prvi kongres hrvatskih znanstvenika iz domovine i inozemstva - HATZ

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PRVI KONGRES HRVATSKIH ZNANSTVENIKA IZ DOMOVINE I INOZEMSTVAZagreb - Vukovar, 15. - 19. studenog 2004.2
PRVI KONGRES HRVATSKIH ZNANSTVENIKA IZ DOMOVINE I INOZEMSTVAZagreb - Vukovar, 15. - 19. studenog 2004.P - 1PROKARYOTIC HOMOLOGS HELP TO DEFINE CONSENSUSSEQUENCES IN METALLOPEPTIDASE FAMILY M49Abramić Marija, Špoljarić Jasminka, Šimaga ŠumskiRudjer Bošković Institute, Zagreb, CroatiaIn recent years the number of deduced amino acid sequences of metallopeptidases hasincreased dramatically revealing that these enzymes are the most diverse of the fourmain catalytic types of peptidases, with 51 families identified to date.Peptidase family M49 (dipeptidyl peptidase III family) has been recogn<strong>iz</strong>ed as a distinctgroup of metallopeptidases based on the significant similarity in primary structures of itsmembers and the unique structural motif, hexapeptide HELLGH, which harbors thepredicted active site residues.Dipeptidyl peptidase III (DPP III) was previously biochemically character<strong>iz</strong>ed as acytosolic zinc-exopeptidase involved in the final steps of intracellular protein catabolism ofeukaryotes.The regulatory role of DPP III in the metabolism of biologically active peptides(angiotensins and enkephalins) has been suggested. However, 3-D structure,physiological significance, regulation and distribution of this enzyme in the living world stillneed to be elucidated. Our results indicated that enhanced expression of DPP III mightbe used as biochemical marker for endometrial and ovarian cancer.We assumed that the new data of genomes sequencing also contain unknown membersof this family and we attempted to define its evolutionary conserved amino acid sequenceregions through the analysis of their primary structures.By the similarity search and additional manual stringency we have revealed 14homologous protein sequences (members of family M49), two of them prokaryotic,whose multiple alignment gave five highly conserved regions. Two conserved linearmotifs (consensus sequences) harboring four known active site residues of family M49were defined as stretches of 16 and 6 amino acids located in the third and fourthconserved region. A part of sixteen-amino acid consensus sequence and the completeconsensus sequence of six amino acid were predicted to reside in a α-helix.In conclusion, the most recent data on complete genome sequences helped us to revealthat metallopeptidase family M49 (DPP III family) is distributed in four kingdoms oforganisms (Eubacteria, Protista, Fungi and Animalia), and to define two consensussequences containing the active site residues. Bacterial homologs have been unexpectedand so far confined to the proteins from one human symbiont and one oral pathogen.Presented on:2 nd Central European Conference Chemistry towards Biology,Seggau, Austria, 26-29 September 2004.Principal Investigator : Dr.sc. Marija AbramićProject No. 00980553
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prvi kongres hrvatskih znanstvenika iz domovine i inozemstva - HATZ

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