Abstract
We discuss the basic features of divergent versus convergent evolution and of the common scenario of parallel evolution. The example of quorum-quenching lactonases is subsequently described. Three different quorum-quenching lactonase families are known, and they belong to three different superfamilies. Their key active-site architectures have converged and are strikingly similar. Curiously, a promiscuous organophosphate hydrolase activity is observed in all three families. We describe the structural and mechanistic features that underline this converged promiscuity and how this promiscuity drove the parallel divergence of organophosphate hydrolases within these lactonase families by either natural or laboratory evolution.
Highlights
Darwin’s theory of evolution is associated mostly with the idea of natural selection, as manifested in the title of his book, On the Origins of Species by Means of Natural Selection
The ultimate goal is a detailed description of the tree of life, starting from the earliest life forms to the last universal common ancestor (LUCA)3 that appeared over 3.5 billion years ago and subsequently to all extant species
Small [4], the LUCA protein set presumably included the progenitors of the major protein superfamilies that are presently seen in all three kingdoms (Refs. 5–7 and references therein)
Summary
Darwin’s theory of evolution is associated mostly with the idea of natural selection, as manifested in the title of his book, On the Origins of Species by Means of Natural Selection. QQLs exhibit different specificities with respect to short or long N-acyl chains and/or for the presence of a 3-oxo group, but some of these enzymes hydrolyze lactones other than HSLs. As exemplified below, lactonase families appear to have diverged such that some members specialize in hydrolyzing HSLs, whereas other members hydrolyze other lactones (either ␥-lactones, as are HSLs, or ␦-lactones). The second known QQL family is named phosphotriesterase-like lactonases (PLLs) It belongs to the amidohydrolase superfamily, a highly diverse superfamily that, as is the case with the metallo--lactamase superfamily, includes many different hydrolytic and other activities [37]. Asp-256 in SsoPox adopts a very similar position to Asp-108 in AiiA, suggesting that this Asp plays a similar role in catalysis in both lactonase families
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