Ability of an enzyme to catalyse multiple metabolic reactions simultaneously
Enzyme promiscuity is the ability of an enzyme to catalyse a fortuitous 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 promiscuous 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.[1] An example of this is the atrazine chlorohydrolase (atzA encoded) from Pseudomonas sp. ADP that evolved from melamine deaminase (triA encoded), which has very small promiscuous activity toward atrazine, a man-made chemical.[2]
^Khersonsky O, Tawfik DS (2010). "Enzyme promiscuity: a mechanistic and evolutionary perspective". Annual Review of Biochemistry. 79: 471–505. doi:10.1146/annurev-biochem-030409-143718. PMID 20235827.
^Scott C, Jackson CJ, Coppin CW, Mourant RG, Hilton ME, Sutherland TD, Russell RJ, Oakeshott JG (April 2009). "Catalytic improvement and evolution of atrazine chlorohydrolase". Applied and Environmental Microbiology. 75 (7): 2184–91. Bibcode:2009ApEnM..75.2184S. doi:10.1128/AEM.02634-08. PMC 2663207. PMID 19201959.
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