Sandbox 172: Difference between revisions
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==Functional Overview== | ==Functional Overview== | ||
===Basic Function=== | ===Basic Function=== | ||
Hexokinase Type I functions in a mainly catabolic role; it is responsible for introducing glucose the glycolytic process in attempts to produce ATP. Hexokinase Type I phosphorylates a hexose into a hexose phosphate; most commonly the substrate of hexokinase I is found to be glucose and the product found to be glucose-6-phosphate. Mammalian brain tissue shows a high content of Hexokinase Type I which reiterates the idea that this isoenzyme is needed to maintain high rates of energy metabolism. Hexokinase Type I associated with brain homogenates demonstration an interaction with outer mitochondrial membrane. The binding of to this mitochondria is highly dependent on the N-terminus sequence. The protein porin is then responsible for the formation of a channel in which metabolites can pass through the mitochondrial membrame.<ref>Wilson, J. Isozymes of mammalian hexokinase: structure, subcellular localization and metabolic function. The Journal of Experimental Biology. 2003.'''206''':2049-2057.</ref> | Hexokinase Type I functions in a mainly catabolic role; it is responsible for introducing glucose the glycolytic process in attempts to produce ATP. Hexokinase Type I phosphorylates a hexose into a hexose phosphate; most commonly the substrate of hexokinase I is found to be glucose and the product found to be glucose-6-phosphate.<ref>Bianchi M., Casabianca A., Magnani M., Serafini G., Stocchi V. Human hexokinase type I microheterogeneity is due to different amino-terminal sequences. The Journal of Biological Chemistry. 1991. '''266''': 502-505.</ref> Mammalian brain tissue shows a high content of Hexokinase Type I which reiterates the idea that this isoenzyme is needed to maintain high rates of energy metabolism. Hexokinase Type I associated with brain homogenates demonstration an interaction with outer mitochondrial membrane. The binding of to this mitochondria is highly dependent on the N-terminus sequence. The protein porin is then responsible for the formation of a channel in which metabolites can pass through the mitochondrial membrame.<ref>Wilson, J. Isozymes of mammalian hexokinase: structure, subcellular localization and metabolic function. The Journal of Experimental Biology. 2003.'''206''':2049-2057.</ref> | ||
===Allosteric Regulation=== | ===Allosteric Regulation=== | ||
==References== | ==References== | ||
