engleski

Bioinformatics Approach to Characterisation of SGNH Hydrolase

The present analysis is aimed to recognize structural elements of SGNH/GDSL family of enzymes with a novel folding type using bioinformatics tools on data of primary and secondary structures. Out of 770 proteins sequences deposited, data of seven different structures of GDSL hydrolases are solved, only ; those of the best resolution were selected among twenty available in PDB (including mutants): rhamnogalacturonan acetyleserase from Aspergillus aculeatus, thioesterase I from E. coli, platelet-activating factor acetylhydrolase IBγ from Bos taurus, platelet-activating factor human acetylhydrolase IBβ , and esterase from Streptomyces scabies. Two novel enzymes of our interest, esterase from Pseudomonas aeruginosa and lipase from Streptomyces rimosus, were included in the analysis and compared with GDSL hydrolases of known three-dimensional structures. These two enzymes were recognized as the members of the SGNH/GDSL family with a fold being different from the common α / hydrolase fold. Alignment of amino acid sequences of SGNH/GDSL hydrolases studied reveals similarity about 20%. However, four blocks of conserved sequence, with one conserved residue in each block (S, G, N, H) are common characteristics.

Data Bases; Bioinformatics; Proteins; SGNH Hydrolases

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