TAILIEUCHUNG - Báo cáo khoa học: A new phospholipase A2 isolated from the sea anemone Urticina crassicornis – its primary structure and phylogenetic classification

Disulfide pairings and active site residues are highly conserved in secretory phospholipases A2 (PLA2s). However, secretory PLA2 s of marine inverte-brates display some distinctive structural features. In this study, we report the isolation and characterization of a PLA2 from the northern Pacific sea anemone,Urticina crassicornis(UcPLA2), containing a C27N substitution and a truncated C-terminal Tom Turk1 1 2 3 4 Biotechnical Faculty, Department of Biology, University of Ljubljana, Slovenia ˇ Department of Molecular and Biomedical Sciences, Jozef Stefan Institute, Ljubljana, Slovenia Faculty of Veterinary Medicine, University of Ljubljana, Slovenia Department of Pharmacology and Therapeutics, College of Medicine, University of Florida, Gainesville, FL, USA Keywords enzymatic activity; phospholipase. | ỊFEBS Journal A new phospholipase A2 isolated from the sea anemone Urticina crassicornis - its primary structure and phylogenetic classification . i ll 2 2 2 v3 Andrej Razpotnik Igor Krizaj Jernej Sribar Dusan Kordis Peter Macek Robert Frangez William R. Kem4 and Tom Turk1 1 BiotechnicalFaculty Department of Biology University of Ljubljana Slovenia 2 Department of Molecular and BiomedicalSciences Jozef Stefan Institute Ljubljana Slovenia 3 Faculty of Veterinary Medicine University of Ljubljana Slovenia 4 Department of Pharmacology and Therapeutics College of Medicine University of Florida Gainesville FL USA Keywords enzymatic activity phospholipase A2 phylogenetic classification sea anemone sequence venom Correspondence T. Turk BiotechnicalFaculty Department of Biology University of Ljubljana Vecna pot 111 SI-1000 Ljubljana Slovenia Fax 386 1 257 33 90 Tel 386 1 423 33 88 E-mail Database The nucleotide sequence described in this article has been submitted to EMBL GeriBarik DDBJ under the accession number EU003992 Received 26 February 2010 revised 7 April 2010 accepted 8 April 2010 Disulfide pairings and active site residues are highly conserved in secretory phospholipases A2 PLA2s . However secretory PLA2s of marine invertebrates display some distinctive structural features. In this study we report the isolation and characterization of a PLA2 from the northern Pacific sea anemone Urticina crassicornis UcPLA2 containing a C27N substitution and a truncated C-terminal sequence. This novel cnidarian PLA2 shares about 60 identity and almost 70 homology with two putative PLA2s identified in the starlet sea anemone Nematostella vectensis genome project. UcPLA2 lacks hemolytic and neurotoxic activities. A search of available sequences revealed that Asn27- type PLA2s are present in a few other marine animal species including some vertebrates. The possibility that the C27N replacement represents a structural adaptation for PLA2 digestion activity in the

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