Enzyme Catalysis SBS017 Basic Biochemistry Dr John Puddefoot [email protected].
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Transcript of Enzyme Catalysis SBS017 Basic Biochemistry Dr John Puddefoot [email protected].
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Learning objectives Lecture 11
• You should be able to use Lineweaver-Burk plots to calculate KM and Vmax
• You will be able to describe competitive, uncompetitive and non-competitive inhibitors and how they alter enzyme kinetics
• You should understand the terms Allosteric and Cooperative regulation in relation to enzymes
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Michaelis-Menten Reminder
V is the velocity (or rate) of reaction[S] is the substrate concentrationVmax is the maximal velocity of the reactionKM is the Michaelis constant ([S] at Vmax/2)
𝑉 𝑜=𝑉𝑚𝑎𝑥[𝑆 ]
[𝑆 ]+𝐾𝑀
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K+1[E][S] = k-1 + k2[ES]
[𝐸 ] [𝑆 ][𝐸𝑆 ]
=(k −1+k 2)k+1
=𝐾𝑀
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𝐾𝑀=𝐾𝑀 (1+ [ 𝐼 ]𝐾 𝑖 )App
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𝑉𝑚𝑎𝑥=𝑉𝑚𝑎𝑥1+ [𝐼 ] /𝐾𝑖
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