Báo cáo khoa học: Human salivary a-amylase Trp58 situated at subsite )2 is critical for enzyme activity
Số trang: 13
Loại file: pdf
Dung lượng: 1.02 MB
Lượt xem: 16
Lượt tải: 0
Xem trước 2 trang đầu tiên của tài liệu này:
Thông tin tài liệu:
The nonreducing end of the substrate-binding site of humansalivarya-amylase contains two residues Trp58 and Trp59,which belong tob2–a2 loop of the catalytic (b/a)8barrel.While Trp59 stacks onto the substrate, the exact role ofTrp58 is unknown. To investigate its role in enzyme activitythe residue Trp58 was mutated to Ala, Leu or Tyr. Kineticanalysis of the wild-type and mutant enzymes was carriedout with starch and oligosaccharides as substrates. All threemutants exhibited a reduction in specific activity (150–180-fold lower than the wild type) with starch as substrate....
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: Human salivary a-amylase Trp58 situated at subsite )2 is critical for enzyme activity
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: Human salivary a-amylase Trp58 situated at subsite )2 is critical for enzyme activity
Tìm kiếm theo từ khóa liên quan:
Report medicine traditional medicine scientific reports intermediate cells cell proliferation medical analysisTài liệu liên quan:
-
Báo cáo khóa học: The structure–function relationship in the clostripain family of peptidases
10 trang 39 0 0 -
Báo cáo khoa học: Parsing in the Ahsmmeeofa Comldete Lexicon
2 trang 31 0 0 -
7 trang 30 0 0
-
8 trang 30 0 0
-
Báo cáo khoa học: Are UV-induced nonculturable Escherichia coli K-12 cells alive or dead?
7 trang 27 0 0 -
10 trang 26 0 0
-
14 trang 25 0 0
-
Báo cáo khoa học: Viral entry mechanisms: cellular and viral mediators of herpes simplex virus entry
9 trang 25 0 0 -
Báo cáo khoa học: Cellular response to unfolded proteins in the endoplasmic reticulum of plants
20 trang 24 0 0 -
Báo cáo khoa học: Endoribonucleases – enzymes gaining spotlight in mRNA metabolism
15 trang 24 0 0