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GLUT2 in contrast has a high Km value (15-20mM) and therefore a low affinity for glucose. They are located in the plasma membranes of hepatocytes and pancreatic beta cells (in mice, but GLUT1 in human beta cells). [5] The high Km of GLUT2 allows for glucose sensing; rate of glucose entry is proportional to blood glucose levels.
Hexokinases I, II, and III are referred to as low-K m isoenzymes because of a high affinity for glucose (below 1 mM). Hexokinases I and II follow Michaelis-Menten kinetics at physiological concentrations of substrates.
low-glucose sensor; repressed by glucose; low expression level; repressor of Hxt6: Rgt2: high-glucose sensor; low expression level Hxt1: Km: 100 mM, [3] 129 - 107 mM [1] low-affinity glucose transporter; induced by high glucose level Hxt2: Km = 1.5 [1] - 10 mM [3] high/intermediate-affinity glucose transporter; induced by low glucose level [3] Hxt3
GLUT2 has high capacity for glucose but low affinity (high K M, ca. 15–20 mM) and thus functions as part of the "glucose sensor" in the pancreatic β-cells of rodents, though in human β-cells the role of GLUT2 seems to be a minor one. [8] It is a very efficient carrier for glucose.
The pH optimum of human glucokinase was identified only recently and is surprisingly high, at pH 8.5–8.7. [19] A "minimal mathematical model" has been devised based on the above kinetic information to predict the beta cell glucose phosphorylation rate (BGPR) of normal ("wild type") glucokinase and the known mutations. The BGPR for wild type ...
In the field of biochemistry, the specificity constant (also called kinetic efficiency or /), is a measure of how efficiently an enzyme converts substrates into products.A comparison of specificity constants can also be used as a measure of the preference of an enzyme for different substrates (i.e., substrate specificity).
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The binding constant, or affinity constant/association constant, is a special case of the equilibrium constant K, [1] and is the inverse of the dissociation constant. [2] It is associated with the binding and unbinding reaction of receptor (R) and ligand (L) molecules, which is formalized as: R + L ⇌ RL