Scribd
Upload
31 views20 pages

Enzyme Kinetics

The rate of an enzyme reaction is calculated as the change in amount of product over time. Reaction velocity is affected by factors like temperature, pH, substrate and enzyme concentration, and presence of activators or inhibitors. The Michaelis-Menten equation describes the quantitative relationship between reaction rate and substrate concentration. Enzyme inhibition decreases reaction velocity and can be reversible or irreversible. Reversible inhibition includes competitive, noncompetitive, and uncompetitive inhibition which have distinct effects on kinetic plots.

Uploaded by

Islam Samir
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PPT, PDF, TXT or read online on Scribd
31 views20 pages

Enzyme Kinetics

The rate of an enzyme reaction is calculated as the change in amount of product over time. Reaction velocity is affected by factors like temperature, pH, substrate and enzyme concentration, and presence of activators or inhibitors. The Michaelis-Menten equation describes the quantitative relationship between reaction rate and substrate concentration. Enzyme inhibition decreases reaction velocity and can be reversible or irreversible. Reversible inhibition includes competitive, noncompetitive, and uncompetitive inhibition which have distinct effects on kinetic plots.

Uploaded by

Islam Samir
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PPT, PDF, TXT or read online on Scribd
You are on page 1/ 20

Reaction Velocity

The rate of an enzyme reaction is computed as a change


in the amount of product produced per unit time

Example:

Rate = grams of ethanol produced/ minute


= change in absorbance at 240 nm/ min
The change in the amount of substrate consumed per
unit time
Factors affecting reaction velocity
 Temperature
 pH
 Substrate concentration
 Enzyme concentration
 Presence of activator/inhibitor
Effect of Temperature

Reaction
Velocity
(v)

Temperature(oC)
Effect of pH

Trypsin
Pepsin

Reaction
Velocity
(v)

q r

pH
Effect of Enzyme Concentration
Rate of the reaction or velocity is directly
proportional to the enzyme concentration when
sufficient substrate is present.
Effect of Substrate Concentration

Reaction
Velocity
(v)

Substrate Concentration/arbitrary Units


Enzyme Kinetics
Kinetics is the study of reaction rates and
how they change in response to changes
in experimental parameters

The amount of substrate present is one of


the key factor affecting the rate of reaction
catalyzed by an enzyme in vitro.
Effect of Substrate Concentration on
Reaction Velocity
Michaelis- Menten Kinetics
The model involves one substrate molecule,
k1 k2
E + S ‹-------------› ES ------------ › E + P
k-1
S is the substrate
E is the enzyme
k1, k-1 and k2 are the rate constants
The mathematical equation that defines the quantitative
relationship between the rate of an enzyme reaction and
the substrate concentration is the Michaelis-Menten
equation:
Vmax [S]
V = -------------
Km + [S]

v is the observed velocity at the given [S]


Km is the Michaelis-Menten constant
Km = (K-1 + K2) / K1
Vmax is the maximum velocity at saturating [S] conc.
Lineweaver-Burk Plot

A linear representation is more accurate


and convenient for determining Vmax and
Km.

This is obtained by taking reciprocal of


both the side of Michelis-Menten equation
and plotting1/[S] vs. 1/V
Lineweaver-Burk Plot

1 Km 1 1
 
v Vmax [ S ] Vmax
Enzyme Inhibition
Inhibition refers to the decrease in the velocity
of an enzyme reaction

An inhibitor is any substance that can diminish


the velocity of an enzyme catalyzed

These can include drugs, antibiotics, poisons,


and anti-metabolites.
Enzyme Inhibition
Inhibitors are useful in understanding the
sequence of enzyme catalyzed reactions,
metabolic regulation, studying the mechanism
of cell toxicity produced by toxicants.

They also form the basis of drug designing.


Types of Enzyme Inhibition

Reversible Inhibition
These type of inhibition is caused by breakage or
formation of intermolecular forces of attraction

Irreversible Inhibition
These type of inhibition is caused by breakage or
formation of covalent bonds
Classification of Reversible inhibition

Competitive
The inhibitor binds to the active site
Noncompetitive
The inhibitor binds to an allosteric site or
another site in the enzyme
Uncompetitive
The inhibitor binds to the enzyme-substrate
complex
Competitive Inhibition
NonCompetitive Inhibition
Uncompetitive Inhibition

ES Complex
Enzyme

+ Inhibitor

ESI complex
Enzyme Inhibition (Plots)

I Competitive I Non-competitive I Uncompetitive


Vmax Vmax Vmax
vo vo
Vmax’ Vmax’
Direct Plots

I I I

Km Km’ [S], mM Km = Km’ [S], mM Km’ Km [S], mM


Vmax unchanged Vmax decreased
Both Vmax & Km decreased
Km increased Km unchanged
Double Reciprocal

1/vo I 1/vo I 1/vo


I
Two parallel
Intersect lines
at Y axis 1/ Vmax 1/ Vmax
Intersect 1/ Vmax
at X axis

1/Km 1/[S] 1/Km 1/[S] 1/Km 1/[S]

You might also like

pFad - Phonifier reborn

Pfad - The Proxy pFad of © 2024 Garber Painting. All rights reserved.

Note: This service is not intended for secure transactions such as banking, social media, email, or purchasing. Use at your own risk. We assume no liability whatsoever for broken pages.


Alternative Proxies:

Alternative Proxy

pFad Proxy

pFad v3 Proxy

pFad v4 Proxy