TY - JOUR
AU - 
AB - THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 275, No. 7, Issue of February 18, pp. 4871–4879, 2000 © 2000 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in U.S.A. The Molecular Structure of Hyperthermostable Aromatic Aminotransferase with Novel Substrate Specificity from Pyrococcus horikoshii* (Received for publication, August 10, 1999, and in revised form, October 14, 1999) Ikuo Matsui‡§, Eriko Matsui‡, Yukihiro Sakai‡, Hisasi Kikuchi¶, Yutaka Kawarabayasi ¶, Hideaki Urai, Shin-ichi Kawaguchii, Seiki Kuramitsui, and Kazuaki Harata‡§ From the ‡National Institute of Bioscience and Human Technology, Tsukuba, Ibaraki 305, the ¶National Institute of Technology and Evaluation, Ministry of International Trade and Industry, Nishihara, Shibuyaku, Tokyo, and the iDepartment of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan Aromatic amino acid aminotransferase (ArATPh), includes the aspartate aminotransferases (AspATs), aromatic amino acid aminotransferases (ArATs), alanine ATs, and his- which has a melting temperature of 120 °C, is one of the most thermostable aminotransferases yet to be discov- tidinol phosphate aminotransferase. All members of Family I ered. The crystal structure of this aminotransferase efficiently utilize a-ketoglutarate as an amino donor and glu- from the hyperthermophilic archaeon Pyrococcus hori- tamate as an amino acceptor. Eleven residues are invariant koshii 
TI - The Molecular Structure of Hyperthermostable Aromatic Aminotransferase with Novel Substrate Specificity from Pyrococcus horikoshii
JF - Journal of Biological Chemistry
DO - 10.1074/jbc.275.7.4871
DA - 2000-02-01
UR - https://www.deepdyve.com/lp/unpaywall/the-molecular-structure-of-hyperthermostable-aromatic-aminotransferase-UPRmWu8psD
DP - DeepDyve
ER -