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In-Silico Analysis of Proteins

Celebrating the 20th anniversary of Swiss-Prot

July 30 - August 04, 2006 : Fortaleza, Brazil

Poster #RP205

Heterogeneity Analysis of the Aminoacid Sequences from the Glycolytic Enzymes and Building of Hexokinase Phylogenetic Tree

Renato Milani*, Eduardo Galembeck*

*Unicamp, Campinas, Brazil

The methods from molecular phylogenetic analysis of biological sequences were applied here in order to determine the heterogeneity of the glycolytic enzymes sequences, towards a better understanding of their phylogenetic relationships. A MySQL database was built with information pertaining all the enzymes from glycolysis in KEGG, ExPASy, MetaCyc and PUMA2. As a first step, FASTA files for each enzyme were generated including every sequence present in KEGG related to the ten glycolytic enzymes. After alignment with CLUSTALW, the results show the most divergence (93,3%) among fructose-bisphosphate aldolase sequences (EC 4.1.2.13) while 53,4% were found among hexokinase sequences (EC 2.7.1.1). A phylogenetic tree was built for the 44 sequences retrieved from hexokinase by the Neighbor-Joining method, showing a taxonomic clustering through the major taxa (Animalia, Plantae, Fungi, Protozoa and Bacteria). However, four separate groups formed under Protozoa and two under Fungi. These results might be due to the high rate of heterogeneity found in the sequences, reflecting the wide diversity of the organisms selected. Further analysis for all the glycolytic enzymes is needed to a better understanding of the evolutionary relationships involving these proteins.