Abstract
ALTHOUGH a number of reports have been published on α-amino acylase, little is known about ɛ-lysine acylase, which hydrolyses ɛ-N-acyllysine. Paik et al.1 first confirmed the activity in rat tissues, and Kameda et al.2 and Wada3 reported the activity in a microorganism of Pseudomonas. The activities of the enzymes in these reports were very low and the enzymes were not obtained as a pure protein.
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References
Paik, W. K., Bloch-Frankenthal, L., Birnbaum, S. M., Winitz, M., and Greenstein, J. P., Arch. Biochem. Biophys., 69, 56 (1957).
Kameda, Y., Toyoura, E., Kimura, Y., and Matsui, K., Chem. Pharm. Bull. Jap., 6, 394 (1958).
Wada, S., J. Biochem. Jap., 46, 445, 1541 (1959).
Chibata, I., Ishikawa, T., and Tosa, T., Bull. Agric. Chem. Soc. Jap., 24, 31 (1960).
Chibata, I., Ishikawa, T., and Tosa, T., Bull. Agric. Chem. Soc. Jap., 24, 37 (1960).
Chiba, H., Sugimoto, E., and Kito, M., Bull. Agric. Chem. Soc. Jap., 24, 428 (1960).
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CHIBATA, I., ISHIKAWA, T. & TOSA, T. ɛ-Lysine Acylase in Bacteria. Nature 195, 80–81 (1962). https://doi.org/10.1038/195080a0
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DOI: https://doi.org/10.1038/195080a0
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