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Bioinformatic analysis of lipases from bacteria of genus Streptomyces (CROSBI ID 530979)

Prilog sa skupa u zborniku | sažetak izlaganja sa skupa

Leščić Ašler, Ivana Bioinformatic analysis of lipases from bacteria of genus Streptomyces // European Biomarkers Summit and Proteomics Europe / - (ur.). Acton Sudbury, 2007. str. --x

Podaci o odgovornosti

Leščić Ašler, Ivana

engleski

Bioinformatic analysis of lipases from bacteria of genus Streptomyces

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.

bioinformatics; lipases; Streptomyces

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Podaci o prilogu

--x.

2007.

objavljeno

Podaci o matičnoj publikaciji

European Biomarkers Summit and Proteomics Europe

-

Acton Sudbury:

Podaci o skupu

Proteomics Europe

poster

04.09.2007-05.09.2007

Amsterdam, Nizozemska

Povezanost rada

Kemija, Biologija