کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9745130 | 1491459 | 2005 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The three-dimensional structures of peptide methionine sulfoxide reductases: current knowledge and open questions
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
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چکیده انگلیسی
Methionine sulfoxides are easily formed in proteins exposed to reactive oxidative species commonly present in cells. Their reduction back to methionine residues is catalyzed by peptide methionine sulfoxide reductases. Although grouped in a unique family with respect to their biological function, these enzymes are divided in two classes named MsrA and MsrB, depending on the sulfoxide enantiomer of the substrate they reduce. This specificity-based classification differentiates enzymes which display no sequence homology. Several three-dimensional structures of peptide methionine sulfoxide reductases have been determined, so that members of both classes are known to date. These crystal structures are reviewed in this paper. The folds and active sites of MsrAs and MsrBs are discussed in the light of the methionine sulfoxide reductase sequence diversity.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1703, Issue 2, 17 January 2005, Pages 249-260
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1703, Issue 2, 17 January 2005, Pages 249-260
نویسندگان
Brice Kauffmann, André Aubry, Frédérique Favier,