کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
9121518 1159190 2005 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Analysis of the C-terminal domain of Burkholderia sp. strain LB400 BphK reveals a conserved motif that affects catalytic activity
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی ژنتیک
پیش نمایش صفحه اول مقاله
Analysis of the C-terminal domain of Burkholderia sp. strain LB400 BphK reveals a conserved motif that affects catalytic activity
چکیده انگلیسی
The bphK gene encoding glutathione S-transferase (GST) is located in the bph operon (PCB co-metabolism) in Burkholderia sp. strain LB400 and the enzyme has recently been shown to have dechlorination activity in relation to 4-chlorobenzoate (4-CBA). Alignments using other glutathione S-transferase sequences found in PCB degradation operons identified a highly conserved region in the C-terminal domain of these enzymes that included a conserved motif implicated in protein folding in eukaryotic GSTs. Site-directed mutagenesis indicated that the region is indirectly involved in the catalytic activity and substrate specificity of BphK. Predicted hydrogen bond interactions involving Asp155 play an important role in the enzymatic properties of this glutathione S-transferase.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEMS Microbiology Letters - Volume 249, Issue 1, 1 August 2005, Pages 23-30
نویسندگان
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