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Soto Biochem 10/8

by: Kayli Antos

Soto Biochem 10/8 CHEM 351

Marketplace > Towson University > Chemistry > CHEM 351 > Soto Biochem 10 8
Kayli Antos
GPA 3.37
Ana Soto

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Chapter: Enzymes Topics: Vmax And Kcat, Double Reciprocal Plot, Enzyme Inhibition, Competitive Inhibitors
Ana Soto
Class Notes
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This 2 page Class Notes was uploaded by Kayli Antos on Friday October 9, 2015. The Class Notes belongs to CHEM 351 at Towson University taught by Ana Soto in Summer 2015. Since its upload, it has received 12 views. For similar materials see Biochemistry in Chemistry at Towson University.

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Date Created: 10/09/15
Biochem Soto Fall 2015 Enzymes gt Vmax And Kcat 339 K2 is Kcat Vmax Vmax 2 KMS KM 3 KM is related to the affinity of E for S to Can say KM z This is also the Keq for a dissociation equation of E8 to E S V Kcat KM S Vmax ET Kcat 3 Catalytic efficiency is represented by 1 Kcat should be a large value and Vmax KM should be a small value 3 V0 2 2L if S is much smaller than KM it can be removed from the M denominator V0 2 KwtETS KM to Can solve for Vmax by using V0 2 End jg and inputting two values of V0 M and 8 setting each equation equal to Vmax then setting them equal to each other and solving to KM then Vmax Double Reciprocal Plot V S 1 KM 1 9 max V0 2 S can be expressed as 0 5 ax 3 When this is plotted it is called the Lineweaver Burk plot 3 X axis is 1S y axis is 1Vo x intercept is 1KM y intercept is 1Vmax Enzyme Inhibition to A molecule that interferes with catalytic activity is called an enzyme inhibitor to Inhibitors can be reversible or irreversible 3 Irreversible inhibitors will covalently bind to the enzyme or will destroy its functional groups that are needed for functionality 3 Reversible inhibitors will bind noncovalently to the enzyme and can be competitive uncompetitive or mixed noncompetitive binding to E8 or E E I Kd K Competitive Inhibitors to Competes with the substrate to bind to the enzymes active site When it binds it blocks the substrate from binding to Is structurally similar to the substrate to When it binds to the enzyme and enzyme inhibitor complex is formed 3 Increasing S will increase the amount of El When the S is very high the enzyme is saturated with substrate and the Vmax is unaffected When VOKM the S and KM will be higher when an inhibitor is present The MM equation is slightly changed by a factor of or 1 IKi when an Vmax5 i KM 1 KMS V0 Vmax5 Vmax The double reciprocal plot will also be affected with the slopedKMVmax and x intercept1dKM or is always greater than 1 so the slope will increase and the x intercept will decrease inhibitor is present V0 2


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