Báo cáo khoa học: The ‘pair of sugar tongs' site on the non-catalytic domain C of barley a-amylase participates in substrate binding and activity
Số trang: 13
Loại file: pdf
Dung lượng: 422.56 KB
Lượt xem: 5
Lượt tải: 0
Xem trước 2 trang đầu tiên của tài liệu này:
Thông tin tài liệu:
Some starch-degrading enzymes accommodate carbohydrates at sites situ-ated at a certain distance from the active site. In the crystal structure ofbarleya-amylase 1, oligosaccharide is thus bound to the ‘sugar tongs’ site.This site on the non-catalytic domain C in the C-terminal part of the mole-cule contains a key residue, Tyr380, which has numerous contacts with theoligosaccharide.
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: The ‘pair of sugar tongs’ site on the non-catalytic domain C of barley a-amylase participates in substrate binding and activity
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: The ‘pair of sugar tongs’ site on the non-catalytic domain C of barley a-amylase participates in substrate binding and activity
Tìm kiếm theo từ khóa liên quan:
Report medicine traditional medicine scientific reports Structural biochemistry bacteria chemical reactionTài liệu liên quan:
-
Báo cáo khóa học: The structure–function relationship in the clostripain family of peptidases
10 trang 42 0 0 -
8 trang 34 0 0
-
7 trang 34 0 0
-
14 trang 32 0 0
-
Báo cáo khoa học: Parsing in the Ahsmmeeofa Comldete Lexicon
2 trang 32 0 0 -
Báo cáo khoa học: Viral entry mechanisms: cellular and viral mediators of herpes simplex virus entry
9 trang 31 0 0 -
10 trang 29 0 0
-
Báo cáo khoa học: Are UV-induced nonculturable Escherichia coli K-12 cells alive or dead?
7 trang 28 0 0 -
Báo cáo Y học: Mycobacterium tuberculosis FprA, a novel bacterial NADPH-ferredoxin reductase
9 trang 26 0 0 -
Báo cáo khoa học: Cellular response to unfolded proteins in the endoplasmic reticulum of plants
20 trang 26 0 0