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Reference.org
Enzyme promiscuity
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<p>Enzyme promiscuity is the ability of an <a href="/facts/Enzyme/DSI1Fh7y">enzyme</a> to catalyze an unexpected side reaction in addition to its main reaction. Although enzymes are remarkably specific catalysts, they can often perform side reactions in addition to their main, native catalytic activity. These wild activities are usually slow relative to the main activity and are under neutral selection. Despite ordinarily being physiologically irrelevant, under new selective pressures, these activities may confer a fitness benefit therefore prompting the evolution of the formerly promiscuous activity to become the new main activity. An example of this is the <a href="/facts/Atrazine/cPx70RaK">atrazine</a> chlorohydrolase (<i>atzA</i> encoded) from <i><a href="/facts/Pseudomonas_sp./FKEX7p7K">Pseudomonas sp.</a></i> ADP evolved from <a href="/facts/Melamine/wvvc4rrz">melamine</a> <a href="/facts/Deaminase/aBIhMC23">deaminase</a> (<i>triA</i> encoded), which has very small promiscuous activity toward atrazine, a man-made chemical. </p>