Enzyme Catalysis SBS017 Basic Biochemistry Dr John Puddefoot

Slides:

Advertisements

Similar presentations

Enzymes and Coenzymes I Dr. Sumbul Fatma Clinical Chemistry Unit Department of Pathology.

Advertisements

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

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.

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

Enzymes Have properties shared by all catalysts Enhance the rates of both forward and reverse reactions so equilibrium is achieved more rapidly Position.

Enzymes 2 nd Year Dentistry By Eman Mokbel Alissa, Ph.D.

Enzymes: increase the rates of reactions are highly specific for their preferred substrate Can be regulated can be localized in certain organelles Can.

Lecture 15 Tuesday 3/4/08 Enzymes Michealis-Menten Kinetics Lineweaver-Burk Plot Enzyme Inhibition.

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

Enzyme Catalysis (26.4) Enzymes are catalysts, so their kinetics can be explained in the same fashion Enzymes – Rate law for enzyme catalysis is referred.

Medical Enzymology By Amr S. Moustafa, M.D.; Ph.D. Assistant Prof. & Consultant, Medical Biochemistry Dept. College of Medicine, KSU

Medical Enzymology By Amr S. Moustafa, M.D.; Ph.D. Assistant Prof. & Consultant, Medical Biochemistry Dept. College of Medicine, KSU

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.

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

The Behavior of Proteins: Enzymes

LEHNINGER PRINCIPLES OF BIOCHEMISTRY

Molecule, Gene, and disease Sun. 2 – 3 – 2014 Session 3 Enzymes and enzyme regulation Dr. Muna A. R.

Chapter 6.3: Enzyme Kinetics CHEM 7784 Biochemistry Professor Bensley.

23.6 Enzymes Three principal features of enzyme-catalyzed reactions: 1. For a given initial concentration of substrate, [S] 0, the initial rate of product.

Enzyme Kinetics and Inhibition

Enzymes (If you don’t have the energy, we can help!)

SURVEY OF BIOCHEMISTRY Enzyme Kinetics and Inhibition

Lecture 6: Kumar Measuring enzyme activity 1. Effect of pH on enzyme activity 2.

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

Experiment4 Effects of substrate concentration on enzyme activity ——determination of Km of alkaline phosphatase ）

ENZYME INHIBITION Studies on Inhibitors are useful for:Studies on Inhibitors are useful for: Mechanistic studies to learn about how enzymes interact with.

ENZYME KINETICS. catalyzed uncatalyzed Formation of product is faster in the catalyzed reaction than in the uncatalyzed reaction and initially is linear.

Prof. R. Shanthini 23 Sept 2011 Enzyme kinetics and associated reactor design: Determination of the kinetic parameters of enzyme-induced reactions CP504.

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

Lecture – 4 The Kinetics of Enzyme-Catalyzed Reactions Dr. AKM Shafiqul Islam School of Bioprocess Engineering University Malaysia Perlis

E + S ES P + E k2k2 v o = k 2 (ES) Michaelis reasoned that If k 2 is the smallest rate constant, the overall velocity of the reaction is Problem: We cannot.

Lab: principles of protein purification

Michaelis-Menten kinetics

Enzyme Kinetics Velocity (V) = k [S]

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)

Mechanisms of enzyme inhibition

Biochemical Reaction Rate: Enzyme Kinetics What affect do enzymes and enzyme inhibitors have on enzyme catalysis on a quantitative level? Lipitor inhibits.

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.

Enzymes Biological Catalysts. Activation Energy Why don’t thermodynamically favorable reactions occur without the aid of enzymes?

Lecture 5:Enzymes Ahmad Razali Ishak

Key topics about enzyme function:

Interpretation of Michaelis Menten Equation. Michaelis-Menten  Graphically representation:

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

Enzyme kinetics & Michaelis-Menten Equation Abdul Rehman Abbasi MSc Chemistry Semester – I Preston University Isb.

Many factors influence the activity of an enzyme

Enzyme Kinetics II 10/16/2008.

Bioreactors Engineering

Lecture 15 Chemical Reaction Engineering (CRE) is the field that studies the rates and mechanisms of chemical reactions and the design of the reactors.

Lab 7 An Investigation of Enzymes and the Rate of Reactions Using a

ENZYME INHIBITION.

Enzymes II:kinetics Dr. Nabil Bashir.

Lecture 15 Chemical Reaction Engineering (CRE) is the field that studies the rates and mechanisms of chemical reactions and the design of the reactors.

Chapter 6 CHM 341 Fall 2016 Suroviec.

(BIOC 231) Enzyme Kinetics

Chapter Three: Enzymes

Chapter Three: Enzymes

Enzymes and coenzymes II

ENZYME Enzyme Reaction Energy of reaction Factors affect rate Other.

Enzyme Kinetics Nilansu Das Dept. of Molecular Biology

Lecture 15 Chemical Reaction Engineering (CRE) is the field that studies the rates and mechanisms of chemical reactions and the design of the reactors.

Lecture 15 Chemical Reaction Engineering (CRE) is the field that studies the rates and mechanisms of chemical reactions and the design of the reactors.

Presentation transcript:

Enzyme Catalysis SBS017 Basic Biochemistry Dr John Puddefoot

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

Michaelis-Menten Reminder V is the velocity (or rate) of reaction [S] is the substrate concentration Vmax is the maximal velocity of the reaction K M is the Michaelis constant ([S] at Vmax/2)

K +1 [E][S] = k -1 + k 2 [ES]

App