@article{bastard2017parallel,

title = {Parallel evolution of non-homologous isofunctional enzymes in methionine biosynthesis},

author = {Karine Bastard and Alain Perret and Aline Mariage and Thomas Bessonnet and Agnès Pinet-Turpault and Jean-Louis Petit and Ekaterina Darii and Pascal Bazire and Carine Vergne-Vaxelaire and Clémence Brewee and Adrien Debard and Virginie Pellouin and Marielle Besnard-Gonnet and François Artiguenave and Claudine Médigue and David Vallenet and Antoine Danchin and Anne Zaparucha and Jean Weissenbach and Marcel Salanoubat and Véronique de Berardinis },

doi = {10.1038/nchembio.2397},

year  = {2017},

date = {2017-01-01},

journal = {Nature Chemical Biology},

volume = {13},

number = {8},

pages = {858},

publisher = {Nature Publishing Group},

abstract = {Experimental validation of enzyme function is crucial for genome interpretation, but it remains challenging because it cannot be scaled up to accommodate the constant accumulation of genome sequences. We tackled this issue for the MetA and MetX enzyme families, phylogenetically unrelated families of acyl-L-homoserine transferases involved in L-methionine biosynthesis. Members of these families are prone to incorrect annotation because MetX and MetA enzymes are assumed to always use acetyl-CoA and succinyl-CoA, respectively. We determined the enzymatic activities of 100 enzymes from diverse species, and interpreted the results by structural classification of active sites based on protein structure modeling. We predict that >60% of the 10,000 sequences from these families currently present in databases are incorrectly annotated, and suggest that acetyl-CoA was originally the sole substrate of these isofunctional enzymes, which evolved to use exclusively succinyl-CoA in the most recent bacteria. We also uncovered a divergent subgroup of MetX enzymes in fungi that participate only in L-cysteine biosynthesis as O-succinyl-L-serine transferases.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}