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Temperature Adaptation of Glutathione S-Transferase P1–1

Authors :
A.P. Mazzetti
Marzia Nuccetelli
Paolo Ascenzi
Giorgio Ricci
Mario Lo Bello
Giovanni Antonini
Giorgio Federici
Maria Rita Nicotra
Anna Maria Caccuri
Source :
Journal of Biological Chemistry. 274:19276-19280
Publication Year :
1999
Publisher :
Elsevier BV, 1999.

Abstract

Human glutathione S-transferase P1-1 (GST P1-1) is a homodimeric enzyme expressed in several organs as well as in the upper layers of epidermis, playing a role against carcinogenic and toxic compounds. A sophisticated mechanism of temperature adaptation has been developed by this enzyme. In fact, above 35 degrees C, glutathione (GSH) binding to GST P1-1 displays positive cooperativity, whereas negative cooperativity occurs below 25 degrees C. This binding mechanism minimizes changes of GSH affinity for GST P1-1 because of temperature fluctuation. This is a likely advantage for epithelial skin cells, which are naturally exposed to temperature variation and, incidentally, to carcinogenic compounds, always needing efficient detoxifying systems. As a whole, GST P1-1 represents the first enzyme which displays a temperature-dependent homotropic regulation of substrate (e.g. GSH) binding.

Details

ISSN :
00219258
Volume :
274
Database :
OpenAIRE
Journal :
Journal of Biological Chemistry
Accession number :
edsair.doi...........d8b93140a88495b9a14fdca2c4042298
Full Text :
https://doi.org/10.1074/jbc.274.27.19276