TY - JOUR
T1 - Investigation of the active site of an unclassified glutathione transferase in Bombyx mori by alanine scanning
AU - Yamamoto, Kohji
AU - Yamaguchi, Misuzu
AU - Yamada, Naotaka
N1 - Funding Information:
This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Culture, Sports, Science, and Technology of Japan (grant numbers JP15H04611 and 17K19272).
Publisher Copyright:
© 2020 Pesticide Science Society of Japan. All Rights Reserved.
PY - 2020
Y1 - 2020
N2 - Glutathione transferase (GST) is an important class of detoxification enzymes that are vital for defense against various xenobiotics and cellular oxidative stress. Previously, we had reported an unclassified glutathione transferase 2 in Bombyx mori (bmGSTu2) to be responsible for detoxifying diazinon. In this study, we aimed to identify the amino acid residues that constitute a hydrogen-bonding network important for GST activity. Site-directed mutagenesis of bmGSTu2 suggested that residues Asn102, Pro162, and Ser166 contribute to its catalytic activity.
AB - Glutathione transferase (GST) is an important class of detoxification enzymes that are vital for defense against various xenobiotics and cellular oxidative stress. Previously, we had reported an unclassified glutathione transferase 2 in Bombyx mori (bmGSTu2) to be responsible for detoxifying diazinon. In this study, we aimed to identify the amino acid residues that constitute a hydrogen-bonding network important for GST activity. Site-directed mutagenesis of bmGSTu2 suggested that residues Asn102, Pro162, and Ser166 contribute to its catalytic activity.
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U2 - 10.1584/JPESTICS.D20-036
DO - 10.1584/JPESTICS.D20-036
M3 - Article
AN - SCOPUS:85097735747
SN - 1348-589X
VL - 45
SP - 238
EP - 240
JO - Journal of Pesticide Sciences
JF - Journal of Pesticide Sciences
IS - 4
ER -