Biochemical Characterization of Deblocking Aminopeptidase from Hyperthermophilic Archaeon Thermococcus onnurineus NA1(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

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A genomic analysis of the hyperthermophilic archaeon Thermoccoccus onnurineus NA1 (TNA1) revealed the presence of a deblocking aminopeptidase (DAP) gene with high similarity to the genes of DAPs from Pyrococcus furiosus (86%) and Pyrococcus horikoshii (83% identity). The optimum aminopeptidase activity of the recombinant enzyme was observed at pH 7.5 and in the range of 90℃ to 100℃. The specific aminopeptidase and deblocking activities of the enzyme toward Leu-pNA and Ac-Leu-pNA were 18- and 3-fold higher than those of a P horikoshii DAP (DAP2), respectively. The enzyme activity was significantly increased by Co^<2+>ions. The presence of Co^<2+>ions induced the activation of the enzyme with heating and changed the large oligomer to a dimer. The enzyme activated by Co^<2+>ions appeared to eventually be inactivated by autodegradation, which was confirmed by mass spectrometry.
社団法人日本生物工学会の論文
2007-09-25