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Enzymes 1

The document discusses enzymatic reactions and Michaelis-Menten kinetics, detailing how enzymes catalyze reactions and the relationship between substrate concentration and reaction velocity. It explains key concepts such as Vmax, Km, and their significance in enzyme kinetics, including how Km indicates substrate affinity. Additionally, it introduces the Lineweaver-Burk plot as a method to analyze enzyme kinetics.

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mishulop23
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7 views16 pages

Enzymes 1

The document discusses enzymatic reactions and Michaelis-Menten kinetics, detailing how enzymes catalyze reactions and the relationship between substrate concentration and reaction velocity. It explains key concepts such as Vmax, Km, and their significance in enzyme kinetics, including how Km indicates substrate affinity. Additionally, it introduces the Lineweaver-Burk plot as a method to analyze enzyme kinetics.

Uploaded by

mishulop23
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as PDF, TXT or read online on Scribd
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Enzymes

Jason Ryan, MD, MPH


Enzymatic Reactions
enzyme: catalists: increase rate of conversion

substrate product

P
S

S + E ⇄ ES ⇄ E + P
Enzymatic Reactions
S + E ⇄ ES ⇄ E + P

Image courtesy of Wikipedia/U+003F


Michaelis-Menten Kinetics
V = Reaction velocity
Rate of P formation
Vmax

V = Vm* [S]
Km + [S]
V
product rate formation

when we add more substrate we get [S]


increase speed of formation of product
Michaelis-Menten Kinetics
• Adding S → More P formation → Faster V
• Eventually, reach Vmax
ou cant go on no matter how much substrate you add
Michaelis-Menten Kinetics
• At Vmax, enzymes saturated (doing all they can)
• Only way to increase Vmax is to add enzyme
Enzyme Kinetics
Vmax
More Enzyme
Vmax

[S]
Michaelis-Menten Kinetics
V = Reaction velocity
Rate of P formation
Vmax

V = Vm* [S]
Km + [S]
V

[S]
Michaelis Constant (Km)

V = Vm * [S]
Km + [S]

Key Points:
1. Km has same units as [S]
2. At some point on graph, Km must equal [S]
Michaelis Constant (Km)

V = Vm * [S] = Vm * [S] = Vm
[S] + [S] 2 [S] 2

When V = Vm/2
[S] = Km
Michaelis Constant (Km)

Vmax

V = Vm* [S]
Vmax/2 Km + [S]

Km
[S]
Michaelis Constant (Km)
• Small Km → Vm reached at low concentration [S]
• Large Km → Vm reached at high concentration [S]

Vmax

V = Vm* [S]
Vmax/2
Km + [S]

Km
[S]
Michaelis Constant (Km)
• Small Km → Substrate binds easily at low [S]
• High affinity substrate for enzyme
• Large Km → Low affinity substrate for enzyme

Vmax

V = Vm* [S]
Vmax/2
Km + [S]

Km
[S]
Key Points
• Km is characteristic of each substrate/enzyme
• Vm depends on amount of enzyme present
• Can determine Vm/Km from
• Michaelis Menten plot V vs. [S]
• Lineweaver Burk plot 1/V vs. 1/[S]
Lineweaver Burk Plot
V = Vm* [S]
Km + [S]

1 = Km + [S] = Km + [S]
V Vm [S] Vm [S] Vm[S]

1= C *1 + 1
V [S] Vm
Lineweaver Burk Plot
1
V
Km
Vm

1
Vm
1
S
-1
Km

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