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Glucose-6-Phosphate Appears to be a Competitive Inhibitor of the Bovine Intestine Enzyme Alkaline Phosphatase Abstract This study focuses on the effects of glucose-6-phosphate G6P on the kinetics of the enzyme alkaline phosphatase Because G6P is a common molecule and has a phosphoester bond it may prevent alkaline phosphatase from hydrolyzing certain substrates The data collected in this study seem to indicate that G6P is a competitive inhibitor of the enzyme and causes an increased Km for the reaction Further studies should be done to investigate the initial conclusion Introduction An enzyme is a catalyst that increases the rate at which a biological reaction occurs by providing a surface where the reactants can be bound in such a way that they become more likely to react with each other The point on the enzyme where a reactant binds is known as the active site Becker et al 2000 The binding of a reactant or substrate to the active site depends on random collisions and by increasing the substrate concentration more collisions occur and the overall rate of the reaction increases Eventually the reaction will reach a maximum velocity When reaction velocity is graphed as a function of substrate concentration many enzymatic reactions give rectangular hyperbolas This type of graph is referred to as a Michaelis-Menten plot and two important features are the maximum velocity Vmax and the substrate concentration at one half of the maximum velocity Km Becker et al 2001 Because it is difficult to estimate Vmax and Km from a Michaelis-Menten plot a Lineweaver-Burk plot can also be used This plot is a double reciprocal plot 1v vs 1S is graphed and the x and y intercept values are used in determining Km and Vmax The velocity of an enzymatic reaction can be affected not only by changing the substrate concentration but also by the presence of an inhibitor A competitive inhibitor is one that decreases the velocity of a reaction by
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