enzyme catalysis sbs017 basic biochemistry dr john puddefoot [email protected]

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Enzyme Catalysis SBS017 Basic Biochemistry Dr John Puddefoot [email protected]

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Page 1: Enzyme Catalysis SBS017 Basic Biochemistry Dr John Puddefoot J.R.Puddefoot@qmul.ac.uk

Enzyme Catalysis

SBS017Basic Biochemistry

Dr John [email protected]

Page 2: Enzyme Catalysis SBS017 Basic Biochemistry Dr John Puddefoot J.R.Puddefoot@qmul.ac.uk

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

Page 3: Enzyme Catalysis SBS017 Basic Biochemistry Dr John Puddefoot J.R.Puddefoot@qmul.ac.uk

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

Page 4: Enzyme Catalysis SBS017 Basic Biochemistry Dr John Puddefoot J.R.Puddefoot@qmul.ac.uk
Page 5: Enzyme Catalysis SBS017 Basic Biochemistry Dr John Puddefoot J.R.Puddefoot@qmul.ac.uk

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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