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 language | English |
|---|---|
| Pages (from-to) | 19276-19280 |
| Number of pages | 5 |
| Journal | Journal of Biological Chemistry |
| Volume | 274 |
| Issue number | 27 |
| DOIs | |
| Publication status | Published - Jul 2 1999 |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Temperature adaptation of glutathione S-transferase P1-1. A case for homotropic regulation of substrate binding. / Caccuri, Anna Maria; Antonini, Giovanni; Ascenzi, Paolo; Nicotra, Maria; Nuccetelli, Marzia; Mazzetti, Anna Paola; Federici, Giorgio; Lo Bello, Mario; Ricci, Giorgio.
In: Journal of Biological Chemistry, Vol. 274, No. 27, 02.07.1999, p. 19276-19280.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Temperature adaptation of glutathione S-transferase P1-1. A case for homotropic regulation of substrate binding
AU - Caccuri, Anna Maria
AU - Antonini, Giovanni
AU - Ascenzi, Paolo
AU - Nicotra, Maria
AU - Nuccetelli, Marzia
AU - Mazzetti, Anna Paola
AU - Federici, Giorgio
AU - Lo Bello, Mario
AU - Ricci, Giorgio
PY - 1999/7/2
Y1 - 1999/7/2
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0033516580&partnerID=8YFLogxK
U2 - 10.1074/jbc.274.27.19276
DO - 10.1074/jbc.274.27.19276
M3 - Article
C2 - 10383436
AN - SCOPUS:0033516580
VL - 274
SP - 19276
EP - 19280
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 27
ER -