mechanism of Aminomutase Reaction: A Case Study of Phenylalanine Aminomutase by Computational Approach. J. Mol. Graphics Modell. 2013, 46, 65−73.
181. Bartsch, S.; Wybenga, G. G.; Jansen, M.; Heberling, M. M.; Wu, B.; Dijkstra, B. W.; Janssen, D. B. Redesign of a Phenylalanine Aminomutase into a Phenylalanine Ammonia Lyase. ChemCatChem 2013, 5, 1797−1802.
182. Ghosh, A. C.; Manmade, A.; Townsend, J. M.; Bousquet, A.; Howes, J. F.; Demain, A. L. Production of Cyclochlorotine and a New Metabolite, Simatoxin, by Penicillium islandicum Sopp. Appl. Environ. Microbiol. 1978, 35, 1074−1078.
183. Morita, H.; Nagashima, S.; Takeya, K.; Itokawa, H.; Iitaka, Y. Structures and Conformation of Antitumour Cyclic Pentapeptides, Astins A, B and C, from Aster tataricus. Tetrahedron 1995, 51, 1121− 1132.
184. Schafhauser, T.; Wibberg, D.; Rueckert, C.; Winkler, A.; Flor, L.; Van Peé, K.-H.; Fewer, D. P.; Sivonen, K.; Jahn, L.; Ludwig-Müller, J.; Caradec, T.; Jacques, P.; Huijbers, M. M. E.; Van Berkel, W. J. H.; Weber, T.; Wohlleben, W.; Kalinowski, J. Draft Genome Sequence of Talaromyces islandicus (“Penicillium islandicum”) WF-38−12, a Neglected Mold with Significant Biotechnological Potential. J. Biotechnol. 2015, 211, 101−102.
185. Schafhauser, T.; Kirchner, N.; Kulik, A.; Huijbers, M. M. E.; Flor, L.; Caradec, T.; Fewer, D. P.; Gross, H.; Jacques, P.; Jahn, L.; Jokela, J.; Leclere, V.; Ludwig-Muller, J.; Sivonen, K.; Van Berkel, W. J. H.; Weber, T.; Wohlleben, W.; Van Peé, K.-H. The Cyclochlorotine Mycotoxin Is Produced by the Nonribosomal Peptide Synthetase CctN in Talaromyces islandicus (“Penicillium islandicum”). Environ. Microbiol. 2016, 18, 3728−3741.
186. Jahn, L. Characterization of a New Endophytic Astin Producer, Pelliciarosea asterica, from Aster tataricus. Dissertation, TU Dresden, 2015.
187. Jin, M.; Fischbach, M. A.; Clardy, J. A Biosynthetic Gene Cluster for the Acetyl-CoA Carboxylase Inhibitor Andrimid. J. Am. Chem. Soc. 2006, 128, 10660−10661.
188. Magarvey, N. A.; Fortin, P. D.; Thomas, P. M.; Kelleher, N. L.; Walsh, C. T. Gatekeeping versus Promiscuity in the Early Stages of the Andrimid Biosynthetic Assembly Line. ACS Chem. Biol. 2008, 3, 542− 554.
189. Strom, S.; Wanninayake, U.; Ratnayake, N. D.; Walker, K. D.; Geiger, J. H. Insights into the Mechanistic Pathway of the Pantoea agglomerans Phenylalanine Aminomutase. Angew. Chem., Int. Ed. 2012, 51 (12), 2898−2902.
190. Weise, N. J.; Ahmed, S. T.; Parmeggiani, F.; Turner, N. J. Kinetic Resolution of Aromatic β-Amino Acids Using a Combination of Phenylalanine Ammonia Lyase and Aminomutase Biocatalysts. Adv. Synth. Catal. 2017, 359, 1570−1576.
191. Kudo, F.; Kawamura, K.; Uchino, A.; Miyanaga, A.; Numakura, M.; Takayanagi, R.; Eguchi, T. Genome Mining of the Hitachimycin Biosynthetic Gene Cluster: Involvement of a Phenylalanine-2,3Aminomutase in Biosynthesis. ChemBioChem 2015, 16, 909−914.
192. Xiang, L.; Moore, B. S. Inactivation, Complementation, and Heterologous Expression of encP, a Novel Bacterial Phenylalanine Ammonia-Lyase Gene. J. Biol. Chem. 2002, 277, 32505−32509.
193. Xiang, L.; Moore, B. S. Biochemical Characterization of a Prokaryotic Phenylalanine Ammonia Lyase. J. Bacteriol. 2005, 187, 4286−4289.
194. Chesters, C.; Wilding, M.; Goodall, M.; Micklefield, J. Thermal Bifunctionality of Bacterial Phenylalanine Aminomutase and Ammonia Lyase Enzymes. Angew. Chem., Int. Ed. 2012, 51, 4344−4348.
195. Tosa, T.; Sato, T.; Mori, T.; Chibata, I. Basic Studies for Continuous Production of L-Aspartic Acid by Immobilized Escherichia coli Cells. Appl. Microbiol. 1974, 27, 886−889.
196. Fusee, M. C. Industrial Production of L-Aspartic Acid Using Polyurethane-Immobilized Cells Containing Aspartase. Methods Enzymol. 1987, 136, 463−471.
197. Nishida, Y.; Sato, T.; Tosa, T.; Chibata, I. Immobilization of Escherichia coli Cells Having Aspartase Activity with Carrageenan and Locust Bean Gum. Enzyme Microb. Technol. 1979, 1, 95−99.
198. Chibata, I.; Tosa, T.; Sato, T. Continuous Production of L-Aspartic Acid. Improvement of Productivity by Both Development of Immobilization Method and Construction of New Escherichia coli Strain. Appl. Biochem. Biotechnol. 1986, 13, 231−240.
199. Kimura, K.; Takayama, K.; Ado, Y.; Kawamoto, T.; Masunaga, I. Process for Producing Thermophilic Aspartase. U.S. Patent US 4391910, 1983.
200. 13C]Aspartic Acid. J. Labelled Compd. Radiopharm. 1985, 22, 909−915.
201. Tajima, T.; Hamada, M.; Nakashimada, Y.; Kato, J. Efficient Aspartic Acid Production by a Psychrophile-Based Simple Biocatalyst. J. Ind. Microbiol. Biotechnol. 2015, 42, 1319−1324.
202. Sherwin, M. B.; Blouin, J. J. Process for Preparing L-Aspartic Acid. U.S. Patent US 4560653, 1985.
203. Sakano, K.; Hayashi, T.; Mukouyama, M. Process for Production of L-Aspartic Acid. U.S. Patent US 5541090, 1996.
204. Cardenas-Ferna ndez, M.; Khalikova, E.; Korpela, T.; Lopez, C.; Álvaro, G. Co-Immobilised Aspartase and Transaminase for High-Yield Synthesis of L-Phenylalanine. Biochem. Eng. J. 2015, 93, 173− 178.
205. Han, C.; Yao, P.; Yuan, J.; Duan, Y.; Feng, J.; Wang, M.; Wu, Q.; Zhu, D. Nitrilase-Catalyzed Hydrolysis of 3-Aminopropionitrile at High Concentration with a Tandem Reaction Strategy for Shifting the Reaction to β-Alanine Formation. J. Mol. Catal. B: Enzym. 2015, 115, 113−118.
206. Tessaro, D.; Pollegioni, L.; Piubelli, L.; D’Arrigo, P.; Servi, S. Systems Biocatalysis: An Artificial Metabolism for Interconversion of Functional Groups. ACS Catal. 2015, 5, 1604−1608.
207. Emery, T. F. Aspartase-Catalyzed Synthesis of N-Hydrox-yaspartic Acid. Biochemistry 1963, 2, 1041−1045.
208. Weiner, B.; Poelarends, G. J.; Janssen, D. B.; Feringa, B. L. Biocatalytic Enantioselective Synthesis of N-Substituted Aspartic Acids by Aspartate Ammonia Lyase. Chem. - Eur. J. 2008, 14, 10094−10100.
209. Vogel, A.; Schmiedel, R.; Hofmann, U.; Gruber, K.; Zangger, K. Converting Aspartase into a β-Amino Acid Lyase by Cluster Screening. ChemCatChem 2014, 6, 965−968.
210. Winkler, M. F.; Williams, V. R. New Substrates for β-Methylaspartase. Biochim. Biophys. Acta 1967, 146, 287−289.
211. Akhtar, M.; Cohen, M. A.; Gani, D. Enzymic Synthesis of 3-Halogenoaspartic Acids Using β-Methylaspartase: Inhibition by 3-Bromoaspartic Acid. J. Chem. Soc., Chem. Commun. 1986, 1290−1291.
212. Akhtar, M.; Cohen, M. A.; Gani, D. Stereochemical Course of the Enzymic Amination of Chloro- and Bromo- Fumaric Acid by 3-Methylaspartate Ammonia-Lyase. Tetrahedron Lett. 1987, 28 (21), 2413−2416.
213. Akhtar, M.; Botting, N. P.; Cohen, M. A.; Gani, D. Enantiospecific Synthesis of 3-Substituted Aspartic Acids via Enzymic Amination of Substituted Fumaric Acids. Tetrahedron 1987, 43, 5899− 5908.
214. Gulzar, M. S.; Akhtar, M.; Gani, D. Preparation of N-Substituted Aspartic Acids via Enantiospecific Conjugate Addition of N-Nucleophiles to Fumaric Acids Using Methylaspartase: Synthetic Utility and Mechanistic Implications. J. Chem. Soc., Perkin Trans. 1 1997, 649−655.
215. Raj, H.; Szymanski, W.; De Villiers, J.; Rozeboom, H. J.; Veetil, V. P.; Reis, C. R.; De Villiers, M.; Dekker, F. J.; De Wildeman, S.; Quax, W. J.; Thunnissen, A. W. H.; Feringa, B. L.; Janssen, D. B.; Poelarends, G. J. Engineering Methylaspartate Ammonia Lyase for the Asymmetric Synthesis of Unnatural Amino Acids. Nat. Chem. 2012, 4, 478−484.
216. Song, C. W.; Lee, J.; Ko, Y.-S.; Lee, S. Y. Metabolic Engineering of Escherichia coli for the Production of 3-Aminopropionic Acid. Metab. Eng. 2015, 30, 121−129.
217. Wang, J.; Zhang, K. Production of Mesaconate in Escherichia coli by Engineered Glutamate Mutase Pathway. Metab. Eng. 2015, 30, 190−196.
218. Williams, V. R.; Hiroms, J. M. Reversibility of the “Irreversible” Histidine Ammonia-Lyase Reaction. Biochim. Biophys. Acta 1967, 139, 214−216.
219. Havir, E. A.; Hanson, K. R. L-Phenylalanine Ammonia-Lyase. II. Mechanism and Kinetic Properties of the Enzyme from Potato Tubers. Biochemistry 1968, 7, 1904−1914.
220. Knowles, W. S. Asymmetric Hydrogenation. Acc. Chem. Res. 1983, 16, 106−112.
221. Strecker, A. Ueber Die Künstliche Bildung Der Milchsaëure Und Einen Neuen Dem Glycocoll Homologen Köerper. Justus Liebigs Ann. Chem. 1850, 75, 27−45.
222. Wang, J.; Liu, X.; Feng, X. Asymmetric Strecker Reactions. Chem. Rev. 2011, 111, 6947−6983.
223. Nelson, R. P. Immobilized Microbial Cells. U.S. Patent US 3957580, 1976.
224. Yamada, S.; Nabe, K.; Izuo, N.; Nakamichi, K.; Chibata, I. Production of L-Phenylalanine from trans-Cinnamic Acid with Rhodotorula glutinis Containing L-Phenylalanine Ammonia-Lyase Activity. Appl. Environ. Microbiol. 1981, 42, 773−778.
225. Renard, G.; Guilleux, J.-C.; Bore, C.; Malta-Valette, V.; Lerner, D. A. Synthesis of L-Phenylalanine Analogs by Rhodotorula glutinis. Bioconversion of Cinnamic Acid Derivatives. Biotechnol. Lett. 1992, 14, 673−678.
226. 1]Phenylalanine and Evaluation of the Stereochemical Course of the Reaction of (R)-Phenylalanine with (S)-Phenylalanine Ammonia-Lyase. J. Chem. Soc., Perkin Trans. 1 1994, 3545−3548.
227. Viergutz, S.; Poppe, L.; Tomin, A.; Retey, J. Mechanistic Investigation of Phenylalanine Ammonia Lyase by Using N-Methylated Phenylalanines. Helv. Chim. Acta 2003, 86, 3601−3612.
228. Rowles, I.; Groenendaal, B.; Binay, B.; Malone, K. J.; Willies, S. C.; Turner, N. J. Engineering of Phenylalanine Ammonia Lyase from Rhodotorula graminis for the Enhanced Synthesis of Unnatural L-Amino Acids. Tetrahedron 2016, 72, 7343−7347.
229. Ahmed, S. T.; Parmeggiani, F.; Weise, N. J.; Flitsch, S. L.; Turner, N. J. Chemoenzymatic Synthesis of Optically Pure L- and D-Biarylalanines through Biocatalytic Asymmetric Amination and Palladium-Catalyzed Arylation. ACS Catal. 2015, 5, 5410−5413.
230. Van Assema, F. B. J.; Sereinig, N. Method for Producing Optically Active Phenylalanine compounds from Cinnamic Acid Derivatives Employing Phenylalanine Ammonia Lyase Derived from Idiomarina loihiensis. World Patent WO 2008031578 A1, 2008.
231. Weise, N. J.; Ahmed, S. T.; Parmeggiani, F.; Siirola, E.; Pushpanath, A.; Schell, U.; Turner, N. J. Intensified Biocatalytic Production of Enantiomerically Pure Halophenylalanines from Acrylic Acids Using Ammonium Carbamate as the Ammonia Source. Catal. Sci. Technol. 2016, 6, 4086−4089.
232. Parmeggiani, F.; Ahmed, S. T.; Weise, N. J.; Turner, N. J. Telescopic One-Pot Condensation-Hydroamination Strategy for the Synthesis of Optically Pure L-Phenylalanines from Benzaldehydes. Tetrahedron 2016, 72, 7256−7262.
233. D’Cunha, G. B.; Satyanarayan, V.; Nair, P. M. Novel Direct Synthesis of L-Phenylalanine Methyl Ester by Using Rhodotorula glutinis Phenylalanine Ammonia Lyase in an Organic-Aqueous Biphasic System. Enzyme Microb. Technol. 1994, 16, 318−322.
234. Hanson, K. R.; Havir, E. A.; Ressler, C. Phenylalanine Ammonia-Lyase: Enzymatic Conversion of 3-(1,4-Cyclohexadienyl)-L-Alanine to trans-3-(1,4-Cyclohexadienyl)acrylic Acid. Biochemistry 1979, 18, 1431−1438.
235. Skolaut, A.; Retey, J. 1,4-Dihydro-L-Phenylalanine. Its Synthesis and Behavior in the Phenylalanine Ammonia-Lyase Reaction. Arch. Biochem. Biophys. 2001, 393, 187−191.
236. Gloge, A.; Langer, B.; Poppe, L.; Retey, J. The Behavior of Substrate Analogues and Secondary Deuterium Isotope Effects in the Phenylalanine Ammonia-Lyase Reaction. Arch. Biochem. Biophys. 1998, 359, 1−7.
237. Paizs, C.; Katona, A.; Retey, J. The Interaction of Heteroaryl-Acrylates and Alanines with Phenylalanine Ammonia-Lyase from Parsley. Chem. - Eur. J. 2006, 12, 2739−2744.
238. Paizs, C.; Tosa, M. I.; Bencze, L. C.; Brem, J.; Irimie, F. D.; Retey, J. 2-Amino-3-(5-Phenylfuran-2-yl)propionic Acids And 5-Phenylfuran-2-ylacrylic Acids Are Novel Substrates of Phenylalanine Ammonia-Lyase. Heterocycles 2010, 82, 1217−1228.
239. Hashimoto, M.; Hatanaka, Y.; Nabeta, K. Novel Photoreactive Cinnamic Acid Analogues to Elucidate Phenylalanine Ammonia-Lyase. Bioorg. Med. Chem. Lett. 2000, 10, 2481−2483.
240. Tian, Z.; Zhu, W.; Xu, Y.; Qian, X. An Unnatural Amino Acid Based Fluorescent Probe for Phenylalanine Ammonia Lyase. Org. Biomol. Chem. 2014, 12, 5818−5821.
241. Lovelock, S. L.; Turner, N. J. Bacterial Anabaena variabilis Phenylalanine Ammonia Lyase: A Biocatalyst with Broad Substrate Specificity. Bioorg. Med. Chem. 2014, 22, 5555−5557.
242. Barron, C. C.; Sponagle, B. J. D.; Arivalagan, P.; D’Cunha, G. B. Optimization of Oligomeric Enzyme Activity in Ionic Liquids Using Rhodotorula glutinis Yeast Phenylalanine Ammonia Lyase. Enzyme Microb. Technol. 2017, 96, 151−156.
243. Bartha-Vari, J. H.; Tosa, M. I.; Irimie, F. D.; Weiser, D.; Boros, Z.; Vertessy, B. G.; Paizs, C.; Poppe, L. Immobilization of Phenylalanine Ammonia-Lyase on Single-Walled Carbon Nanotubes for Stereoselective Biotransformations in Batch and Continuous-Flow Modes. ChemCatChem 2015, 7, 1122−1128.
244. Bartha-Vari, J. H.; Bencze, L. C.; Bell, E.; Poppe, L.; Katona, G.; Irimie, F. D.; Paizs, C.; Tosa, M. I. Aminated Single-Walled Carbon Nanotubes as Carrier for Covalent Immobilization of Phenylalanine Ammonia-Lyase. Period. Polytechn. Chem. Eng. 2017, 61, 59−66.
245. Zhang, Z. Enantioselective Scavenging Using Homogenate of Rhodotorula graminis: A Facile Preparation of D-Amino Acid Derivatives in Enantiopure Form. Tetrahedron Lett. 2008, 49, 6468− 6470.
246. Shibatani, T.; Nishimura, N.; Nabe, K.; Kakimoto, T.; Chibata, I. Enzymatic Production of Urocanic Acid by Achromobacter liquidum. Appl. Microbiol. 1974, 27, 688−694.
247. Zhu, L.; Zhou, L.; Huang, N.; Cui, W.; Liu, Z.; Xiao, K.; Zhou, Z. Efficient Preparation of Enantiopure D-Phenylalanine through Asymmetric Resolution Using Immobilized Phenylalanine Ammonia-Lyase from Rhodotorula glutinis JN-1 in a Recirculating Packed-Bed Reactor. PLoS One 2014, 9, e108586.
248. Ahmed, S. T.; Parmeggiani, F.; Weise, N. J.; Flitsch, S. L.; Turner, N. J. Synthesis of Enantiomerically Pure Ring-Substituted L-Pyridylalanines by Biocatalytic Hydroamination. Org. Lett. 2016, 18, 5468−5471.
249. Ratnayake, N. D.; Liu, N.; Kuhn, L. A.; Walker, K. D. Ring-Substituted α-Arylalanines for Probing Substituent Effects on the Isomerization Reaction Catalyzed by an Aminomutase. ACS Catal. 2014, 4, 3077−3090.
250. Ratnayake, N. D.; Theisen, C.; Walter, T.; Walker, K. D. Whole-Cell Biocatalytic Production of Variously Substituted β-Aryl- and β-Heteroaryl-β-Amino Acids. J. Biotechnol. 2016, 217, 12−21.
251. Gademann, K.; Hintermann, T.; Schreiber, J. V. β-Peptides: Twisting and Turning. Curr. Med. Chem. 1999, 6, 905−925.
252. Steer, D. L.; Lew, R. A.; Perlmutter, P.; Smith, A. I.; Aguilar, M.-I. β-Amino Acids: Versatile Peptidomimetics. Curr. Med. Chem. 2002, 9, 811−822.
253. Aguilar, M.-I.; Purcell, A. W.; Devi, R.; Lew, R.; Rossjohn, J.; Smith, A. I.; Perlmutter, P. β-Amino Acid-Containing Hybrid Peptides. New Opportunities in Peptidomimetics. Org. Biomol. Chem. 2007, 5, 2884−2890.
254. Wu, B.; Szymanski, W.; Wijma, H. J.; Crismaru, C. G.; De Wildeman, S.; Poelarends, G. J.; Feringa, B. L.; Janssen, D. B. Engineering of an Enantioselective Tyrosine Aminomutase by Mutation of a Single Active Site Residue in Phenylalanine Aminomutase. Chem. Commun. 2009, 46, 8157−8159.
255. Klettke, K. L.; Sanyal, S.; Mutatu, W.; Walker, K. D. β-Styryl- and β-Aryl-β-Alanine Products of Phenylalanine Aminomutase Catalysis. J. Am. Chem. Soc. 2007, 129, 6988−6989.
256. Cox, B. M.; Bilsborrow, J. B.; Walker, K. D. Enhanced Conversion of Racemic α-Arylalanines to (R)-β-Arylalanines by Coupled Racemase/Aminomutase Catalysis. J. Org. Chem. 2009, 74, 6953−6959.
257. Walker, K. D.; Cox, B. M. Process for the Preparation of (R)Beta-Arylalanines by Coupled Racemase/Aminomutase Catalysis. U.S. Patent US 20100285540, 2010.
258. Wanninayake, U.; DePorre, Y.; Ondari, M.; Walker, K. D. S)-Styryl-α-Alanine Used to Probe the Intermolecular Mechanism of an Intramolecular MIO-Aminomutase. Biochemistry 2011, 50, 10082− 10090.
259. Wanninayake, U.; Walker, K. D. Assessing the Deamination Rate of a Covalent Aminomutase Adduct by Burst Phase Analysis. Biochemistry 2012, 51, 5226−5228.
260. Hidesaki, T. Phenylalanine Aminomutase with Selectivity for S-Form, DNA Encoding the Same, Method for Producing (S)-β-Phenylalanine and Method for Producing (S)-β-Phenylalanine Analogs. World Patent WO 2008129873, 2008.
261. Hidesaki, T. Method for Producing β-Amino Acid. World Patent WO 2009044531, 2009.
262. Varga, A.; Bano ćzi, G.; Nagy, B.; Bencze, L. C.; Tosa, M. I.; Gellert, Á.; Irimie, F. D.; Retey, J.; Poppe, L.; Paizs, C. Influence of the Aromatic Moiety in α- and β-Arylalanines on Their Biotransformation with Phenylalanine 2,3-Aminomutase from Pantoea agglomerans. RSC Adv. 2016, 6, 56412−56420.
263. Wu, B.; Szymanski, W.; De Wildeman, S.; Poelarends, G. J.; Feringa, B. L.; Janssen, D. B. Efficient Tandem Biocatalytic Process for the Kinetic Resolution of Aromatic β-Amino Acids. Adv. Synth. Catal. 2010, 352, 1409−1412.
264. Wu, B.; Szymanski, W.; Wietzes, P.; De Wildeman, S.; Poelarends, G. J.; Feringa, B. L.; Janssen, D. B. Enzymatic Synthesis of Enantiopure α- and β-Amino Acids by Phenylalanine Aminomutase-Catalysed Amination of Cinnamic Acid Derivatives. ChemBioChem 2009, 10, 338−344.
265. Szymanski, W.; Wu, B.; Weiner, B.; de Wildeman, S.; Feringa, B. L.; Janssen, D. B. Phenylalanine Aminomutase-Catalyzed Addition of Ammonia to Substituted Cinnamic Acids: A Route to Enantiopure α- and β-Amino Acids. J. Org. Chem. 2009, 74, 9152−9157.
266. Verkuijl, B. J. V; Szymanski, W.; Wu, B.; Minnaard, A. J.; Janssen, D. B.; de Vries, J. G.; Feringa, B. L. Enantiomerically Pure β -Phenylalanine Analogues from α-β-Phenylalanine Mixtures in a Single Reactive Extraction Step. Chem. Commun. 2010, 46, 901−903.
267. Heberling, M. M.; Masman, M. F.; Bartsch, S.; Wybenga, G. G.; Dijkstra, B. W.; Marrink, S. J.; Janssen, D. B. Ironing out Their Differences: Dissecting the Structural Determinants of a Phenylalanine Aminomutase and Ammonia Lyase. ACS Chem. Biol. 2015, 10, 989− 997.
268. Williams, J. S.; Thomas, M.; Clarke, D. J. The Gene stlA Encodes a Phenylalanine Ammonia-Lyase That Is Involved in the Production of a Stilbene Antibiotic in Photorhabdus luminescens TT01. Microbiology 2005, 151, 2543−2550.
269. Weise, N. J.; Parmeggiani, F.; Ahmed, S. T.; Turner, N. J. The Bacterial Ammonia Lyase EncP: A Tunable Biocatalyst for the Synthesis of Unnatural Amino Acids. J. Am. Chem. Soc. 2015, 137, 12977−12983.
270. Segala, M.; Takahata, Y.; Chong, D. P. Geometry, Solvent, and Polar Effects on the Relationship between Calculated Core-Electron Binding Energy Shifts (ΔCEBE) and Hammett Substituent (σ) Constants. J. Mol. Struct.: THEOCHEM 2006, 758, 61−69.
271. Paizs, C.; Katona, A.; Retey, J. Chemoenzymatic One-Pot Synthesis of Enantiopure L-Arylalanines from Arylaldehydes. Eur. J. Org. Chem. 2006, 2006, 1113−1116.
272. De Lange, B.; Hyett, D. J.; Maas, P. J. D.; Mink, D.; Van Assema, F. B. J.; Sereinig, N.; De Vries, A. H. M.; De Vries, J. G. Asymmetric Synthesis of (S)-2-Indolinecarboxylic Acid by Combining Biocatalysis and Homogeneous Catalysis. ChemCatChem 2011, 3, 289−292.
273. Parmeggiani, F.; Weise, N. J.; Ahmed, S. T.; Turner, N. J. Chemoenzymatic Synthesis of (S)-1,2,3,4-Tetrahydroisoquinoline-3-Carboxylic Acid by PAL-Mediated Amination and Pictet-Spengler Cyclization. Practical Methods for Biocatalysis and Biotransformations 3; Whittall, J., Sutton, P. W., Kroutil, W., Eds.; Wiley: 2016; pp 243−246.
274. Roughley, S. D.; Jordan, A. M. The Medicinal Chemist’s Toolbox: An Analysis of Reactions Used in the Pursuit of Drug Candidates. J. Med. Chem. 2011, 54, 3451−3479.
275. Nielsen, D. R.; McKenna, R. Microbial Conversion of Glucose to Styrene and Its Derivatives. World Patent WO 2012122333 A1, 2012.
276. Busto, E.; Simon, R. C.; Kroutil, W. Vinylation of Unprotected Phenols Using a Biocatalytic System. Angew. Chem., Int. Ed. 2015, 54, 10899−10902.
277. Zhou, Y.; Wu, S.; Li, Z. Cascade Biocatalysis for Sustainable Asymmetric Synthesis: From Biobased L-Phenylalanine to High-Value Chiral Chemicals. Angew. Chem., Int. Ed. 2016, 55, 11647−11650.
278. Katsuyama, Y.; Funa, N.; Horinouchi, S. Precursor-Directed Biosynthesis of Stilbene Methyl Ethers in Escherichia coli. Biotechnol. J. 2007, 2, 1286−1293.
279. Li, M.; Kildegaard, K. R.; Chen, Y.; Rodriguez, A.; Borodina, I.; Nielsen, J. De novo Production of Resveratrol from Glucose or Ethanol by Engineered Saccharomyces cerevisiae. Metab. Eng. 2015, 32, 1−11.
280. Li, M.; Schneider, K.; Kristensen, M.; Borodina, I.; Nielsen, J. Engineering Yeast for High-Level Production of Stilbenoid Antioxidants. Sci. Rep. 2016, 6, 36827.
281. Ro, D. K.; Douglas, C. J. Reconstitution of the Entry Point of Plant Phenylpropanoid Metabolism in Yeast (Saccharomyces cerevisiae): Implications for Control of Metabolic Flux into the Phenylpropanoid Pathway. J. Biol. Chem. 2004, 279, 2600−2607.
282. Miyahisa, I.; Funa, N.; Ohnishi, Y.; Martens, S.; Moriguchi, T.; Horinouchi, S. Combinatorial Biosynthesis of Flavones and Flavonols in Escherichia coli. Appl. Microbiol. Biotechnol. 2006, 71, 53−58.
283. Trantas, E.; Panopoulos, N.; Ververidis, F. Metabolic Engineering of the Complete Pathway Leading to Heterologous Biosynthesis of Various Flavonoids and Stilbenoids in Saccharomyces cerevisiae. Metab. Eng. 2009, 11, 355−366.
284. Jendresen, C. B.; Stahlhut, S. G.; Li, M.; Gaspar, P.; Siedler, S.; Förster, J.; Maury, J.; Borodina, I.; Nielsen, A. T. Highly Active and Specific Tyrosine Ammonia-Lyases from Diverse Origins Enable Enhanced Production of Aromatic Compounds in Bacteria and Saccharomyces cerevisiae. Appl. Environ. Microbiol. 2015, 81, 4458− 4476.
285. Cantor, J. R.; Panayiotou, V.; Agnello, G.; Georgiou, G.; Stone, E. M. Engineering Reduced-Immunogenicity Enzymes for Amino Acid Depletion Therapy in Cancer. Methods Enzymol. 2012, 502, 291−319.
286. Fu, Y. M.; Yu, Z. X.; Pelayo, B. A.; Ferrans, V. J.; Meadows, G. G. Focal Adhesion Kinase-Dependent Apoptosis of Melanoma Induced by Tyrosine and Phenylalanine Deficiency. Cancer Res. 1999, 59, 758−765.
287. Pelayo, B. A.; Fu, Y. M.; Meadows, G. G. Inhibition of B16BL6 Melanoma Invasion by Tyrosine and Phenylalanine Deprivation Is Associated with Decreased Secretion of Plasminogen Activators and Increased Plasminogen Activator Inhibitors. Clin. Exp. Metastasis 1999, 17, 841−848.
288. Kovaćs, K.; Bano ćzi, G.; Varga, A.; Szabo, I.; Holczinger, A.; Hornyanszky, G.; Zagyva, I.; Paizs, C.; Vertessy, B. G.; Poppe, L. Expression and Properties of the Highly Alkalophilic Phenylalanine Ammonia-Lyase of Thermophilic Rubrobacter xylanophilus. PLoS One 2014, 9, e85943.
289. Abell, C. W.; Stith, W. J.; Hodgins, D. S. The Effects of Phenylalanine Ammonia-Lyase on Leukemic Lymphocytes in vitro. Cancer Res. 1972, 32, 285−290.
290. Stith, W. J.; Hodgins, D. S.; Abell, C. W. Effects of Phenylalanine Ammonia-Lyase and Phenylalanine Deprivation on Murine Leukemic Lymphoblasts in vitro. Cancer Res. 1973, 33, 966− 971.
291. Abell, C. W.; Hodgins, D. S.; Stith, W. J. An in vivo Evaluation of the Chemotherapeutic Potency of Phenylalanine Ammonia-Lyase. Cancer Res. 1973, 33, 2529−2532.
292. Roberts, J.; Schmid, F. A.; Rosenfeld, H. J. Biological and Antineoplastic Effects of Enzyme-Medicated in vivo Deletion of L-Glutamine, L-Tryptophan, and L-Histidine. Cancer Treat. Rep. 1979, 63, 1045−1054.
293. Jack, G.; Wiblin, C.; McMahon, P. The Effect of Histidine Ammonia Lyase on Some Murine Tumours. Leuk. Res. 1983, 7, 421− 429.
294. Shen, R.; Fritz, R.; Abell, C. Biochemical Properties and Immunogenicity of L-Phenylalanine Ammonia-Lyase: Effects on Tumor-Bearing Mice. Cancer Treat. Rep. 1979, 63, 1063−1068.
295. Sethuraman, N.; Roberts, J.; Macallister, T. Cloning of Corynebacteriaceae Histidine Ammonia Lyase and Therapeutic Uses. World Patent WO 2001079469, 2001.
296. Sethuraman, N.; Roberts, J.; Macallister, T. Cloning, Overexpression and Therapeutic Use of Bioactive Histidine Ammonia Lyase. U.S. Patent US 6939541, 2005.
297. Vellard, M. C.; Fitzpatrick, P. A.; Kakkis, E. D.; Wendt, D. J.; Muthalif, M.; Bell, S. M.; Okhamafe, A. O. Compositions of Prokaryotic Phenylalanine Ammonia-Lyase and Methods of Treating Cancer Using Compositions Thereof. World Patent WO 2009025760, 2009.
298. Babich, O. O.; Pokrovsky, V. S.; Anisimova, N. Y.; Sokolov, N. N.; Prosekov, A. Y. Recombinant L-Phenylalanine Ammonia Lyase from Rhodosporidium toruloides as a Potential Anticancer Agent. Biotechnol. Appl. Biochem. 2013, 60, 316−322.
299. Gamez, A.; Sarkissian, C. N.; Wang, L.; Kim, W.; Straub, M.; Patch, M. G.; Chen, L.; Striepeke, S.; Fitzpatrick, P.; Lemontt, J. F.; O’Neill, C.; Scriver, C. R.; Stevens, R. C. Development of Pegylated Forms of Recombinant Rhodosporidium toruloides Phenylalanine Ammonia-Lyase for the Treatment of Classical Phenylketonuria. Mol. Ther. 2005, 11, 986−989.
300. Sarkissian, C. N.; Kang, T. S.; Gamez, A.; Scriver, C. R.; Stevens, R. C. Evaluation of Orally Administered PEGylated Phenylalanine Ammonia Lyase in Mice for the Treatment of Phenylketonuria. Mol. Genet. Metab. 2011, 104, 249−254.
301. enu2 Mice. J. Controlled Release 2014, 194, 37−44.
302. Belanger-Quintana, A.; Burlina, A.; Harding, C. O.; Muntau, A. C. Up to Date Knowledge on Different Treatment Strategies for Phenylketonuria. Mol. Genet. Metab. 2011, 104, S19−S25.
303. Ikeda, K.; Schiltz, E.; Fujii, T.; Takahashi, M.; Mitsui, K.; Kodera, Y.; Matsushima, A.; Inada, Y.; Schulz, G. E.; Nishimura, H. Phenylalanine Ammonia-Lyase Modified with Polyethylene Glycol: Potential Therapeutic Agent for Phenylketonuria. Amino Acids 2005, 29, 283−287.
304. Huisman, G. W.; Agard, N. J.; Elgart, D.; Zhang, X. Engineered Tyrosine Ammonia Lyase. World Patent WO 2015161019 A1, 2015.
305. Castañeda, M. T.; Adachi, O.; Hours, R. A. Reduction of L-Phenylalanine in Protein Hydrolysates Using L-Phenylalanine Ammonia-Lyase from Rhodosporidium toruloides. J. Ind. Microbiol. Biotechnol. 2015, 42, 1299−1307.
306. Sarkissian, C. N.; Gamez, A. Phenylalanine Ammonia Lyase, Enzyme Substitution Therapy for Phenylketonuria, Where Are We Now? Mol. Genet. Metab. 2005, 86, S22−S26.
307. Kang, T. S.; Wang, L.; Sarkissian, C. N.; Gamez, A.; Scriver, C. R.; Stevens, R. C. Converting an Injectable Protein Therapeutic into an Oral Form: Phenylalanine Ammonia Lyase for Phenylketonuria. Mol. Genet. Metab. 2010, 99, 4−9.
308. Longo, N.; Harding, C. O.; Burton, B. K.; Grange, D. K.; Vockley, J.; Wasserstein, M.; Rice, G. M.; Dorenbaum, A.; Neuenburg, J. K.; Musson, D. G.; Gu, Z.; Sile, S. Single-Dose, Subcutaneous Recombinant Phenylalanine Ammonia Lyase Conjugated with Polyethylene Glycol in Adult Patients with Phenylketonuria: an Open-Label, Multicentre, Phase 1 Dose-Escalation Trial. Lancet 2014, 384, 37−44.
309. Jaliani, H. Z.; Farajnia, S.; Mohammadi, S. A.; Barzegar, A.; Talebi, S. Engineering and Kinetic Stabilization of the Therapeutic Enzyme Anabaena variabilis Phenylalanine Ammonia Lyase. Appl. Biochem. Biotechnol. 2013, 171, 1805−1818.
310. Liu, J.; Jia, X.; Zhang, J.; Xiang, H.; Hu, W.; Zhou, Y. Study on a Novel Strategy to Treatment of Phenylketonuria. Artif. Cells, Blood Substit., Immobil. Biotechnol. 2002, 30, 243−257.
311. Zhang, Y.; Jia, X.; Wang, L.; Liu, J.; Ma, G. Preparation of Ca-Alginate Microparticles and Its Application for Phenylketonuria Oral Therapy. Ind. Eng. Chem. Res. 2011, 50, 4106−4112.
312. Bourget, L.; Chang, T. M. S. Phenylalanine Ammonia-Lyase Immobilized in Semipermeable Microcapsules for Enzyme Replacement in Phenylketonuria. FEBS Lett. 1985, 180, 5−8.
313. Shah, R. M.; D’mello, A. P. Stabilization of Phenylalanine Ammonia Lyase against Organic Solvent Mediated Deactivation. Int. J. Pharm. 2007, 331, 107−115.
314. Shah, R. M.; D’mello, A. P. Strategies to Maximize the Encapsulation Efficiency of Phenylalanine Ammonia Lyase in Microcapsules. Int. J. Pharm. 2008, 356, 61−68.
315. Wang, L.; Gamez, A.; Sarkissian, C. N.; Straub, M.; Patch, M. G.; Won Han, G.; Striepeke, S.; Fitzpatrick, P.; Scriver, C. R.; Stevens, R. C. Structure-Based Chemical Modification Strategy for Enzyme Replacement Treatment of Phenylketonuria. Mol. Genet. Metab. 2005, 86, 134−140.
316. MacDonald, C. B. J.; Tobin, A. M. F.; Morrison, A. A. E.; Tait, M. E.; D’Cunha, A. G. B.; MacQuarrie, S. L. Generation of a Highly Stable Reusable Biocatalyst by Entrapment of an Oligomeric Enzyme in Ultra-Large-Pore Mesoporous Silica. Aust. J. Chem. 2015, 68, 396− 400.
317. Hosta-Rigau, L.; York-Duran, M. J.; Kang, T. S.; Stadler, B. Extracellular Microreactor for the Depletion of Phenylalanine Toward Phenylketonuria Treatment. Adv. Funct. Mater. 2015, 25, 3860−3869.
318. Cui, J. D.; Zhang, S.; Sun, L. M. Cross-Linked Enzyme Aggregates of Phenylalanine Ammonia Lyase: Novel Biocatalysts for Synthesis of L-Phenylalanine. Appl. Biochem. Biotechnol. 2012, 167, 835−844.
319. Cui, J. D.; Li, L. L.; Zhao, Y. M. Simple Technique for Preparing Stable and Recyclable Cross-Linked Enzyme Aggregates with Crude-Pored Microspherical Silica Core. Ind. Eng. Chem. Res. 2014, 53, 16176−16182.
320. Zhu, L.; Zhou, L.; Cui, W.; Liu, Z.; Zhou, Z. Mechanism-Based Site-Directed Mutagenesis to Shift the Optimum pH of the Phenylalanine Ammonia-Lyase from Rhodotorula glutinis JN-1. Biotechnol. Reports 2014, 3, 21−26.
321. Eigtved, P.; Groth Clausen, I. Stabilised Phenylalanine Ammonia Lyase. U.S. Patent US 5753487 A, 1998.
322. Huisman, G. W.; Agard, N. J.; Mijts, B.; Vroom, J.; Zhang, X. Engineered Phenylalanine Ammonia Lyase Polypeptides. World PatentWO 2014172541 A3, 2015.
323. Noel, J. P.; Louie, G. V.; Bowman, M. E.; Moore, B. S.; Moffitt, M. C. Substrate Switched Ammonia Lyases and Mutases. U.S. Patent US 20090011400, 2009.