Please use this identifier to cite or link to this item:
標題: Identification of amino acid residues essential for the catalytic reaction of Bacillus kaustophilus leucine aminopeptidase
作者: Chi, M.C.
Chou, W.M.
Hsu, W.H.
Lin, L.L.
關鍵字: Bacillus kaustophilus;leucine aminopeptidase;active-site residues;site-directed mutagenesis;site-specific recombination;x-ray crystallography;bovine lens;escherichia-coli;mechanism;ion
Project: Bioscience Biotechnology and Biochemistry
期刊/報告no:: Bioscience Biotechnology and Biochemistry, Volume 68, Issue 8, Page(s) 1794-1797.
The 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.
ISSN: 0916-8451
DOI: 10.1271/bbb.68.1794
Appears in Collections:期刊論文

Show full item record

Google ScholarTM




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