structural and biochemical characterization of the mitochondrial conformation reveals higher conformational stability and slow protein unfolding rate compared with the cytosolic conformation
type I isozyme, binds with a hydrophobic N-terminal sequence to mitochondria through interaction with porin using intermitochondrial ATP as cosubstrate facilitating the coordination of the introduction of glucose into glycolysis, type II isozyme binds with a hydrophobic N-terminal sequence to mitochondria in vitro
HK I, 2 kinds of interactions between HK I and mitochondria: a very specific one with the hexokinase-binding protein of the outer mitochondrial membrane, which is supressed by glucose 6-phosphate, and a less specific, cation-mediated one
the majority of the green fluorescent protein tagged HxkC appears to be associated with mitochondria both in cells grown in medium containing glucose as a carbon source and cells subjected to carbon starvation
bound at type A sites and type B sites of brain mitochondria, ratio of type A:type B is 40:60, enzyme bound at type A sites is releaved by glucose 6-phosphate, but not that of type B sites
hexokinase 2 is overexpressed in all aggressive tumors and predominantly found on the outer mitochondrial membrane. Structural and biochemical characterization of the mitochondrial conformation reveals higher conformational stability and slow protein unfolding rate compared with the cytosolic conformation. The interaction of hexokinase 2 with the mitochondria through its N-half is proposed to facilitate higher stability on the mitochondria
type I isozyme, binds with a hydrophobic N-terminal sequence to mitochondria through interaction with porin using intermitochondrial ATP as cosubstrate facilitating the coordination of the introduction of glucose into glycolysis, type II isozyme binds with a hydrophobic N-terminal sequence to mitochondria in vitro, in vivo preferably in cancer cells
oleate decreases hexokinase-mitochondrial binding and abolishes insulin-mediated translocation of HK I. Under basal conditions, the fraction of hexokinase I that is mitochondrially bound is 5times greater than for hexokinase II. Insulin and ischemia cause a fourfold increase in hexokinase II binding but only a doubling of hexokinase I binding
under basal conditions, the fraction of hexokinase I that is mitochondrially bound is 5times greater than for hexokinase II. Insulin and ischemia cause a fourfold increase in hexokinase II binding but only a doubling of hexokinase I binding
the mitochondrial membrane exopolyphosphatase activity is stimulated by the hexokinase reaction product, glucose-6-phosphate. Polyphosphates increase hydrogen peroxide generation in mitochondria in a situation where mitochondrial hexokinase is also active
the green fluorescent protein tagged HxkD is localized to the nucleus in cells grown in medium containing glucose, lactose or glycerol as carbon sources and when transferred to media lacking a carbon source
enzyme has the ability to associate with cellular organelles, this association indicates a conformational equilibrium which is strikingly influenced by glucose 6-phosphate