engleski

Scanning for genes encoding GDS(L) hydrolases in Actinobacteria from wide diversity of ecological niches

Due to their multifunctionality, GDS(L) hydrolases have great potential for application (e.g. in food, pharmaceutical and detergent industry). The member of this protein family often exhibits various catalytic activities like lipase, phospholipase, esterase and thioesterase and has broad substrate specificities, which makes them very interesting for biotechnology. However, finding new GDS(L) enzymes using BLAST is difficult due to their low sequence similarity. A novel HMM-based method (Inverse Posterior Probability Assignment - IPPA) was applied for GDS(L) motifs scanning. In addition, searching for novel members of GDS(L) family was accelerated using automated GDS(L) detection pipeline. We have shown that Actinobacteria from wide variety of ecological niches posses high number of genes encoding for GDS(L) enzymes. We have found 257 GDS(L) enzymes in 52 actinobacterial proteomes (up to 24 per proteome), majority coming from soil-inhabiting species. Clustering and phylogenetic analysis divided these enzymes into 8 well defined groups. Further, horizontal gene transfer had a significant impact on evolution of actinobacterial GDS(L) genes and it can be hypothesized that these enzymes facilitated adaptation to novel ecological niches, e.g. saprophytic lifestyle in soil. Moreover, we have found interesting variations in active site amino acids that possibly reflect novel enzyme properties of biotechnological interest.

GDS(L) family; Actinobacteria; motif scanning

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