TY - JOUR
T1 - Structural insight into the active site of a Bombyx mori unclassified glutathione transferase
AU - Hossain, Tofazzal
AU - Yamamoto, Kohji
N1 - Publisher Copyright:
© 2015 Japan Society for Bioscience, Biotechnology, and Agrochemistry.
PY - 2015
Y1 - 2015
N2 - Glutathione transferases (GSTs) are major detoxification enzymes that play central roles in the defense against various environmental toxicants as well as oxidative stress. Here, we identify amino acid residues of an unclassified GST from Bombyx mori, bmGSTu-interacting glutathione (GSH). Site-directed mutagenesis of bmGSTu mutants indicated that amino acid residues Asp103, Ser162, and Ser166 contribute to catalytic activity.
AB - Glutathione transferases (GSTs) are major detoxification enzymes that play central roles in the defense against various environmental toxicants as well as oxidative stress. Here, we identify amino acid residues of an unclassified GST from Bombyx mori, bmGSTu-interacting glutathione (GSH). Site-directed mutagenesis of bmGSTu mutants indicated that amino acid residues Asp103, Ser162, and Ser166 contribute to catalytic activity.
UR - http://www.scopus.com/inward/record.url?scp=84940052523&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84940052523&partnerID=8YFLogxK
U2 - 10.1080/09168451.2014.1002450
DO - 10.1080/09168451.2014.1002450
M3 - Article
C2 - 25608724
AN - SCOPUS:84940052523
SN - 0916-8451
VL - 79
SP - 989
EP - 991
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
IS - 6
ER -