کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8289212 | 1536300 | 2016 | 34 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The death enzyme CP14 is a unique papain-like cysteine proteinase with a pronounced S2 subsite selectivity
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
MCAmAbCDRDTTpapain-like cysteine proteinase4-methylcoumaryl-7-amideNicotiana benthamianaPICsCHN2DegradomicsALP - آلکالن فسفاتازMonoclonal antibody - آنتی بادی مونوکلونالbenzoyl - بنزویلbenzyloxycarbonyl - بنزیلوسیکروبنیلdithiothreitol - دیتیوتریتولCysteine protease - سیستئین پروتئازCell death - مرگ سلولی Complementarity-determining region - منطقه تعریف کننده تکمیلیCathepsin - کاتپسینPlant - گیاه
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: The death enzyme CP14 is a unique papain-like cysteine proteinase with a pronounced S2 subsite selectivity The death enzyme CP14 is a unique papain-like cysteine proteinase with a pronounced S2 subsite selectivity](/preview/png/8289212.png)
چکیده انگلیسی
The cysteine protease CP14 has been identified as a central component of a molecular module regulating programmed cell death in plant embryos. CP14 belongs to a distinct subfamily of papain-like cysteine proteinases of which no representative has been characterized thoroughly to date. However, it has been proposed that CP14 is a cathepsin H-like protease. We have now produced recombinant Nicotiana benthamiana CP14 (NbCP14) lacking the C-terminal granulin domain. As typical for papain-like cysteine proteinases, NbCP14 undergoes rapid autocatalytic activation when incubated at low pH. The mature protease is capable of hydrolysing several synthetic endopeptidase substrates, but cathepsin H-like aminopeptidase activity could not be detected. NbCP14 displays a strong preference for aliphatic over aromatic amino acids in the specificity-determining P2 position. This subsite selectivity was also observed upon digestion of proteome-derived peptide libraries. Notably, the specificity profile of NbCP14 differs from that of aleurain-like protease, the N. benthamiana orthologue of cathepsin H. We conclude that CP14 is a papain-like cysteine proteinase with unusual enzymatic properties which may prove of central importance for the execution of programmed cell death during plant development.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 603, 1 August 2016, Pages 110-117
Journal: Archives of Biochemistry and Biophysics - Volume 603, 1 August 2016, Pages 110-117
نویسندگان
Melanie Paireder, Ulrich Mehofer, Stefan Tholen, Andreas Porodko, Philipp Schähs, Daniel Maresch, Martin L. Biniossek, Renier A.L. van der Hoorn, Brigita Lenarcic, Marko Novinec, Oliver Schilling, Lukas Mach,