C-N lyases Catalyzing Addition of Ammonia, Amines, and Amides to C=C and C=O Bonds

Enzyme Catalysis in Organic Synthesis, Third Edition

Volumn 2, Issue , 2012, Pages 749-778

  Wu, Bian ^a   Szymanski, Wiktor ^a,b   Crismaru, Ciprian G ^a   Feringa, Ben L ^b   Janssen, Dick B ^b  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

^b UNIVERSITY OF GRONINGEN   (Netherlands)

Author keywords

Amination; Ammonia lyases; Aspartase; Biocatalysis; Michael addition

Indexed keywords

EID: 84871854963     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527639861.ch18     Document Type: Chapter

References (109)

1. Poppe, L. and Rétey, J. (2005) Friedel-Crafts-type mechanism for the enzymatic elimination of ammonia from histidine and phenylalanine. Angew. Chem. Int. Ed., 44 (24), 3668-3688.
2. MacDonald, M.J. and D'Cunha, G.B. (2007) A modern view of phenylalanine ammonia lyase. Biochem. Cell. Biol., (3), 273-282.
3. Cooke, H.A., Christianson, C.V., and Bruner, S.D. (2009) Structure and chemistry of 4-methylideneimidazole-5- one containing enzymes. Curr. Opin. Chem. Biol., 13 (4), 453-461.
4. Asano, Y., Kato, Y., Levy, C., Baker, P., and Rice, D. (2004) Structure and function of amino acid ammonia-lyases. Biocatal. Biotransform., 22 (2), 131-138.
5. Mizobata, T. and Kawata, Y. (2007) Aspartases, in Industrial Enzymes - Structure, Functions and Applications (eds J. Polaina and A.P. MacCabe), Springer, Dordrecht, pp. 549-565.
6. Poechlauer, P., Braune, S., de Vries, A., and May, O. (2010) Sustainable route design for pharmaceuticals. Why, how and when. Chim. Oggi, 28 (4), 14-17.
7. Takagi, J.S., Ida, N., Tokushige, M., Sakamoto, H., and Shimura, Y. (1985) Cloning and nucleotide sequence of the aspartase gene of Escherichia coli W. Nucleic Acids Res., 13 (6), 2063-2074.
8. Karsten,W.E.,Gates, R.B., and Viola, R.E. (1986) Kinetic studies of L-aspartase from Escherichia coli: substrate activation. Biochemistry, 25 (6), 1299-1303.
9. Kawata, Y., Tamura, K., Yano, S., Mizobata,T., Nagai, J., Esaki, N., Soda, K., Tokushige, M., and Yumoto, N. (1999) Purification and characterization of thermostable aspartase from Bacillus sp YM55-1. Arch. Biochem. Biophys., 366 (1), 40-46.
10. Nuiry, I.I., Hermes, J.D., Weiss, P.M., Chen, C.Y., and Cook, P.F. (1984) Kinetic mechanism and location of ratedetermining steps for aspartase from Hafnia alvei. Biochemistry, 23 (22), 5168-5175.
11. Shi, W., Dunbar, J., Jayasekera, M.M., Viola, R.E., and Farber, G.K. (1997) The structure of L-aspartate ammonialyase from Escherichia coli. Biochemistry, (30), 9136-9144.
12. Fujii, T., Sakai, H., Kawata, Y., and Hata, Y. (2003) Crystal structure of thermostable aspartase from Bacillus sp. YM55-1: structure-based exploration of functional sites in the aspartase family. J. Mol. Biol., 328 (3), 635-654.
13. Puthan Veetil, V., Raj, H., Quax, W.J., Janssen, D.B., and Poelarends, G.J. (2009) Site-directed mutagenesis, kinetic and inhibition studies of aspartate ammonia lyase from Bacillus sp. YM55-1. FEBS J., 276 (11), 2994-3007.
14. Takagi, J.S., Tokushige, M., and Shimura, Y. (1986) Cloning and nucleotide sequence of the aspartase gene of Pseudomonas fluorescens. J. Biochem., 100 (3), 697-705.
15. Sun, D.X. and Setlow, P. (1991) Cloning, nucleotide sequence, and expression of the Bacillus subtilis ans operon, which codes for L-asparaginase and L-aspartase. J. Bacteriol., 173 (12), 3831-3845.
16. Kawata, Y., Tamura, K., Kawamura, M., Ikei, K., Mizobata, T., Nagai, J., Fujita, M., Yano, S., Tokushige, M., and Yumoto, N. (2000) Cloning and over-expression of thermostable Bacillus sp. YM55-1 aspartase and site-directed mutagenesis for probing a catalytic residue. Eur. J. Biochem., 267 (6), 1847-1857.
17. Kazuoka, T., Masuda, Y., Oikawa, T., and Soda, K. (2003) Thermostable aspartase from a marine psychrophile, Cytophaga sp. KUC-1: molecular characterization and primary structure. J. Biochem., (1), 51-58.
18. Sato, T., Nishida, Y., Tosa, T., and Chibata, I. (1979) Immobilization of Escherichia coli cells containing aspartase activity with k-carrageenan: enzymic properties and application for l-aspartic acid production. Biochim. Biophys. Acta, (1), 179-186.
19. Tokushige, M. (1985) Aspartate ammonia-lyase. Meth. Enzymol., 113, 618-627.
20. Chibata, I., Tosa, T., and Sato, T. (1974) Immobilized aspartase-containing microbial cells: preparation and enzymatic properties. Appl. Microbiol., (5), 878-885.
21. Tosa, T., Sato, T., Nishida, Y., and Chibata, I. (1977) Reason for higher stability of aspartase activity of immobilized Escherichia coli cells. Biochim. Biophys. Acta, 483 (1), 193-202.
22. Nishida, Y., Sato, T., Tosa, T., and Chibata, I. (1979) Immobilization of Escherichia coli cells having aspartase activity with carrageenan and locust bean gum. Enzyme Microb. Technol., 1 (2), 95-99.
23. Hamilton, B.K., Hsiao, H.Y., Swann, W.E., Anderson, D.M., and Delente, J.J. (1985) Manufacture of Lamino acids with bioreactors. Trends Biotechnol., 3 (3), 64-68.
24. Chao, Y.P., Lo, T.E., and Luo, N.S. (2000) Selective production of L-aspartic acid and L-phenylalanine by coupling reactions of aspartase and aminotransferase in Escherichia coli. Enzyme Microb. Technol., 27 (1-2), 19-25.
25. Xu, H., Wei, P., Zhou, H., Fan, W., and Ouyang, P. (2003) Efficient production of L-phenylalanine catalyzed by a coupled enzymatic system of transaminase and aspartase. Enzyme Microb. Technol., 33 (5), 537-543.
26. Fatibello-Filho, O., Suleiman, A.A., Guilbault, G.G., and Lubrano, G.J. (1988) Bienzymatic electrode for the determination of aspartame in dietary products. Anal. Chem., 60 (21), 2397-2399.
27. Wang, Z.W., Chen, Y., and Chao, Y.P. (2006) Enhancement of recombinant protein production in Escherichia coli by coproduction of aspartase. J. Biotechnol., (2), 403-411.
28. Weiner, B., Poelarends, G.J., Janssen, D.B., and Feringa, B.L. (2008) Biocatalytic enantioselective synthesis of N-substituted aspartic acids by aspartate ammonia lyase. Chemistry, 14 (32), 10094-10100.
29. Wang, L.J., Kong, X.D., Zhang, H.Y., Wang, X.P., and Zhang, J. (2000) Enhancement of the activity of Laspartase from Escherichia coli W by directed evolution. Biochem. Biophys. Res. Commun., 276 (1), 346-349.
30. Kong, X., Li, Z., Gou, X., Zhu, S., Zhang, H., Wang, X., and Zhang, J. (2002) A monomeric L-aspartase obtained by in vitro selection. J. Biol. Chem., 277 (27), 24289-24293.
31. Sheng, Y., Li, S., Gou, X., Kong, X., Wang, X., Sun, Y., and Zhang, J. (2005) The hybrid enzymes from alpha-aspartyl dipeptidase and L-aspartase. Biochem. Biophys. Res. Commun., (1), 107-112.
32. Asano, Y., Kira, I., and Yokozeki, K. (2005) Alteration of substrate specificity of aspartase by directed evolution. Biomol. Eng., 22 (1-3), 95-101.
33. Bulusu, V., Srinivasan, B., Bopanna, M.P., and Balaram, H. (2009) Elucidation of the substrate specificity, kinetic and catalytic mechanism of adenylosuccinate lyase from Plasmodium falciparum. Biochim. Biophys. Acta, 1794 (4), 642-654.
34. Kozlov, G., Nguyen, L., Pearsall, J., and Gehring, K. (2009) The structure of phosphate-bound Escherichia coli adenylosuccinate lyase identifies His171 as a catalytic acid. Acta Crystallogr., Sect. F, (9), 857-861.
35. Bhaumik, P., Koski, M.K., Bergmann, U., and Wierenga, R.K. (2004) Structure determination and refinement at 2.44 A resolution of argininosuccinate lyase from Escherichia coli. Acta. Crystallogr., Sect. D, 60 (11), 1964-1970.
36. Lam, T.L., Wong, G.K., Chong, H.C., Cheng, P.N., Choi, S.C., Chow, T.L., Kwok, S.Y., Poon, R.T., Wheatley, D.N., Lo, W.H., and Leung, Y.C. (2009) Recombinant human arginase inhibits proliferation of human hepatocellular carcinoma by inducing cell cycle arrest. Cancer Lett., 277 (1), 91-100.
37. Wu, C.Y., Lee, H.J.,Wu, S.H., Chen, S.T., Chiou, S.H., and Chang, G.G. (1998) Chemical mechanism of the endogenous argininosuccinate lyase activity of duck lens delta2-crystallin. Biochem J., 333 (2), 327-334.
38. Bauerle, B., Cokesa, Z., Hofmann, S., and Rieger, P.G. (2006) Sequencing and heterologous expression of an epimerase and two lyases from iminodisuccinate-degrading bacteria. Appl. Environ. Microbiol., 72 (4), 2824-2828.
39. Wataru, M. (1998) Protein having ethylenediamine-N,N0-disuccinic acid: ethylenediamine lyase activity and gene encoding the same. European Patent EP0845536.
40. Kaneko, M. (2003) Processes for producing S,S-2-hydroxypropylene diamine-N,N0-disuccinic acid. US Patent 6503739.
41. Mizunashi, W. and Nakamura, T. (2005) Modified ethylenediamine-N,N0 disuccinic acid: ethylenediamine lyase. European Patent EP1757685.
42. Gerlt, J.A., Babbitt, P.C., and Rayment, I. (2005) Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity. Arch. Biochem. Biophys., (1), 59-70.
43. Goda, S.K., Minton, N.P., Botting, N.P., andGani, D. (1992) Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein. Biochemistry, 31 (44), 10747-10756.
44. Kato, Y. and Asano, Y. (1988) Cloning, nucleotide sequencing, and expression of the 3-methylaspartate ammonia-lyase gene from Citrobacter amalonaticus strain YG-1002. Appl. Microbiol. Biotechnol., (4), 468-474.
45. Kato, Y. and Asano, Y. (1995) 3-Methylaspartate ammonia-lyase from a facultative anaerobe, strain YG-1002. Appl. Microbiol. Biotechnol., 43 (5), 901-907.
46. Levy, C.W., Buckley, P.A., Sedelnikova, S., Kato, Y., Asano, Y., Rice, D.W., and Baker, P.J. (2002) Insights into enzyme evolution revealed by the structure of methylaspartate ammonia lyase. Structure, 10 (1), 105-113.
47. Asuncion, M., Blankenfeldt, W., Barlow, J.N., Gani, D., and Naismith, J.H. (2002) The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step. J. Biol. Chem., 277 (10), 8306-8311.
48. Raj, H., Weiner, B., Veetil, V.P., Reis, C.R., Quax, W.J., Janssen, D.B., Feringa, B.L., and Poelarends, G.J. (2009) Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis. ChemBioChem, 10 (13), 2236-2245.
49. Akhtar, M., Botting, N.P., Cohen, M.A., and Gani, D. (1987) Enantiospecific synthesis of 3-substituted aspartic acids via enzymic amination of substituted fumaric acids. Tetrahedron, 43 (24), 5899-5908.
50. Akhtar, M., Cohen, M.A., and Gani, D. (1987) Stereochemical course of the enzymic amination of chloro- and bromo fumaric acid by 3-methylaspartate ammonia-lyase. Tetrahedron Lett., 28 (21), 2413-2416.
51. Botting, N.P., Akhtar, M., Cohen, M., and Gani, D. (1988) Substrate-specificity of the 3-methylaspartate ammonia-lyase reaction: observation of differential relative reaction-rates for substrate product pairs. Biochemistry, 27 (8), 2953-2955.
52. Gulzar, M.S., Akhtar, M., and Gani, D. (1997) 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, 649-655.
53. Lee, H.Y., Yoon, M., and Marsh, E.N. (2007) Synthesis of mono- and di-deuterated (2S, 3S)-3-methylaspartic acids to facilitate measurement of intrinsic kinetic isotope effects in enzymes. Tetrahedron, 63 (22), 4663-4668.
54. Schwede, T.F., Retey, J., and Schulz, G.E. (1999) Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile. Biochemistry, 38 (17), 5355-5361.
55. Christianson, C.V., Montavon, T.J., Van Lanen, S.G., Shen, B., and Bruner, S.D. (2007) The structure of L-tyrosine 2,3-aminomutase from the C-1027 enediyne antitumor antibiotic biosynthetic pathway. Biochemistry, (24), 7205-7214.
56. Pilbák, S., Tomin, A., Rétey, J., and Poppe, L. (2006) The essential tyrosinecontaining loop conformation and the role of the C-terminal multi-helix region in eukaryotic phenylalanine ammonialyases. FEBS J., 273 (5), 1004-1019.
57. 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., and Stevens, R.C. (2008) Structural and biochemical characterization of the therapeutic Anabaena variabilis phenylalanine ammonia lyase. J. Mol. Biol., 380 (4), 623-635.
58. Ritter, H. and Schulz, G.E. (2004) Structural basis for the entrance into the phenylpropanoid metabolism catalyzed by phenylalanine ammonia-lyase. Plant Cell, 16 (12), 3426-3436.
59. Calabrese, J.C., Jordan, D.B., Boodhoo, A., Sariaslani, S., and Vannelli, T. (2004) Crystal structure of phenylalanine ammonia lyase: multiple helix dipoles implicated in catalysis. Biochemistry, 43 (36), 11403-11416.
60. Moffitt, M.C., Louie, G.V., Bowman, M.E., Pence, J., Noel, J.P., and Moore, B.S. (2007) Discovery of two cyanobacterial phenylalanine ammonia lyases: kinetic and structural characterization. Biochemistry, 46 (4), 1004-1012.
61. Louie, G.V., Bowman, M.E., Moffitt, M.C., Baiga, T.J., Moore, B.S., and Noel, J.P. (2006) Structural determinants and modulation of substrate specificity in phenylalaninetyrosine ammonia-lyases. Chem. Biol., 13, 1327-1338.
62. 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., Lemontth, J.F., Scriver, C.R., and Stevens, R.C. (2008) Structural and biochemical characterization of the therapeutic Anabaena variabilis phenylalanine ammonia lyase. J. Mol. Biol., 380 (4), 623-635.
63. Wu, B., Szymanski, W., Wietzes, P., de Wildeman, S., Poelarends, G.J., Feringa, B.L., and Janssen, D.B. (2009) Enzymatic synthesis of enantiopure alpha- and beta-amino acids by phenylalanine aminomutase-catalysed amination of cinnamic acid derivatives. ChemBioChem, 10 (2), 338-344.
64. Bartsch, S. and Bornscheuer, U.T. (2009) A single residue influences the reaction mechanism of ammonia lyases and mutases. Angew. Chem. Int. Ed., 48 (18), 3362-3365.
65. Xiang, L. and Moore, B.S. (2002) Inactivation, complementation, and heterologous expression of encP, a novel bacterial phenylalanine ammonia-lyase gene. J. Biol. Chem., 277 (36), 32505-32509.
66. Christenson, S.D., Liu, W., Toney, M.D., and Shen, B. (2003) A novel 4- methylideneimidazole-5-one-containing tyrosine aminomutase in enediyne antitumor antibiotic C-1027 biosynthesis. J. Am. Chem. Soc., 125 (20), 6062-6063.
67. Krug, D. and Müller, R. (2009) Discovery of additional members of the tyrosine aminomutase enzyme family and the mutational analysis of CmdF. ChemBioChem, 10 (4), 741-750.
68. Ro, D.K. and Douglas, C.J. (2004) 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., (4), 2600-2607.
69. Gloge, A., Langer, B., Poppe, L., and Rétey, J. (1998) The behavior of substrate analogues and secondary deuterium isotope effects in the phenylalanine ammonia-lyase reaction. Arch. Biochem. Biophys., 359 (1), 1-7.
70. Gloge, A., Zoń, J., Kövári, A., Poppe, L., and Rétey, J. (2000) Phenylalanine ammonia-lyase: the use of its broad substrate specificity for mechanistic investigations and biocatalysis-synthesis of L-arylalanines. Chem. Eur. J., 6 (18), 3386-3390.
71. Paizs, C., Katona, A., and Rétey, J. (2006) The interaction of heteroaryl-acrylates and alanines with phenylalanine ammonia-lyase from parsley. Chem. Eur. J., 12 (10), 2739-2744.
72. Liu,W. (1999) Synthesis of optically active phenylalanine analogs using Rhodotorula graminis. US Patent 5981239.
73. Van Assema, F.B.J. and Sereinig, N. (2008) Method for producing optically active phenylalanine compounds from cinnamic acid derivatives employing a phenylalanine ammonia lyase derived from Idiomarina loihiensis. Intern. Patent Appl. No. PCT/EP2007/007945.
74. Gámez, 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., and Stevens, R.C. (2005) Development of pegylated forms of recombinant Rhodosporidium toruloides phenylalanine ammonia-lyase for the treatment of classical phenylketonuria. Mol. Therapy, (6), 986-989.
75. Kang, T.S., Wang, L., Sarkissian, C.N., Gámez, A., Scriver, C.R., and Stevens, R.C. (2010) Converting an injectable protein therapeutic into an oral form: phenylalanine ammonia lyase for phenylketonuria. Mol. Genet. Metab., (1), 4-9.
76. Klettke, K.L., Sanyal, S., Mutatu, W., and Walker, K.D. (2007) Beta-aryl-betaalanine products of phenylalanine aminomutase catalysis. J. Am. Chem. Soc., 129 (22), 6988-6989.
77. Szymanski, W., Wu, B., Weiner, B., de Wildeman, S., Feringa, B.L., and Janssen, D.B. (2009) Phenylalanine aminomutase-catalyzed addition of ammonia to substituted cinnamic acids: a route to enantiopure alpha- and betaamino acids. J. Org. Chem., 74 (23), 9152-9157.
78. Wang, L., Gamez, A., Sarkissian, C.N., Straub, M., Patch, M.G., Han, G.W., Striepeke, S., Fitzpatrick, P., Scriver, C.R., and Stevens, R.C. (2005) Structurebased chemical modification strategy for enzyme replacement treatment of phenylketonuria. Mol. Genet. Metab., (1-2), 134-140.
79. Watts, K.T., Mijts, B.N., Lee, P.C., Manning, A.J., and Schmidt-Dannert, C. (2006) Discovery of a substrate selectivity switch in tyrosine ammonialyase, a member of the aromatic amino acid lyase family. Chem. Biol., 13 (12), 1317-1326.
80. Herrmann, G., Selmer, T., Jessen, H.J., Gokarn, R.R., Selifonova, O., Gort, S.J., and Buckel, W. (2005) Two beta-alanyl- CoA: ammonia lyases in Clostridium propionicum. FEBS J., 272 (3), 813-821.
81. Kreimeyer, A., Perret, A., Lechaplais, C., Vallenet, D., Médigue, C., Salanoubat, M., and Weissenbach, J. (2007) Identification of the last unknown genes in the fermentation pathway of lysine. J. Biol. Chem., 282 (10), 7191-7197.
82. Jiang, X., Meng, X., and Xian, M. (2009) Biosynthetic pathways for 3- hydroxypropionic acid production. Appl. Microbiol. Biotechnol., 82 (6), 995-1003.
83. Dillon, S.C. and Bateman, A. (2004) The hotdog fold: wrapping up a superfamily of thioesterases and dehydratases. BMC Bioinformatics, 12 (5), 109.
84. Eliot, A.C. and Kirsch, J.F. (2004) Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations. Annu. Rev. Biochem., 73, 383-415.
85. John, R.A. (1995) Pyridoxal phosphate-dependent enzymes. Biochim. Biophys. Acta, 1248 (2), 81-96.
86. Yamada, T., Komoto, J., Takata, Y., Ogawa, H., Pitot, H.C., and Takusagawa, F. (2003)Crystal structure of serine dehydratase from rat liver. Biochemistry, 42 (44), 12854-12865.
87. Sun, L., Bartlam, M., Liu, Y., Pang, H., and Rao, Z. (2005)Crystal structure of the pyridoxal-50-phosphate-dependent serine dehydratase from human liver. Protein Sci., 14 (3), 791-798.
88. Okuda, H., Nagata, S., and Misono, H. (2002) Cloning, sequencing, and overexpression in Escherichia coli of a phenylserine dehydratase gene from Ralstonia pickettii PS22. Biosci. Biotechnol. Biochem., 66 (12), 2755-2758.
89. Ito, T., Takahashi, K., Naka, T., Hemmi, H., and Yoshimura, T. (2007) Enzymatic assay of D-serine using Dserine dehydratase from Saccharomyces cerevisiae. Anal. Biochem., 371 (2), 167-172.
90. Gallagher, D.T., Gilliland, G.L., Xiao, G., Zondlo, J., Fisher, K.E., Chinchilla, D., and Eisenstein, E. (1998) Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase. Structure, 6 (4), 465-475.
91. Simanshu, D.K., Savithri, H.S., and Murthy, M.R. (2006) Crystal structures of Salmonella typhimurium biodegradative threonine deaminase and its complex withCMPprovide structural insights into ligand-induced oligomerization and enzyme activation. J. Biol. Chem., (51), 39630-39641.
92. Wada, M., Matsumoto, T., Nakamori, S., Sakamoto, M., Kataoka, M., Liu, J.Q., Itoh, N., Yamada, H., and Shimizu, S. (1999) Purification and characterization of a novel enzyme, L-threo-3- hydroxyaspartate dehydratase, from Pseudomonas sp. T62. FEMS Microbiol. Lett., 179 (1), 147-151.
93. Murakami, T., Maeda, T., Yokota, A., and Wada, M. (2009) Gene cloning and expression of pyridoxal 5?-phosphatedependent L-threo-3-hydroxyaspartate dehydratase from Pseudomonas sp. T62, and characterization of the recombinant enzyme. J. Biochem., 145 (5), 661-668.
94. Wada, M., Nakamori, S., and Takagi, H. (2003) Serine racemase homologue of Saccharomyces cerevisiae has L-threo-3- hydroxyaspartate dehydratase activity. FEMS Microbiol. Lett., 225 (2), 189-193.
95. Khan, F., Jala, V.R., Rao, N.A., and Savithri, H.S. (2003) Characterization of recombinant diaminopropionate ammonia-lyase from Escherichia coli and Salmonella typhimurium. Biochem. Biophys. Res. Commun., 306 (4), 1083-1088.
96. Nagasawa, T., Tanizawa, K., Satoda, T., and Yamada, H. (1988) Diaminopropionate ammonia-lyase from Salmonella typhimurium. J. Biol. Chem., (2), 958-964.
97. Imanaga, Y. (1958) Metabolism of Dglucosamine. III. Enzymic degradation of D-glucosaminic acid. J. Biochem., (8), 647-650.
98. 2+ ion. Biosci. Biotechnol. Biochem., 59, 408-411.
99. Iwamoto, R. and Imanga, Y. (1982) Enzymatic microdetermination of Dglucosaminate with D-glucosaminate dehydratase. Anal. Lett., 15 (2), 161-169.
100. Grabowski, R., Hofmeister, A.E., and Buckel, W. (1993) Bacterial L-serine dehydratases: a new family of enzymes containing iron-sulfur clusters. Trends Biochem. Sci., 18 (8), 297-300.
101. Velayudhan, J., Jones, M.A., Barrow, P.A., and Kelly, D.J. (2004) L-serine catabolism via an oxygen-labile L-serine dehydratase is essential for colonization of the avian gut by Campylobacter jejuni. Infect. Immun., 72 (1), 260-268.
102. Laroche, M., Pukall, R., and Ulber, R. (2003) Recovery and characterization of a L-serine dehydratase from the marine bacterium Paracoccus seriniphilus for the construction of bioanalytical systems. Chem. Ing. Tech., 75, 146-149.
103. Takeuchi, M., Asano, N., Kameda, Y., and Matsui, K. (1985) Purification and properties of 3-ketovalidoxylamine A Cń lyase from Flavobacterium saccharophilum. J. Biochem., 98 (6), 1631-1638.
104. Zhang, J.F., Zheng, Y.G., and Shen, Y.C. (2010) Purification and characterization of 3-ketovalidoxylamine A Cń lyase produced by Stenotrophomonas maltrophilia. Appl. Biochem. Biotechnol., (4), 966-974.
105. Stöckigt, J., Barleben, L., Panjikar, S., and Loris, E.A. (2008) 3D-Structure and function of strictosidine synthase - the key enzyme of monoterpenoid indole alkaloid biosynthesis. Plant Physiol. Biochem., 46 (3), 340-355.
106. Loris, E.A., Panjikar, S., Ruppert, M., Barleben, L., Unger, M., Schübel, H., and Stöckigt, J. (2007) Structure-based engineering of strictosidine synthase: auxiliary for alkaloid libraries. Chem. Biol., 14 (9), 979-985.
107. Sagermann, M., Ohtaki, A., and Nikolakakis, K. (2009) Crystal structure of the EutL shell protein of the ethanolamine ammonia lyase microcompartment. Proc. Natl. Acad. Sci. U.S.A., 106 (22), 8883-8887.
108. Gani, D., Wallis, O.C., and Young, D.W. (1983) Stereochemistry of the rearrangement of 2-aminoethanol by ethanolamine ammonia-lyase. Eur. J. Biochem., 136 (2), 303-311.
109. Yamada, S., Nabe, K., Izuo, N., Nakamichi, K., and Chibata, I. (1981) Production of L-phenylalanine from trans-cinnamic acid with Rhodotorula glutinis containing L-phenylalanine ammonia-lyase activity. Appl. Environ. Microbiol., 42 (5), 773-778.