Lecture 6 - . Explain the value of the L-B plot over the...

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Lecture 6, January 18, 2012 100-103 Learning Outcomes 1. Explain the terms Km and Vmax and indicate appropriate unites for each. Vmax- the initial velocity at the theoretical saturation point Km- Michaelis constant, which is equal to the substrate concentration when the reaction velocity is ½ of Vmax 2. Explain the relationship between enzyme affinity and Km. The smaller the Km value, the greater the affinity of the enzyme for the substrate. The higher the Km, the greater the substrate concentration that is required to reach ½ Vmax and, thus, the lower the affinity of the enzyme for that substrate. 3. Be able to illustrate results from an enzyme kinetics experiment using either the Michaelis-Menten plot or the Linweaver-Burke plot
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Unformatted text preview: . Explain the value of the L-B plot over the M-M plot. Vmax and Km are difficult to evaluate from a Michaelis-Menten curve take reciprocal to linearize. 4. Illustrate the M-M and L-B curves that would result from reducing the enzyme concentration. 5. Explain the difference between types of reversible inhibitors and illustrate each on M-M and L-B plots. Competitive inhibitors- reversible inhibitors that compete with a substrate for access to the active site for an enzyme Noncompetitive inhibitors- the substrate and inhibitor do not compete for the same binding site; generally, the inhibitor acts at a site other than the enzymes active site. Illustrated in Notebook....
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This note was uploaded on 02/20/2012 for the course CELL STRUC 301 taught by Professor Tepperman during the Spring '12 term at Ohio State.

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Lecture 6 - . Explain the value of the L-B plot over the...

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