Please use this identifier to cite or link to this item:
|標題:||Cloning of the gene and characterization of the enzymatic properties of the monomeric alkaline phosphatase (PhoX) from Pasteurella multocida strain X-73||作者:||Wu, J.R.
|關鍵字:||alkaline phosphatase;PhoX;Pasteurella multocida;escherichia-coli;vibrio-cholerae;gluconolactonase;identification;membrane;sequence;assay||Project:||Fems Microbiology Letters||期刊/報告no：:||Fems Microbiology Letters, Volume 267, Issue 1, Page(s) 113-120.||摘要:||
We have identified a new phoX gene encoding the monomeric alkaline phosphatase from Pasteurella multocida X-73. This gene was not found in the published genome sequence of Pasteurella multocida pm70. Characterization of the recombinant PhoX of Pasteurella multocida X-73 showed that it is a monomeric enzyme, activated by Ca2+ and possibly secreted by the Tat pathway. These features distinguish phosphatases of the PhoX family from those of the PhoA family. All proteins of the PhoX family were found to contain a conserved motif that shares significant sequence homology with the calcium-binding site of a phosphotriesterase known as diisopropylfluorophosphatase. Site-directed mutagenesis revealed that D527 of PhoX might be the ligand bound to the catalytic calcium. This is the first report on identification of homologous sequences between PhoX and the phosphotriesterase and on the potential calcium-binding site of PhoX.
|Appears in Collections:||微生物暨公共衛生學研究所|
Show full item record
TAIR Related Article
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.