کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10767751 | 1050796 | 2005 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
SocA is a novel periplasmic binding protein for fructosyl amino acid
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Bacterial periplasmic proteins (bPBPs) undergo drastic conformational changes upon binding substrate, making them appealing as novel molecular recognition tools for biosensing. A putative bPBP-encoding gene, socA, belongs to the soc operon responsible for santhopine (fructosyl glutamine, FQ) catabolism of Agrobacterium tumefaciens. The socA gene was isolated and expressed in Escherichia coli as a soluble 28.8 kDa periplasmic protein to investigate its properties as a potential bPBP for fructosyl amino acid (FA). The autofluorescence of SocA was used to monitor the protein's conformational change resulting from substrate binding. The fluorescence intensity changed upon binding FQ in a concentration dependent manner with a calculated Kd of 2.1 μM, but was unaffected by the presence of sugars or amino acid. Our results demonstrate that SocA is a novel FA bPBP that can be utilized as a novel molecular recognition element for the monitoring of FA.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 336, Issue 4, 4 November 2005, Pages 1074-1080
Journal: Biochemical and Biophysical Research Communications - Volume 336, Issue 4, 4 November 2005, Pages 1074-1080
نویسندگان
Akane Sakaguchi, Stefano Ferri, Koji Sode,