Hexokinase: Difference between revisions

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<StructureSection load='1qha' size='450' side='right' scene='' caption=''>
<StructureSection load='1qha' size='450' side='right' scene='' caption='Hexokinase I complex with ATP analog, glucose, glucose-phosphate and Mg+2 ion (PDB code [[1qha]])'>
'''Hexokinase''' is an enzyme that phosphorylates a six-carbon sugar, a hexose, to a hexose phosphate. In most tissues and organisms, glucose is the most important substrate of hexokinases, and glucose 6-phosphate the most important product.  Hexokinases have been found in every organism checked, ranging from bacteria, yeast, and plants, to humans and other vertebrates. They are categorized as actin fold proteins, sharing a common ATP binding site core surrounded by more variable sequences that determine substrate affinities and other properties. Several hexokinase isoforms or isozymes providing different functions can occur in a single species.  
'''Hexokinase''' is an enzyme that phosphorylates a six-carbon sugar, a hexose, to a hexose phosphate. In most tissues and organisms, glucose is the most important substrate of hexokinases, and glucose 6-phosphate the most important product.  Hexokinases have been found in every organism checked, ranging from bacteria, yeast, and plants, to humans and other vertebrates. They are categorized as actin fold proteins, sharing a common ATP binding site core surrounded by more variable sequences that determine substrate affinities and other properties. Several hexokinase isoforms or isozymes providing different functions can occur in a single species.  


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Ann Taylor, Michal Harel, Alexander Berchansky, Karsten Theis