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Glutathione S-transferase activities of S-Type and L-type thioltransferases from Arabidopsis thaliana

Authors
Cho, YWPark, EHLim, CJ
Issue Date
31-Mar-2000
Publisher
SPRINGER-VERLAG SINGAPORE PTE LTD
Keywords
Arabidopsis thaliana; glutaredoxin; glutathione S-transferase; thioltransferase
Citation
JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, v.33, no.2, pp.179 - 183
Journal Title
JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY
Volume
33
Number
2
Start Page
179
End Page
183
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/16775
ISSN
1225-8687
Abstract
The glutathione S-transferase (GST) activities of S-type and L-type thioltransferases (TTases), which are purified from the seeds and leaves of Arabidopsis thaliana, respectively, were identified and compared. The S-type and L-type TTases showed K-m, values of 9.72 mM and 3.18 mM on 1-chloro-2,4-dinitrobenzene (CDNB), respectively, indicating the L-type TTase has higher affinity for CDNB. The GST activity of the L-type TTase was rapidly inactivated after being heated at 70 degrees C or higher. The GST activity of the S-type TTase remains active in a range of 30-90 degrees C. Hg2+ inhibited the GST activity of the S-type TTase, whereas Ca2+ and Cd2+ inhibited the GST activity of the L-type TTase. Our results suggest that the GST activities of two TTases of Arabidopsis thaliana may have different catalytic mechanisms. The importance of the co-existence of TTase and GST activities in one protein remains to be elucidated.
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