A single amino acid substitution of Leu130Ile in snake DNases I contributes to the acquisition of thermal stability.
作者： Haruo Takeshita , Toshihiro Yasuda , Tamiko Nakajima , Kouichi Mogi , Yasushi Kaneko
DOI: 10.1046/J.1432-1033.2003.03387.X
关键词:
摘要: We purified pancreatic deoxyribonucleases I (DNases I) from three snakes, Elaphe quadrivirgata, climacophora and Agkistrodon blomhoffii, cloned their cDNAs. Each mature snake DNase I protein comprised 262 amino acids. Wild-type DNases I with Leu130 were more thermally unstable than wild-type mammalian avian Ile130. After substitution of Leu130Ile, the thermal stabilities enzymes higher those counterparts similar to enzyme levels. Conversely, substituting Ile130Leu made them counterparts. Therefore, a single acid substitution, might be involved in an evolutionally critical change vertebrate DNases I. Amphibian have Ser205 insertion Ca2+-binding site that reduces [Takeshita, H., Yasuda, T., Iida, R., Nakajima, Mori, S., Mogi, K., Kaneko, Y. & Kishi, K. (2001) Biochem. J.357, 473–480]. Thus, it is plausible stable vertebrates, such as mammals birds, been generated by Leu130Ile reptilian through molecular evolution following deletion amphibian enzymes. This mechanism may reflect one evolutionary changes cold-blooded warm-blooded vertebrates.
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