Scientific and Educational Reports of the Faculty
of Science and Technology, Kochi University
Vol. 2 (2019), No. 6
Yumeto Otsuk†1, Daichi Yano†2, Junko Tanaka1, Kouji Uda2, Tomohiko Suzuki2, Shigeru Sugiyama2*
1Graduate School of Science, Kochi University, Kochi 780-8520, Japan
2Faculty of Science & Technology, Kochi University, Kochi 780-8520, Japan
Abstract
The arginine kinase from the ciliate Paramecium tetraurelia catalyzes the reversible transfer of phosphoryl groups from adenosine triphosphate to arginine, generating adenosine diphosphate and arginine phosphate. The ciliate Paramecium tetraurelia has four arginine kinases (PtAK1 to 4). PtAK3 showed typical substrate inhibition toward arginine, and the enzymatic activity markedly decreased when the arginine concentration increased. To elucidate the substrate inhibition mechanism of PtAK3, we performed a crystallographic study of PtAK3. Here we report the crystallization and preliminary X-ray diffraction analysis of PtAK3. The diffraction data were collected and processed with a 2.6 Å resolution based on the PtAK3 crystals. The preliminary crystallographic analysis revealed that the PtAK3 crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 77.5, b = 162.5, c = 68.8 Å. They contained two molecules per asymmetric unit.
Received: May 5, 2019
Reviewed by anonymous referee(s), and accepted: May 31, 2019
Published: July 24, 2019
発行者：高知大学理工学部 〒780-8520 高知県高知市曙町二丁目5-1
Faculty of Science and Technology, Kochi University, Kochi, 780-8520 Japan
問い合わせ先（E-mail）：serfst●kochi-u.ac.jp （送信の際は"●"を半角"@"に変更して送信してください）