The Structure and Mechanism of Hexokinase: Difference between revisions

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<StructureSection load='' size='400' side='right' scene='' caption='Structure of human Glucokinase complex with sulfate and Na+ ion [[1v4t]]'>
<StructureSection load='1v4t' size='400' side='right' scene='' caption='Structure of human Glucokinase complex with sulfate and Na+ ion [[1v4t]]'>


A [[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.
A [[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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Kyle Schroering, Ann Taylor, David Canner, Cody Leatherman, Drew McCaffrey, Michal Harel, Alexander Berchansky, Joel L. Sussman