کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
10758550 1050409 2013 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Structural modelling of substrate binding and inhibition in penicillin V acylase from Pectobacterium atrosepticum
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Structural modelling of substrate binding and inhibition in penicillin V acylase from Pectobacterium atrosepticum
چکیده انگلیسی
Penicillin V acylases (PVAs) and bile salt hydrolases (BSHs) have considerable sequence and structural similarity; however, they vary significantly in their substrate specificity. We have identified a PVA from a Gram-negative organism, Pectobacterium atrosepticum (PaPVA) that turned out to be a remote homolog of the PVAs and BSHs reported earlier. Even though the active site residues were conserved in PaPVA it showed high specificity towards penV and interestingly the penV acylase activity was inhibited by bile salts. Comparative modelling and docking studies were carried out to understand the structural differences of the binding site that confer this characteristic property. We show that PaPVA exhibits significant differences in structure, which are in contrast to those of known PVAs and such enzymes from Gram-negative bacteria require further investigation.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 437, Issue 4, 9 August 2013, Pages 538-543
نویسندگان
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