Marine Biotechnology

, Volume 9, Issue 5, pp 513–542

Marine Glutathione S-Transferases

Authors

  • Brian Blanchette
    • Department of Chemistry and BiochemistryUniversity of Massachusetts Dartmouth
  • Xia Feng
    • Department of Chemistry and BiochemistryUniversity of Massachusetts Dartmouth
    • Department of Chemistry and BiochemistryUniversity of Massachusetts Dartmouth
Review

DOI: 10.1007/s10126-007-9034-0

Cite this article as:
Blanchette, B., Feng, X. & Singh, B.R. Mar Biotechnol (2007) 9: 513. doi:10.1007/s10126-007-9034-0

Abstract

The aquatic environment is generally affected by the presence of environmental xenobiotic compounds. One of the major xenobiotic detoxifying enzymes is glutathione S-transferase (GST), which belongs to a family of multifunctional enzymes involved in catalyzing nucleophilic attack of the sulfur atom of glutathione (γ-glutamyl-cysteinylglycine) to an electrophilic group on metabolic products or xenobiotic compounds. Because of the unique nature of the aquatic environment and the possible pollution therein, the biochemical evolution in terms of the nature of GSTs could by uniquely expressed. The full complement of GSTs has not been studied in marine organisms, as very few aquatic GSTs have been fully characterized. The focus of this article is to present an overview of the GST superfamily and their critical role in the survival of organisms in the marine environment, emphasizing the critical roles of GSTs in the detoxification of marine organisms and the unique characteristics of their GSTs compared to those from non-marine organisms.

Keywords

classificationglutathione S-transferasemarine organism phylogenic relationshipstructure

Copyright information

© Springer Science+Business Media, LLC 2007