bis102-11-2

bis102-11-2 - 1- specificity of enzyme 2. the physical and...

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11/2/2011 accurate determination of vmas is difficult to obtain since vmax is only asymptotically approached. km = 1/2 vmax transform michaelis-menten equation into a linear equation to determine accurate vmax. intercept on x-axis= -1/km intercept on y-axis= 1/ vmax cut off --- for quiz!!!! lineweaver- burk plot! enzyme inhibition -many factors such as pH, temperature, substrate concentration influence the velocity of an enzyme catalyzed reaction. -these reactions are also influenced by inhibitors -inhibition is a key mode of metabolic regulation -also drugs, antibiotics and poisons can all act as inhibitors studies tell about:
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Unformatted text preview: 1- specificity of enzyme 2. the physical and chemical architechture of the active site. 3. the kinetic mechanism of reaction there are 3 classical types of inhibition 1. competitive 2. noncompetitive 3. uncompetitive Competitive inhibition-inhibitor only binds to the free enzyme and competes with the substrate for the active site. or binds close to the site and prevents substrate from binding.-competitive very closely resembles the substrate Ks-- dissociation constant for the enzyme substrate complex. . The Vmax is not affected but Ks is affected in the machaelis -menten equation....
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bis102-11-2 - 1- specificity of enzyme 2. the physical and...

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