Temperature adaptation of glutathione S-transferase P1-1. A case for homotropic regulation of substrate binding

Anna Maria Caccuri, Giovanni Antonini, Paolo Ascenzi, Maria Nicotra, Marzia Nuccetelli, Anna Paola Mazzetti, Giorgio Federici, Mario Lo Bello, Giorgio Ricci

Research output: Contribution to journalArticle

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 °C, glutathione (GSH) binding to GST P1-1 displays positive cooperativity, whereas negative cooperativity occurs below 25 °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.

Original languageEnglish
Pages (from-to)19276-19280
Number of pages5
JournalJournal of Biological Chemistry
Volume274
Issue number27
DOIs
Publication statusPublished - Jul 2 1999

ASJC Scopus subject areas

  • Biochemistry

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    Caccuri, A. M., Antonini, G., Ascenzi, P., Nicotra, M., Nuccetelli, M., Mazzetti, A. P., Federici, G., Lo Bello, M., & Ricci, G. (1999). Temperature adaptation of glutathione S-transferase P1-1. A case for homotropic regulation of substrate binding. Journal of Biological Chemistry, 274(27), 19276-19280. https://doi.org/10.1074/jbc.274.27.19276