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Function
falls under the protein category of a kinase. A kinase is a protein that is responsible for the modification of a molecule through the covalent addition of the phosphate group. The source of the phosphate group is . Human Hexokinase 1 catalyzes the phosphorylation of hexose sugars, primarily to form Glucose-6-Phosphate. This is typically observed during the initial step of glycolysis and is performed in order to attach a charge to the glucose, preventing it from diffusing out of the cell through the cell membrane. Typically, a cofactor also participates in a chelation complex with ATP [3].
Human Hexokinase 1 is also seen to have a function in both innate immunity and inflammation in which the protein acts as a pattern recognition receptor for N-acetyl-D-glucosamine, a hexose present in the peptidoglycan layer of bacterial cell walls. Upon binding to N-acetyl-D-glucosamine, Human Hexokinase 1 dissociates from the mitochondria, which results in the activation of NLRP3 inflammasome [4].
Disease
There are multiple diseases associated with Human Hexokinase 1. It is possible for illness to arise from a deficiency in the protein. A deficiency is a rare autosomal recessive disease in which the Leucine and Threonine residues in the 529 and the 680 positions are mutated and translated as a Serine. This disease results in nonspherocytic hemolytic anemia[5]7655856.
Relevance
Structural highlights
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