TAILIEUCHUNG - Báo cáo khoa học: New members of the brachyurins family in lobster include a trypsin-like enzyme with amino acid substitutions in the substrate-binding pocket

Crustacean serine proteases (Brachyurins, EC ) exhibit a wide variety of primary specificities and no member of this family has been reported for spiny lobsters. The aim of this work was to study the diversity of trypsins in the digestive gland ofPanulirus argus. | ỊFEBS Journal New members of the brachyurins family in lobster include a trypsin-like enzyme with amino acid substitutions in the substrate-binding pocket Erick Perera1 Tirso Pons2 Damir Hernandez1 Francisco J. Moyano3 Gonzalo Martinez-Rodriguez4 and Juan M. Mancera5 1 Center for Marine Research University of Havana Cuba 2 ComputationalBiology Center for Protein Studies Faculty of Biology University of Havana Cuba 3 Department of Applied Biology University of Almeria Spain 4 ICMAN CSIC Cadiz Spain 5 Department of Biology University of Cadiz Spain Keywords brachyurins comparative modelling Panulirus substrate-binding pocket trypsin Correspondence E. Perera Center for Marine Research University of Havana Calle 16 No. 114 e 1ray3ra Miramar Playa CP 11300 Habana Cuba Fax 53 7 2042380 Tel 53 7 2030617 E-mail erickpb@ Database The nucleotide sequence data for PaTry1a PaTry1b PaTry2 PaTry3 and PaTry4 are available in the GenBank database under the accession numbers GU338026 GU338027 GU338028 GU338029 and GU338030 respectively. The model data for PaTry1a PaTry1b PaTry2 PaTry3 and PaTry4 are available in the PMDB database under the accession numbers PM0076235 PM0076234 PM0076233 PM0076232 and PM0076231 respectively Received 16 March 2010 revised 29 May 2010 accepted 28 June 2010 doi Crustacean serine proteases Brachyurins EC exhibit a wide variety of primary specificities and no member of this family has been reported for spiny lobsters. The aim of this work was to study the diversity of trypsins in the digestive gland of Panulirus argus. Several trypsin-like proteases were cloned and the results suggest that at least three gene families encode trypsins in the lobster. Three-dimensional comparative models of each trypsin anticipated differences in the interaction of these enzymes with proteinaceous substrates and inhibitors. Most of the studied enzymes were typical trypsins but one could not be allocated to any of the .

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