MIO-Enzymes Used to Make α-Amino Acids from Cinnamates
Listed Chronologically from Earliest to Latest
Chibata, I.; Yamada, S.; Nabe, K.; Ujimaru, T.; Izumio, N. Enzymic production of L-phenylalanine. JP53096388A, 1978.
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.
Kishore, G. M. Stabilization of D-phenylalanine ammonia-lyase enzyme. EP136996A2, 1985.
Kitsukawa, T.; Kusano, H.; Miyata, E.; Sugawara, T. Separation and recovery of phenylalanine and cinnamic acid from solutions. DE3506958A1, 1985.
Schruber, J. J.; Vollmer, P. J.; Montgomery, J. P. Production and recovery of L-phenylalanine. EP140713A2, 1985.
Swann, W. E. L-Phenylalanine production by reutilizing phenylalanine ammonia lyase. BE901938A4, 1985.
Vollmer, P. J.; Montgomery, J. P.; Schruber, J. J.; Yang, H. H. Stabilizing the enzymic activity of phenylalanine ammonia-lyase during L-phenylalanine production. EP143560A2, 1985.
Yokozeki, K.; Onishi, N.; Kano, H.; Hirose, Y. L-Phenylalanine and microorganisms for its production. EP152235A2, 1985.
Fukuhara, N.; Yamamoto, K.; Iwata, T. L-Phenylalanine from cinnamic acid by microbial enzyme. JP61247395A, 1986.
Kamata, A.; Mikawa, T.; Imada, Y. Microbiological preparation of L-phenylalanine. EP167411A2, 1986.
Kamata, A.; Shibui, T.; Mikawa, T.; Imada, Y. L-Phenylalanine from cinnamic acid by microbial ammonia-lyase. JP61192295A, 1986.
Swann, W. E.; Nolf, C. A. Immobilizing a biological material. EP197784A1, 1986.
Yokozeki, K.; Onishi, I.; Kano, H.; Hirose, Y. L-Phenylalanine production. JP61170398A, 1986.
Evans, C. T.; Choma, C.; Peterson, W.; Misawa, M., Bioconversion of trans-cinnamic acid to L-phenylalanine in an immobilized whole cell reactor. Biotechnol. Bioeng. 1987, 30, 1067-1072.
Evans, C. T.; Hanna, K.; Payne, C.; Conrad, D.; Misawa, M., Biotransformation of trans-cinnamic acid to L-phenylalanine: optimization of reaction conditions using whole yeast cells. Enzyme Microb. Technol. 1987, 9, 417-421.
Yokozeki, K.; Onishi, I.; Yugawa, T.; Hirose, Y. Microbial production of L-phenylalanine. JP62003793A, 1987.
Evans, D. L.; Thimmig, R. L.; Koltz, R. C. Process for recovery and purification of L-phenylalanine from reaction mixtures containing L-phenylalanine and contaminants. US4731469A, 1988.
Renard, G.; Guilleux, J. C.; Bore, C.; Malta-Valette, V.; Lerner, D. A., Synthesis of L-phenylalanine analogs by Rhodotorula glutinis. Bioconversion of cinnamic acids derivatives. Biotechnol. Lett. 1992, 14, 673-678.
Takac, S.; Akay, B.; Oezdamar, T. H., Bioconversion of trans-cinnamic acid to L-phenylalanine by L-phenylalanine ammonia-lyase of Rhodotorula glutinis: parameters and kinetics. Enzyme Microb. Technol. 1995, 17, 445-452.
Jemielity, J.; Kańska, M.; Kański, R., Enzymatic Synthesis of [1-13C]- and [1-14C]-L-Phenyl-Alanine. Isot. Environ. Health Stud. 1998, 34, 335-339.
Gloge, A.; Zon, J.; Kovari, A.; 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.
Augustyniak, W.; Bukowski, J.; Jemielity, J.; Kanski, R.; Kanska, M., Enzymatic syntheses of carbon-14 labeled isotopomers of L-phenylalanine. J. Radioanal. Nucl. Chem. 2001, 247, 371-374.
El-Batal, A. I., Continuous production of L-phenylalanine by Rhodotorula glutinis immobilized cells using a column reactor. Acta Microbiol. Pol. 2002, 51, 153-169.
El-Batal, A. I., 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. 2002, 51, 139-152.
Aoki, H.; Kamachi, H. Method for producing L-amino acids. WO2003000915A1, 2003.
Cui, J.-d.; Jia, S.-r.; Tan, Z.-l., Enhancing conversion ratio of trans-cinnamic acids by improving the permeability of recombinant Escherichia coli. Gaoxiao Huaxue Gongcheng Xuebao 2008, 22, 1015-1019.
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.
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.
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.
Li, M.; Yang, Y.; Yang, S., Optimal conditions for bio-production of L-phenylalanine by immobilized cells of Rhodotolula glutinis. Chin. J. Appl. Environ. Biol. 2010, 16, 279-284.
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.
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.
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.
Onishi, N.; Yokozeki, K.; Hirose, Y.; Kubota, K., Enzymic production of L-phenylalanine from trans-cinnamic acid by Endomyces lindneri. Agric. Biol. Chem. 2014, 51, 291-292.
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.
Tao, R.; Wang, B.; Yang, S.; Wang, Y.; Zhu, F.; Sun, L.; Shen, Q.; Xu, M.; Pan, Z. Histidine ammonia lyase of Pseudoalteromonas sp. p1-26 for catalytic synthesis of L-phenylalanine compounds from cinnamic acids. CN106755160A, 2017.
