With Michaelis-Menten Kinetics, The Vmax is the maximum rate of the enzyme mediated reaction. When a system has a concentration of substrate well above Km (which is the concentration of substrate at which the reaction is proceeding at one-half Vmax), then it is said that the system is saturated. In this state, the reaction is occurring basically at Vmax, since there is plenty of substrate to react with the enzyme, and adding more substrate would not increase the reaction rate. Rather, the concentration of enzyme is the limiting factor of how much reaction product will be produced per unit time.

A Lineweaver-Burk is a double-reciprocal of the Michaelis-Menten equation. The equation for the graph, in  form is: 

From this graph, we can see that the slope is .

In a classic Michaelis-Menten graph, the y-axis represents reaction rate and the x-axis represents substrate concentration. At low substrate concentrations, the reaction rate increases sharply. But as the substrate concentration climbs, the reaction rate begins to increase less and less until it comes to a point where it plateaus into a flat line.

The reason this happens is because the enzyme becomes saturated with substrate. When substrate concentration is low, many of the enzymes in solution aren't doing anything, so they're readily available to convert substrate into product. Thus, adding even just a little bit of substrate will result in a dramatically increased reaction rate. When a high concentration of substrate is present, all of the enzymes in solution are busy. In other words, as soon as an enzyme converts a substrate into product, it immediately becomes occupied with another substrate. Since this process can't occur any faster unless more enzymes are added, all of the other substrate in solution have to wait their turn. Thus, any increase in substrate concentration under these circumstances results in very little, if any, increase in reaction rate.

When substrate concentration is high, all of the active sites can be constantly occupied by enzyme.  Further, the active sites can be saturated by enzyme when concentration is very high.  But, when the concentration of substrate is low, the reaction velocity is considered to be linear.

On a Lineweaver-Burk plot, the following are the correct matches regarding points of importance?

X-axis = 

Y-axis = 

X-intercept = 

Y-intercept = 

Slope = 

 will remain the same for an inhibited enzyme when a competitive inhibitor is used. With this information, one can figure out what will happen to the line for an inhibited enzyme on a Lineweaver Burk plot. The y-intercept represents  on these graphs, and so in the presence of a competitive inhibitor, the y-intercept will remain unchanged for an inhibited enzyme. The x-intercept represents . A competitive inhibitor will raise , and so the inhibited enzyme's x-intercept will be closer to the origin.

GLUT2 have a lower affinity for glucose and is essential for the liver and the pancreas to regulate the blood glucose level. With a lower affinity transporter, glucose will not be taken up immediately by the liver/pancreas while reserving for the high glucose demanding organs (e.g brain, neurons, red blood cells). Therefore, if one were to inherit such disease, extreme hypoglycemia may occur.   

GLUT1 and GLUT3 have the highest affinity for glucose. The Michaelis constant,  is the concentration of the substrate required to reach . The lower the , the higher the affinity is for the substrate.  

The enzyme in this question is said to be saturated with substrate. That means that at any given moment, all of the enzyme in solution is bound to a substrate so that adding more substrate will have no effect. This is referred to as the maximal velocity because the enzymes are working as fast as possible and will not respond to the addition of more substrate. By adding more enzyme, you a providing more active site to bind to more substrate molecules, effectively increasing the velocity of the overall reaction.

In enzyme kinetics,  is the concentration of substrate which allows the enzyme to reach  (maximum reaction velocity). A small  indicates that only a small amount of substrate is needed for the enzyme to become saturated and thus for the reaction to reach maximum velocity. This also indicates that the enzyme and substrate have high affinity for one another. A large  indicates that a large amount of substrate is needed for the enzyme to become saturated and thus for the reaction to reach maximum velocity.