Expression and Characterization of Three New Glutathione Transferases, an Epsilon (AcGSTE2- 2), Omega (AcGSTO1- 1), and Theta (AcGSTT1- 1) From Anopheles cracens (Diptera: Culicidae), a Major Thai Malaria Vector

2010 ◽  
Vol 47 (2) ◽  
pp. 162-171 ◽  
Author(s):  
Jeerang Wongtrakul ◽  
Saengtong Pongjaroenkit ◽  
Posri Leelapat ◽  
Woottichai Nachaiwieng ◽  
La-Aied Prapanthadara ◽  
...  
Keyword(s):  
Malaria Vector ◽  
Glutathione Transferases ◽  
Anopheles Cracens

scholarly journals Expression and Characterization of Three New Glutathione Transferases, an Epsilon (AcGSTE2- 2), Omega (AcGSTO1- 1), and Theta (AcGSTT1- 1) FromAnopheles cracens(Diptera: Culicidae), a Major Thai Malaria Vector

2010 ◽  
Vol 47 (2) ◽  
pp. 162-171 ◽  
Author(s):  
Jeerang Wongtrakul ◽  
Saengtong Pongjaroenkit ◽  
Posri Leelapat ◽  
Woottichai Nachaiwieng ◽  
La-Aied Prapanthadara ◽  
...  
Keyword(s):  
Malaria Vector ◽  
Glutathione Transferases

Characterization of the Major Glutathione Transferases in Carp Liver

1999 ◽  
Vol 284 (2) ◽  
pp. 130-136 ◽  
Author(s):  
Antonia Concetta Elia ◽  
Luciana Mantilacci ◽  
Maria Illuminata Taticchi ◽  
Giovanni Principato
Keyword(s):  
Glutathione Transferases

scholarly journals Novel class of glutathione transferases from cyanobacteria exhibit high catalytic activities towards naturally occurring isothiocyanates

2007 ◽  
Vol 406 (1) ◽  
pp. 115-123 ◽  
Author(s):  
Eric Wiktelius ◽  
Gun Stenberg
Keyword(s):  
Catalytic Properties ◽  
Structural Features ◽  
Glutathione Transferases ◽  
Substrate Specificities ◽  
Catalytic Activities ◽  
Genome Databases ◽  
Naturally Occurring ◽  
Physiological Relevance ◽  
Associated Proteins

In the present paper, we report a novel class of GSTs (glutathione transferases), called the Chi class, originating from cyanobacteria and with properties not observed previously in prokaryotic enzymes. GSTs constitute a widespread multifunctional group of proteins, of which mammalian enzymes are the best characterized. Although GSTs have their origin in prokaryotes, few bacterial representatives have been characterized in detail, and the catalytic activities and substrate specificities observed have generally been very modest. The few well-studied bacterial GSTs have largely unknown physiological functions. Genome databases reveal that cyanobacteria have an extensive arsenal of glutathione-associated proteins. We have studied two cyanobacterial GSTs which are the first examples of bacterial enzymes that are as catalytically efficient as the best mammalian enzymes. GSTs from the thermophile Thermosynechococcus elongatus BP-1 and from Synechococcus elongatus PCC 6301 were found to catalyse the conjugation of naturally occurring plant-derived isothiocyanates to glutathione at high rates. The cyanobacterial GSTs studied are smaller than previously described members of this enzyme family, but display many of the typical structural features that are characteristics of GSTs. They are also active towards several classical substrates, but at the same moderate rates that have been observed for other GSTs derived from prokaryotes. The cloning, expression and characterization of two cyanobacterial GSTs are described. The possible significance of the observed catalytic properties is discussed in the context of physiological relevance and GST evolution.

scholarly journals New members of the glutathione transferase family discovered in red and brown algae

2008 ◽  
Vol 412 (3) ◽  
pp. 535-544 ◽  
Author(s):  
Cécile Hervé ◽  
Pierre-Olivier de Franco ◽  
Agnès Groisillier ◽  
Thierry Tonon ◽  
Catherine Boyen
Keyword(s):  
Glutathione Transferase ◽  
Biochemical Characterization ◽  
Glutathione Transferases ◽  
New Members ◽  
Efficient Inhibitor ◽  
Chemical Treatments ◽  
Organic Hydroperoxides ◽  
The Common ◽  
Derivatives Of

The GSTs (glutathione transferases) are involved in the detoxification of a wide variety of hydrophobic substrates. These enzymes have been found in virtually all types of organisms, including plants, animals, nematodes and bacteria. In the present study, we report the molecular and biochemical characterization of algal GSTs. Phylogenetic analysis showed that most of them were distinct from previously described GST classes, but were most closely related to the Sigma class. Profiling of GST genes from the red alga Chondrus crispus and brown alga Laminaria digitata was undertaken after different chemical treatments and showed that they displayed contrasting patterns of transcription. Recombinant algal GST from both species showed transferase activities against the common substrates aryl halides, but also on the α,β-unsaturated carbonyl 4-hydroxynonenal. Also, they exhibit significant peroxidation towards organic hydroperoxides, including oxygenated derivatives of polyunsaturated fatty acids. Among a range of compounds tested, Cibacron Blue was the most efficient inhibitor of algal GSTs identified.

scholarly journals Characterization of rat glutathione transferases in olfactory epithelium and mucus

PLoS ONE ◽  
2019 ◽  
Vol 14 (7) ◽  
pp. e0220259 ◽  
Author(s):  
Jean-Marie Heydel ◽  
Franck Menetrier ◽  
Christine Belloir ◽  
Francis Canon ◽  
Philippe Faure ◽  
...  
Keyword(s):  
Olfactory Epithelium ◽  
Glutathione Transferases

Characterization of multiple glutathione transferases from the house fly, Musca domestica (L)

1984 ◽  
Vol 22 (1) ◽  
pp. 51-59 ◽  
Author(s):  
Alan G. Clark ◽  
N.A. Shamaan ◽  
Walter C. Dauterman ◽  
Tatsumi Hayaoka
Keyword(s):  
Musca Domestica ◽  
House Fly ◽  
Glutathione Transferases
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