Structural highlights
FunctionPublication Abstract from PubMedSeveral members of C-C meta-cleavage product (MCP) hydrolases family demonstrate an unusual ability to hydrolyze esters as well as the MCPs (including those from mono- and bicyclic aromatics). While the molecular mechanisms responsible for such substrate promiscuity are starting to emerge the full understanding of these complex enzymes is far from complete. Herein, we describe six distinct alpha/beta hydrolases identified through genomic approaches, four of which demonstrate the unprecedented characteristic of activity towards a broad spectrum of substrates including p-nitrophenyl, halogenated, fatty acyl, aryl, glycerol, cinnamoyl and carbohydrate esters, lactones, 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate and 2-hydroxy-6-oxohepta-2,4-dienoate. Using structural analysis and site-directed mutagenesis we have identified the three residues (S32, V130 and W144) determining the unusual substrate specificity of one of these proteins, CCSP0084. The results may open up new research avenues into comparative catalytic models, structural and mechanistic studies, and biotechnological applications of MCP hydrolases. Single residues dictate the co-evolution of dual esterases - MCP hydrolases from the alpha/beta hydrolase family.,Alcaide M, Tornes J, Stogios PJ, Xu X, Gertler C, Di Leo R, Bargiela R, Lafraya A, Guazzaroni ME, Lopez-Cortes N, Chernikova TN, Golyshina OV, Nechitaylo TY, Plumeier I, Pieper DH, Yakimov MM, Savchenko A, Golyshin PN, Ferrer M Biochem J. 2013 Jun 10. PMID:23750508[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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