Chapter 6.3: Enzyme Inhibition CHEM 7784 Biochemistry Professor Bensley.

Slides:

Advertisements

Similar presentations

Enzymes, con't.. Substrate Activation (catalytic mechanisms) Strain on substrate –Weakens bonds –Makes more accessible for reaction Acid/base catalysis.

Advertisements

Enzyme Kinetic Zhi Hui.

Chapter 7 Chem 341 Suroviec Fall I. Introduction The structure and mechanism can reveal quite a bit about an enzyme’s function.

Biochemistry Lecture 8.

Enzyme Kinetics. Rate constant (k) measures how rapidly a rxn occurs AB + C k1k1 k -1 Rate (v, velocity) = (rate constant) (concentration of reactants)

Chapter 8: Enzymes: Basic Concepts and Kinetics Copyright © 2007 by W. H. Freeman and Company Berg Tymoczko Stryer Biochemistry Sixth Edition.

Lecture 2 August 3, 2005 Lehninger (4 th Edition), Chapter 6,

Medical Biochemistry, Lecture 24

Chapter 5 (part 3) Enzyme Kinetics (cont.). Michaelis-Menton V max K m K cat K cat /K m E + S ESE + P k1k1 k -1 k cat Vo = Vmax [S] Km + [S] V max K m.

Enzyme Kinetics Chapter 8. Kinetics Study of rxn rates, changes with changes in experimental conditions Simplest rxn: S P –Rate meas’d by V = velocity.

Multi-Substrate Enzyme Kinetics

Enzyme Kinetics and Catalysis II 3/24/2003. Kinetics of Enzymes Enzymes follow zero order kinetics when substrate concentrations are high. Zero order.

Chemical Reaction Engineering (CRE) is the field that studies the rates and mechanisms of chemical reactions and the design of the reactors in which they.

Inhibited Enzyme Kinetics Inhibitors may bind to enzyme and reduce their activity. Enzyme inhibition may be reversible or irreversible. For reversible.

Enzyme activity is measured by the amount of product produced or the amount of substrate consumed. The rate of the enzymatic reaction is measured by the.

Deriving Kinetic Parameters & Rate Equations for Multi-Substrate Systems.

Enzyme Kinetics - Inhibition. Types of Inhibition Competitive Inhibition Noncompetitive Inhibition Uncompetitive Inhibition Irreversible Inhibition.

ENZYME KINETIC M. Saifur R, PhD. Course content  Enzymatic reaction  Rate of Enzyme-Catalyzed Reactions  Quatification of Substrate Concentration and.

The Behavior of Proteins: Enzymes

HOW ENZYMES WORK. ENZYMES SPEED UP CHEMICAL REACTIONS Enzymes are biological catalysts – substances that speed a reaction without being altered in the.

LEHNINGER PRINCIPLES OF BIOCHEMISTRY

Chapter 6.3: Enzyme Kinetics CHEM 7784 Biochemistry Professor Bensley.

Properties of Enzymes Catalyst - speeds up attainment of reaction equilibrium Enzymatic reactions to faster than the corresponding uncatalyzed.

Kinetics of Enzyme Reactions Srbová Martina. E + S ES E + P k1k1 k -1 k cat rapid reversible reaction slow irreversible reaction Rate of the conversion.

SURVEY OF BIOCHEMISTRY Enzyme Kinetics and Inhibition

LECTURE 2: ENZYME KINETICS. 1.A catalyst lowers energy of activation by providing a different mechanism for the reaction. Both the rates of forward and.

Why study enzyme kinetics?  To quantitate enzyme characteristics  define substrate and inhibitor affinities  define maximum catalytic rates  Describe.

Steady-State Enzyme Kinetics Scott Morrical B407 Given Bldg. General References: Textbook: Frey & Hegeman, Chapter 2, pp Reserve:

CHMI E.R. Gauthier, Ph.D. 1 CHMI 2227E Biochemistry I Enzymes: - Inhibition.

Lecture 7-Kumar Enzyme Inhibition-Drug Discovery Aspirin (anti-inflammatory) Penicillin (effective against gram positive bacteria) Sulfonamides (anti-diarrhea)

Biochemistry Lecture 8. Why Enzymes? Higher reaction rates Greater reaction specificity Milder reaction conditions Capacity for regulation Metabolites.

Allosteric Enzymes • Allosteric enzymes have one or more allosteric sites • Allosteric sites are binding sites distinct from an enzyme’s active site or.

BIOCHEMISTRY REVIEW Overview of Biomolecules Chapter 6 Enzymes.

Paul D. Adams University of Arkansas Mary K. Campbell Shawn O. Farrell Chapter Six The Behavior of Proteins:

Multi-Substrate Systems

Enzyme Inhibition C483 Spring Questions 1. An inhibitor binds to a site other than the active site of the enzyme. Which statement below correlates.

A Lock-and-Key Enzyme Animation. Enzyme Substrate Active Site.

Enzyme Catalysis SBS017 Basic Biochemistry Dr John Puddefoot

Enzyme Kinetics Chapter 6. Kinetics Study of rxn rates, changes with changes in experimental conditions Simplest rxn: S  P –Rate meas’d by V = velocity.

LECTURE 4: Reaction Mechanisms and Inhibitors Reaction Mechanisms A: Sequential Reactions All substrates must combine with enzyme before reaction can.

Enzyme Kinetics.

Draw sketch graphs for enzyme activity with a competitive inhibitor present and for a non-competitive inhibitor present.

Rmax and Km (26.4) Constants from Michaelis-Menten equation give insight into qualitative and quantitative aspects of enzyme kinetics Indicate if enzyme.

R max and K m (26.4) Constants from Michaelis-Menten equation give insight into qualitative and quantitative aspects of enzyme kinetics Constants – Indicate.

Enzyme Inhibition (26.4) Inhibition is a term used to describe the inability of a product being formed due to the presence of another substance (the inhibitor)

Biochemistry 412 Enzyme Kinetics II April 1st, 2005.

6.1 A Brief Look at Enzyme Energetics and Enzyme Chemistry Converting substrates to product requires intermediate states – Intermediates are less stable.

Inhibition is a process by which the enzyme activity is regulated or controlled or stopped To inhibit means to stop enzyme activity Enzyme inhibition.

Enzyme Kinetics Sadia Sayed. What is Enzyme Kinetics?  Kinetics is the study of the rates at which chemical reactions occur  Then what is Enzyme Kinetics?

Lecture 5:Enzymes Ahmad Razali Ishak

Key topics about enzyme function:

Bi-substrate Enzyme Kinetics

1 Chapter 3 - Enzymes. 2 Enzyme Inhibition Enzyme can be inhibited by inhibitors. Inhibitors are tools to scientists to understand enzymes. Inhibitors.

Enzyme Activators Substances that bind with the enzyme and increase its activity.

THE EFFECT OF INHIBITORS (INORGANIC PHOSPHATE & SODIUM FLUORIDE) ON THE RATE OF AN ENZYME CATALYZED REACTION 322 BCH EXP (8)

References for Multi-Substrate Enzyme Kinetics On-line:

Enzyme Kinetics provides Insight into

Many factors influence the activity of an enzyme

Enzyme Kinetics II 10/16/2008.

Bioreactors Engineering

ENZYME INHIBITION.

Graphs to show the effects of Inhibitors on Enzyme Action

Enzymes Department of Biochemistry Foundation Module – Phase: 1.

Chapter Three: Enzymes

Lehninger Principles of Biochemistry

Chapter Three: Enzymes

Lecture 8 Enzyme Kinetics

Do Now Take out your: Vocabulary notes + Toothpickase lab

Enzyme Kinetics Nilansu Das Dept. of Molecular Biology

Presentation transcript:

Chapter 6.3: Enzyme Inhibition CHEM 7784 Biochemistry Professor Bensley

CHAPTER 6.3 Enzyme Inhibition –Various types of enzyme inhibition Today’s Objectives: (To learn and understand the)

Enzyme Inhibition Inhibitors are compounds that decrease enzyme’s activity Irreversible inhibitors (inactivators) react with the enzyme Reversible inhibitors bind to, and can dissociate from the enzyme Reversible inhibitor can bind: –To the free enzyme and prevent the binding of the substrate –To the enzyme-substrate complex and prevent the reaction

Competitive Inhibition Lines intersect at the y-axis

Uncompetitive Inhibition Lines are parallel

Mixed Inhibition Lines intersect left of the y-axis MAKE SURE YOU DISTINGUISH THIS FROM NON- COMPETITIVE INHIBITION!!!!

Viagra (Sildenafil Citrate) Medicinal Inhibitor Example

Irreversible Inhibitors Diisopropyl fluorophosphate (nerve gas) parathion malathion Organophosphates Inhibit serine hydrolases Acetylcholinesterase inhibitors

Kinetics of Multisubstrate Reactions E + A + B E + P + Q Sequential Reactions (Ternary Complex formed) a) Random b) Ordered Ping-Pong Reactions

Sequential Reactions EEA(EAB) (EPQ) EQ E AB P Q AB PQ AB E EA EB (EAB)(EPQ) P Q EQ EP E Ordered Random

Ping-Pong Reactions E (EA)(FP) (F) (FB)(EQ) E ABPQ In Ping-Pong rxns first product released before second substrate binds When E binds A, E changes to F When F binds B, F changes back to E

Lineweaver-Burke Plot of Multisubstrate Reactions Increasing [B] Increasing [B] Sequential Ping-Pong Vmax doesn’t change Km changes Both Vmax & Km change 1/Vo 1/[S] 1/Vo 1/[S]