Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/68255
DC FieldValueLanguage
dc.contributor.authorChi, M.C.en_US
dc.contributor.authorChou, W.M.en_US
dc.contributor.authorHsu, W.H.en_US
dc.contributor.authorLin, L.L.en_US
dc.date2004zh_TW
dc.date.accessioned2014-06-11T05:56:31Z-
dc.date.available2014-06-11T05:56:31Z-
dc.identifier.issn0916-8451zh_TW
dc.identifier.urihttp://hdl.handle.net/11455/68255-
dc.description.abstractThe functional significance of amino acid residues Lys-265, Asp-270, Lys-277, Asp-288, Asp-347, Glu-349, and Arg-351 of Bacillus kaustophilus leucine aminopeptidase was explored by site-directed mutagenesis. Variants with an apparent molecular mass of approximately 54 kDa were overexpressed in Escherichia coli and purified to homogeneity by nickel-chelate chromatography. The purified mutant enzymes had no LAP activity, implying that these residues are important for the catalytic reaction of the enzyme.en_US
dc.language.isoen_USzh_TW
dc.relationBioscience Biotechnology and Biochemistryen_US
dc.relation.ispartofseriesBioscience Biotechnology and Biochemistry, Volume 68, Issue 8, Page(s) 1794-1797.en_US
dc.relation.urihttp://dx.doi.org/10.1271/bbb.68.1794en_US
dc.subjectBacillus kaustophilusen_US
dc.subjectleucine aminopeptidaseen_US
dc.subjectactive-site residuesen_US
dc.subjectsite-directed mutagenesisen_US
dc.subjectsite-specific recombinationen_US
dc.subjectx-ray crystallographyen_US
dc.subjectbovine lensen_US
dc.subjectescherichia-colien_US
dc.subjectmechanismen_US
dc.subjectionen_US
dc.titleIdentification of amino acid residues essential for the catalytic reaction of Bacillus kaustophilus leucine aminopeptidaseen_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1271/bbb.68.1794zh_TW
item.grantfulltextnone-
item.openairetypeJournal Article-
item.cerifentitytypePublications-
item.languageiso639-1en_US-
item.fulltextno fulltext-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
Appears in Collections:期刊論文
Show simple item record
 

Google ScholarTM

Check

Altmetric

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.