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Lipase activity is common in staphylococci. Based on the blast of various known staphylococcal lipase DNA sequences, the degenerate primers were derived to amplify a 782-bp consensus lipase gene sequence of Staphylococcus hominis GIMT1.079, which encoded a deduced polypeptide of 260 amino acid (aa) residues. The alignment of aa sequence revealed that this 260-aa partial lipase of S. hominis shared high homology with those conserved parts of other 11 deduced staphylococcal lipases, in the range of the lowest 43.0% of S. epidermidis and the highest 63.5% of S. saprophyticus. Two aa residues, Ser39 and Asp230, were preliminarily confirmed in the putative catalytic triad as well as the 'P-loop' motif (-[AG]-x4-G-K-[ST]-) in this deduced 260-aa partial S. hominis lipase sequence.