Lecture_20B-Mixed_Inhibition

Lecture_20B-Mixed_Inhibition - does not have to resemble...

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ENZYME INHIBITION Mixed Inhibition The Effect of Mixed Inhibitors on Michaelis Constants E + S k 1 -1 ES 2 E + P + I ESI K' I + I EI+ S K I v 0 = k 2 E [ ] total S [ ] total α ' S [ ] total + K M 1 v 0 = K M V max 1 S [ ] + ' V max E + S ES E + P + I ESI K' I + I EI+ S K I The Effect of Mixed Inhibitors on Michaelis Constants 1 v 0 = K M V max 1 S [ ] + ' V max The Effect of Mixed Inhibitors on Michaelis Constants
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Mixed Inhibitors: Summary binds to a site distinct from the active site
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Unformatted text preview: does not have to resemble the substrate affects both the apparent K M and the apparent V max this type of inhibition is observed in enzymes that have two or more substrates Lineweaver-Burk plots result in intersecting lines that have different slopes and different X- and Y-intercepts...
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Lecture_20B-Mixed_Inhibition - does not have to resemble...

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