کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1952921 1057239 2009 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Bacillusd-stereospecific metallo-amidohydrolase: Active-site metal-ion substitution changes substrate specificity
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Bacillusd-stereospecific metallo-amidohydrolase: Active-site metal-ion substitution changes substrate specificity
چکیده انگلیسی

From investigation of 2000 soil isolates, we identified a d-stereospecific metallo-amidohydrolase that can hydrolyze d-aminoacyl derivatives from the culture supernatant of Bacillus sp. 62E11: 62E11DppA. The enzyme binds two equivalents of zinc, exhibits 70% identity with that of d-aminopeptidases from Bacillus subtilis (DppA). In fact, 62E11DppA has strict specificity toward d-aminoacyl derivatives, i.e., the enzyme shows high activity toward d-aminoacyl benzyl esters and little activity toward d-amino acid containing peptides. Moreover, 62E11DppA exhibits a dramatic change in its activity and substrate specificity by substitution of metal ions in its active site. Based on results of kinetic studies using apo-62E11DppA with various metal ion and substrate concentrations, we propose a possible mechanism for the change in its activity and specificity by substitution of metal ions: the substitution of metal ions in 62E11DppA dramatically changes its activity by altering the substrate specificity.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimie - Volume 91, Issue 4, April 2009, Pages 568–576
نویسندگان
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