Naslov
Bioinformatic analysis of lipases from bacteria of genus Streptomyces

Autori
Leščić Ašler, Ivana

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
European Biomarkers Summit and Proteomics Europe / - Acton Sudbury, 2007

Skup
Proteomics Europe

Mjesto i datum
Amsterdam, Nizozemska, 04.09.2007. - 05.09.2007

Vrsta sudjelovanja
Poster

Vrsta recenzije
Nije recenziran

Ključne riječi
bioinformatics; lipases; Streptomyces

Sažetak
Lipases catalyse hydrolysis and synthesis of lipids, depending on the reaction conditions. The ability of stereospecific catalysis gives them biotechnological potential. Streptomycetes are Gram-positive soil bacteria that are known antibiotics producers. They also secrete various hydrolytic enzymes, but genes of only five lipases are known, with limited structural data. Therefore, bioinformatic analysis of protein sequences was performed. Streptomyces lipases were classified into three groups. Lipases from S. exfoliatus, S. coelicolor and S. albus G have high sequence homology. They are typical lipases containing Ser-His-Asp catalytic triad with Ser in the conserved GXSXG pentapeptide. They have two cysteines bound covalently. Unlike most other lipases, no lid is present that would cover the active site. In spite of structural similarity, they differ in hydrophobicity and stability. Lipase from S. cinnamomeus belongs to Pseudomonas family of bacterial lipases and probably possesses a lid. It is predicted to be stable. Lipase from S. rimosus belongs to family of GDSL-hydrolases. This enzyme has catalytic Ser in GDS(L) motif. Its three disulfide bridges probably contribute to thermal stability of this enzyme. Topology of secondary structure elements and active site residues differs significantly from classical lipases.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Biologija

POVEZANOST RADA