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    Please use this identifier to cite or link to this item: http://asiair.asia.edu.tw/ir/handle/310904400/17232


    Title: Glucose 6-phosphate release of wild-type and mutant human brain hexokinases from mitochondria
    Authors: ;Skaff, D.Andrew;Kim, Chang Sup;蔡建鈞;Tsai, Henry J;Richard, B.Honzatko;Herbert, J.Fromm
    Contributors: 保健營養生技學系
    Date: 2005-11
    Issue Date: 2012-11-26 10:30:19 (UTC+8)
    Abstract: One molecule of glucose 6-phosphate inhibits brain hexokinase (HKI) with high affinity by binding to either one of two sites located in distinct halves of the enzyme. In addition to potent inhibition, glucose 6-phosphate releases HKI from the outer leaflet of mitochondria; however, the site of glucose 6-phosphate association responsible for the release of HKI is unclear. The incorporation of a C-terminal polyhistidine tag on HKI facilitates the rapid purification of recombinant enzyme from Escherichia coli. The tagged construct has N-formyl methionine as its first residue and has mitochondrial association properties comparable with native brain hexokinases. Release of wild-type and mutant hexokinases from mitochondria by glucose 6-phosphate follow equilibrium models, which explain the release phenomenon as the repartitioning of ligand-bound HKI between solution and the membrane. Mutations that block the binding of glucose 6-phosphate to the C-terminal half of HKI have little or no effect on the glucose 6-phosphate release. In contrast, mutations that block glucose 6-phosphate binding to the N-terminal half require approximately 7-fold higher concentrations of glucose 6-phosphate for the release of HKI. Results here implicate a primary role for the glucose 6-phosphate binding site at the N-terminal half of HKI in the release mechanism.
    Relation: JOURNAL OF BIOLOGICAL CHEMISTRY;280(46):38403-9.
    Appears in Collections:[食品營養與保健生技學系] 期刊論文

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