Home Site Map Contact Us
Rapid Learning Member Login  
Rapid Learning Blog Rapid Learning on Facebook Rapid Learning on Youtube Rapid Learning on Twitter
 How to Learn in 24 Hours?

 Need Help?
M-F: 9am-5pm(PST):
Toll-Free: (877) RAPID-10
US Direct: (714) 692-2900
Int'l: 001-714-692-2900


24/7 Technical Support:
The Rapid Support Center

Secure Online Order:
Buy Now

 

 Got Questions?
Frequently Asked Questions
 Need Proof?
Testimonials by Our Users
Rapid Learning Center - BBB Accredited Business

Trustlink is a Better Business Bureau Program.
Read TrustLink Reviews




 Member Login:
User ID: 
Password: 
 

 Rapid Learning Courses:

Chemistry in 24 Hours

Biology in 24 Hours

Physics in 24 Hours

Mathematics in 24 Hours

Psychology in 24 Hours

SAT in 24 Hours

ACT in 24 Hours

AP in 24 Hours

CLEP in 24 Hours

MCAT in 24 Hours (Medical)

USMLE in 24 Hours (Boards)

DAT in 24 Hours (Dental)

OAT in 24 Hours (Optometry)

PCAT in 24 Hours (Pharmacy)

Nursing Entrance Exams

Certification in 24 Hours

eBook - Survival Kits

Audiobooks (MP3)


 Tell-A-Friend:
Have friends taking science and math courses too? Tell them about our rapid learning system.


Enzyme Catalysis and Kinetics

Topic Review on "Title":

Enzyme catalysis
Enzymes act by lowering the activation energy. They do not change the equilibrium of the reactions. Enzyme binds with the substrate to form an unstable complex which breaks up into products liberating enzymes. Lock and key theory and induced fit theory explain the enzyme-substrate complex formation. Small region on the enzyme where the substrate binds and catalysis takes place is called an active site. Enzymes are highly specific in their action. Three types of enzyme specificity are well recognized: They are stereo specificity, reaction specificity and substrate specificity. There are different mechanisms to explain enzyme catalysis. Different mechanisms are: acid base catalysis, covalent catalysis and metal ion catalysis and transition state stabilization.

Enzyme kinetics
Various factors like concentration of substrate, pH and product concentration of products affect enzyme activity. Michaelis-Menten kinetics is based on substrate concentration. When a graph is plotted for substrate concentration [S] on x-axis and velocity [V] on the y axis, a rectangular hyperbola is obtained. A linear plot that is obtained by rearranging the M-M equation is called Lineweaver-Burk plot or double reciprocal plot. Km value is the substrate concentration at half maximal velocity of an enzyme catalyzed reaction. Enzymes having many subunits may not strictly follow the M-M kinetics. Chemical substances which inhibit enzyme activity and reduce velocity of an enzyme catalyzed reaction are known as inhibitors. Enzyme inhibition is broadly classified into reversible and irreversible inhibition. Reversible inhibition is further divided into competitive, non competitive and uncompetitive inhibition. Suicide inhibition is a reversible inhibition.
 
Regulatory Properties of Enzymes
In each enzyme system, there is at least one enzyme that catalyzes the rate limiting reaction. It is known as a regulatory enzyme. There are two major classes: Allosteric enzymes acting through reversible, non covalent modulator. Enzymes regulated by reversible covalent modification. The allosteric sites are different from its active site. Feedback inhibition is the best example for allosteric modulation. Localization of enzymes related to one pathway partly in mitochondria and partly in cytosol is called compartmentation. Ribozymes are the enzymes made of RNA.


Rapid Study Kit for "Title":
Flash Movie Flash Game Flash Card
Core Concept Tutorial Problem Solving Drill Review Cheat Sheet

"Title" Tutorial Summary :

Enzymes act by lowering the activation energy. They do not change the equilibrium of the reactions. Enzyme binds with the substrate to form an unstable complex which breaks up into products liberating enzymes. Small region on the enzyme where the substrate binds and catalysis takes place is called an active site. Enzymes are highly specific in their action. There are different mechanisms to explain enzyme catalysis. Various factors like concentration of substrate, pH and product concentration of products affect enzyme activity. Michaelis-Menten kinetics is based on substrate concentration. Enzyme inhibition is broadly classified into reversible and irreversible inhibition. Enzymes do have regulatory properties. Ribozymes are the enzymes made up of RNA.


Tutorial Features:
  • Concept map to show the factors influencing the rate of biochemical reactions and mechanism of catalysis.
  • Michaelis-Menten theory and hypothesis explained with animations.
  • Enzyme specificities are discussed with suitable reactions and examples.
  • Enzyme kinetics plots are animated and easy to understand.
  • Regulation of enzyme activity is explained with interesting examples.

"Title" Topic List:

Enzyme Catalysis

  • Introduction
  • Mechanism of enzyme action
  • Enzyme-substrate complex and active site
  • Enzyme specificity
  • Mechanisms of catalysis

Enzyme Kinetics

  • Factors affecting enzyme activity
  • Michaelis-Menten kinetics
  • Inhibition

Regulatory Properties of Enzymes

  • Introduction
  • Irreversible covalent activation
  • Reversible covalent modification
  • Allosteric modulation
  • Compartmentation
  • Ribozymes


See all 24 lessons in college chemistry, including concept tutorials, problem drills and cheat sheets:
Teach Yourself Biochemistry Visually in 24 Hours

© 2014 Rapid Learning Inc. All rights reserved         Disclaimer | Privacy Policy | Affiliates