DocumentCode
2830818
Title
Notice of Retraction
Cloning and homologous analysis of a partial lipase gene in Staphylococcus caprae TCCC 11546: Partial lipase gene sequencing of S. caprae
Author
Chen Yi-peng ; Gao Qiang ; Qiao Na-na ; Wang De-pei ; Wang Bin-zhe ; Zhao Wen-yi
Author_Institution
Coll. of Biotechnol., Tianjin Univ. of Sci. & Technol., Tianjin, China
Volume
3
fYear
2010
fDate
21-24 May 2010
Abstract
Notice of Retraction
After careful and considered review of the content of this paper by a duly constituted expert committee, this paper has been found to be in violation of IEEE´s Publication Principles.
We hereby retract the content of this paper. Reasonable effort should be made to remove all past references to this paper.
The presenting author of this paper has the option to appeal this decision by contacting TPII@ieee.org.
Lipase activity is popular in staphylococci. We described here that a 781-bp consensus lipase gene sequence of Staphylococcus caprae TCCC 11546, which encoded a deduced polypeptide of 260 amino acid residues, was cloned using the degenerate primers. The amino acid sequence alignment and the phylogenetic tree revealed that this 260-amino acid partial lipase of S. caprae was highly homologous from 55.0% to 98.8% among other 11 conserved lipase stretches from other 11 Staphylococcus species. Moreover, two amino acid residues, Ser39 and Asp230, were identified in the putative lipase catalytic triad, the consensus `P-loop´ motif (-[AG]-x4-G-K-[ST]-) was also found in this partial lipase stretch.
After careful and considered review of the content of this paper by a duly constituted expert committee, this paper has been found to be in violation of IEEE´s Publication Principles.
We hereby retract the content of this paper. Reasonable effort should be made to remove all past references to this paper.
The presenting author of this paper has the option to appeal this decision by contacting TPII@ieee.org.
Lipase activity is popular in staphylococci. We described here that a 781-bp consensus lipase gene sequence of Staphylococcus caprae TCCC 11546, which encoded a deduced polypeptide of 260 amino acid residues, was cloned using the degenerate primers. The amino acid sequence alignment and the phylogenetic tree revealed that this 260-amino acid partial lipase of S. caprae was highly homologous from 55.0% to 98.8% among other 11 conserved lipase stretches from other 11 Staphylococcus species. Moreover, two amino acid residues, Ser39 and Asp230, were identified in the putative lipase catalytic triad, the consensus `P-loop´ motif (-[AG]-x4-G-K-[ST]-) was also found in this partial lipase stretch.
Keywords
biochemistry; cellular biophysics; enzymes; genetics; genomics; microorganisms; proteomics; P-loop motif; Staphylococcus caprae TCCC 11546; amino acid residues; amino acid sequence alignment; cloning; enzymes; homologous analysis; lipase gene sequence; phylogenetic tree; putative lipase catalytic triad; Amino acids; Bioinformatics; Biotechnology; Capacitive sensors; Cloning; DNA; Genomics; Laboratories; Microorganisms; Sequences; Staphylococcus caprae; degenerate primers; homology; lipase; partial gene cloning;
fLanguage
English
Publisher
ieee
Conference_Titel
Future Computer and Communication (ICFCC), 2010 2nd International Conference on
Conference_Location
Wuha
Print_ISBN
978-1-4244-5821-9
Type
conf
DOI
10.1109/ICFCC.2010.5497690
Filename
5497690
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