The cloning and analysis of a partial lipase gene sequence of Staphylococcus hominis GIMT1.079
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.
QIAO Na-na GAO Qiang ZHAO Qin WANG De-pei Chen Yi-peng ZHAO Wen-yi YU Chang-yan
College of Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, P.R.China College of Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, P.R.China Ke College of Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, P.R.China Ti Key Laboratory of Industrial Microbiology, Ministry of Education, Tianjin 300457, P.R.China The Public health Administration Center of Xiqing District, Tianjin City, Tianjin 300380, P.R.China Tianjin Key Laboratory of Industrial Microbiology, Tianjin 300457, P.R.China
国际会议
成都
英文
1-3
2010-06-18（万方平台首次上网日期，不代表论文的发表时间）