@article {Giuseppe:2012:0929-8665:144,
title = "Enzyme Promiscuity in the Hormone-sensitive Lipase Family of Proteins",
journal = "Protein and Peptide Letters",
parent_itemid = "infobike://ben/ppl",
publishercode ="ben",
year = "2012",
volume = "19",
number = "2",
publication date ="2012-02-01T00:00:00",
pages = "144-154",
itemtype = "ARTICLE",
issn = "0929-8665",
url = "https://www.ingentaconnect.com/content/ben/ppl/2012/00000019/00000002/art00003",
keyword = "detoxification, Promiscuity, hormone-sensitive lipase family, ligands, substrate, conformations, biotechnological, α/β hydrolase fold, carboxylesterases, cytochrome P450s",
author = "Giuseppe, Manco and Luigia, Merone and Elena, Porzio and Yan, Feng and Luigi, Mandrich",
abstract = "The number of enzymes endowed with the capacity to catalyse other reactions than the main, physiological one, a feature that has been called promiscuity, is increasing at a fast pace. Promiscuity is a highly pervasive phenomenon that is present at each level of life complexity. For
enzymes, promiscuity encompasses interesting aspects related to their physiological role, evolution and biotechnological applications. Herein, at first we will describe some general aspects of enzyme promiscuity and then we will report some examples from the / hydrolase superfamily
of proteins, with particular emphasis to the hormone-sensitive lipase family. 
",
}