Glutathione S- transferases and their function as a protein superfamily in plants
نویسندگان
چکیده مقاله:
Glutathione s transferase (GST) is one of the largest protein and multigene families present in all plant species and other living organisms. For these proteins, which are highly inducible to stress and internal and external stimuli, several functions in plants have been identified, including implication in secondary metabolism, growth and development, detoxification of herbicides, coping with environmental stresses such as drought, heat, and salinity through antioxidant activity. These enzymes lead to cell detoxification by binding glutathione to a variety of substrates such as endobiotics and xenobiotics. Most GSTs are cytoplasmic soluble enzymes, but mitochondrial and microsomal isoforms are also known in plants and animals. This article presents some of the most important recent findings on the evolution of GST, its frequency and structural features, with an emphasis on their role in plants. The latest applications of this family of proteins in environmental biotechnology will also be mentioned.
منابع مشابه
Glutathione S-transferases Null Genotype in Acute Myeloid Leukaemia
Background: The glutathione S-transferase (GST) family of metabolising enzymes plays an important role in the detoxification of mutagens and carcinogens. The expression of many of these cancer susceptibility enzymes is genetically polymorphic. An increased frequency of GST-null genotypes has been associated with several malignancies. Objective: To investigate the rate of GSTT1 and GSTM1 null ge...
متن کاملClass-Pi of Glutathione S-Transferases
Class-Pi of glutathione s-transferases (GST-Pi) is the specific form of GSTs that are known to participate particularly in the mechanisms of resistance to drugs and carcinogens. This class of the enzyme is referred to as class-P or class-Pi or class π. The accepted terminology in this review article is class-Pi. In this article following a brief description of identified molecular forms of GSTs...
متن کاملRat lung glutathione S - transferases
Two immunologically distinct types of 22000-Mr subunits are present in rat lung glutathione S-transferases. One of these subunits is probably similar to Ya subunits of rat liver glutathione S-transferases, whereas the other subunit Ya' is immunologically distinct. Glutathione S-transferase II (pI7.2) of rat lung is a heterodimer (YaYa') of these subunits, and glutathione S-transferase VI (pI4.8...
متن کاملHuman intestinal glutathione S - transferases
Cytosolic glutathione S-transferases were purified from the epithelial cells of human small and large intestine. These preparations were characterized with regard to specific activities, subunit and isoenzyme composition. Isoenzyme composition and specific activity showed little variation from proximal to distal small intestine. Specific activities of hepatic and intestinal enzymes from the sam...
متن کاملMouse Liver Glutathione S-Transferases
Three major forms of cytosolic glutathione S-transferase (designated F1, F2, and F3 transferases according to increasing isoelectric points) were purified to homogeneity from liver of DBA/2J mice, primarily by CM-cellulose and hydroxylapatite chromatography. The purified enzymes were shown to have specific activities of 104, 281, and 143 units/mg, respectively, when assayed with 1 m~ each of l-...
متن کاملAntioxidant properties and Glutathione S-transferases inhibitory activity of Alchornea cordifolia leaf extract in Acetaminophen toxicity
Paracetamol (acetaminophen, PCM) is a widely used over-the-counter analgesic and antipyretic drug. Intake of a large dose of PCM may result in severe hepatic necrosis. Oxidative stress is mediated by oxidative capacities of the PCM metabolite (N-acetyl-para-benzo quinoneimine, NAPQI), which covalently binds to proteins and other macromolecules to cause cellular damage. At low doses, NAPQI is ...
متن کاملمنابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ذخیره در منابع من قبلا به منابع من ذحیره شده{@ msg_add @}
عنوان ژورنال
دوره 0 شماره 1
صفحات 23- 36
تاریخ انتشار 2022-12
با دنبال کردن یک ژورنال هنگامی که شماره جدید این ژورنال منتشر می شود به شما از طریق ایمیل اطلاع داده می شود.
کلمات کلیدی برای این مقاله ارائه نشده است
میزبانی شده توسط پلتفرم ابری doprax.com
copyright © 2015-2023