کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10770699 | 1050835 | 2005 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Carboxy-monopeptidase substrate specificity of human cathepsin X
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
Cathepsin X is a papain-like cysteine protease with restricted positional specificity, acting primarily as a carboxy-monopeptidase. We mapped the specificities at the S2, S1, and S1â² subsites of human cathepsin X by systematically and independently substituting the P2, P1, and P1â² positions of the carboxy-monopeptidase substrate Abz-FRF(4NO2) with natural amino acids. Human cathepsin X has broad S2, S1, and S1â² specificities within two orders of magnitude in kcat/KM, excluding proline that is not tolerated at these subsites. Glycine is not favored in S2, but is among the preferred residues in S1 and S1â², which highlights S2 as the affinity-determinant subsite. The presence of peculiar residues at several binding site positions (Asp76, His234, Asn75, and Glu72) does not translate into a markedly different sequence specificity profile relative to other human cathepsins. These findings suggest that a specific function of human cathepsin X is unlikely to result from sequence specificity, but rather from a combination of its unique positional specificity and the co-localization of enzyme and substrate in a specific cellular environment.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 329, Issue 2, 8 April 2005, Pages 445-452
Journal: Biochemical and Biophysical Research Communications - Volume 329, Issue 2, 8 April 2005, Pages 445-452
نویسندگان
Gopal Devanathan, Joanne L. Turnbull, Edmund Ziomek, Enrico O. Purisima, Robert Ménard, Traian Sulea,