{"title":"The Cloning and Analysis of a Partial Lipase Gene Sequence of Staphylococcus hominis GIMT1.079: Partial Lipase Gene Sequencing of S. hominis","authors":"Na Qiao, Q. Gao, Q. Zhao, Depei Wang, Yi-peng Chen, Wenfan Zhao, Changyan Yu","doi":"10.1109/ICBBE.2010.5518078","DOIUrl":null,"url":null,"abstract":"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.","PeriodicalId":6396,"journal":{"name":"2010 4th International Conference on Bioinformatics and Biomedical Engineering","volume":"10 1","pages":"1-3"},"PeriodicalIF":0.0000,"publicationDate":"2010-06-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"2010 4th International Conference on Bioinformatics and Biomedical Engineering","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1109/ICBBE.2010.5518078","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 1
Abstract
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.
脂肪酶活性在葡萄球菌中很常见。基于已知的多种葡萄球菌脂肪酶DNA序列的blast，得到的简并引物扩增出了人型葡萄球菌GIMT1.079全长782 bp的脂肪酶基因序列，该序列编码260个氨基酸残基的推断多肽。aa序列比对表明，该260-aa部分脂肪酶与其他11种推断的葡萄球菌脂肪酶的保守部分同源性较高，在表皮葡萄球菌中同源性最低的43.0%和腐生葡萄球菌中同源性最高的63.5%之间。两个aa残基Ser39和Asp230在推测的催化三联体中得到了初步确认，在推断的260-aa部分人链球菌脂肪酶序列中也得到了“P-loop”基序(-[AG]-x4- g - k -[ST]-)的初步确认。
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