کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1933636 | 1050620 | 2009 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The quaternary structure of Escherichia coli N-acetylneuraminate lyase is essential for functional expression
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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
As part of a general study into the impact of quaternary structure on enzyme function, a library of 31 point mutations were engineered at the dimer–dimer interface of the homotetrameric (β/α)8-barrel protein, N-acetylneuraminate lyase (NAL, EC 4.1.3.3). Disruption of the interface generated either soluble tetramers or putative dimers that were absolutely insoluble and inactive. Intriguingly, the soluble tetramers were found to have widely varying kcat values, hinting at a role for the interface in catalysis. Leucine 171 was identified as essential to interface integrity. We conclude that the dimer–dimer interface of NAL is intolerant to mutation and essential for functional expression.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 388, Issue 1, 9 October 2009, Pages 107–111
Journal: Biochemical and Biophysical Research Communications - Volume 388, Issue 1, 9 October 2009, Pages 107–111
نویسندگان
Sean R.A. Devenish, Juliet A. Gerrard,