Kinetic Cooperativity in Human Pancreatic Glucokinase Originates from Millisecond Dynamics of the Small Domain
نویسندگان
چکیده
منابع مشابه
Human pancreatic glucokinase Structural and physico-chemical studies related to catalytic activation, kinetic cooperativity and GCK-diabetes
.................................................................................................................................... 8 List of publications .................................................................................................................. 10
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Glucokinase (GCK) catalyzes the rate-limiting step of glucose catabolism in the pancreas, where it functions as the body's principal glucose sensor. GCK dysfunction leads to several potentially fatal diseases including maturity-onset diabetes of the young type II (MODY-II) and persistent hypoglycemic hyperinsulinemia of infancy (PHHI). GCK maintains glucose homeostasis by displaying a sigmoidal...
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15 صفحه اولBinding of ATP at the active site of human pancreatic glucokinase – nucleotide-induced conformational changes with possible implications for its kinetic cooperativity
Glucokinase (GK) is the central player in glucose-stimulated insulin release from pancreatic β-cells, and catalytic activation by α-D-glucose binding has a key regulatory function. Whereas the mechanism of this activation is well understood, on the basis of crystal structures of human GK, there are no similar structural data on ATP binding to the ligand-free enzyme and how it affects its confor...
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chapter i provides an overview of structural linguistics and touches upon the saussurean dichotomies with the final goal of exploring their relevance to the stylistic studies of literature. to provide evidence for the singificance of the study, chapter ii deals with the controversial issue of linguistics and literature, and presents opposing views which, at the same time, have been central to t...
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ژورنال
عنوان ژورنال: Angewandte Chemie International Edition
سال: 2015
ISSN: 1433-7851
DOI: 10.1002/anie.201501204