Enzyme catalysis
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Enzyme kinetics is the study of chemical reactions catalyzed by enzymes. The reaction rate is measured under varying conditions to investigate the catalytic mechanism of the enzyme. The Michaelis-Menten model describes enzyme kinetics as a two-step process where the substrate forms a reversible enzyme-substrate complex that then decomposes into products. This model derives the Michaelis-Menten equation which relates reaction rate to substrate concentration and defines kinetic parameters like the Michaelis constant Km and maximum reaction rate Vmax.
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D07 abbrev arrhenius and catalysts_alg
This document discusses the effects of temperature on reaction rates and provides an explanation using collision theory and activation energy. It introduces the Arrhenius equation and shows how to use it to determine activation energy from rate constants measured at different temperatures. Catalysts are discussed as lowering the activation energy of reactions without being consumed. Enzymes are described as biological catalysts that regulate metabolic reaction speeds. An example problem determines activation energy for a temperature-dependent firefly flashing process using rate data.
Enzyme kinetics
Enzyme kinetics is the study of reaction rates catalyzed by enzymes. Michaelis and Menten developed an equation to describe enzyme kinetics based on the assumptions that enzyme-substrate complexes form rapidly and at steady state. The Michaelis-Menten equation relates reaction rate to substrate concentration and can be linearized using double reciprocal plots. Enzyme kinetics are affected by factors like pH, temperature, and substrate concentration, and some enzymes use two substrates in either sequential or double displacement mechanisms.
Enzymes 2
Enzymes catalyze biochemical reactions and are characterized by their catalytic activity. The document discusses several key aspects of enzyme mechanisms and kinetics, including:
1) Enzymes have an active site that binds substrates and facilitates chemical reactions through proximity, orientation, and catalytic groups like metal ions or amino acid residues.
2) Michaelis-Menten kinetics describe the relationship between substrate concentration, reaction rate, and parameters like Vmax and Km.
3) Common metalloenzymes contain catalytic metal ions like zinc, copper, iron and manganese that participate in redox reactions.
Chemical kinetics
1. Chemical kinetics deals with the rates of chemical reactions and factors that affect reaction rates. It examines how fast reactions occur and the mechanisms of reactions.
2. Reaction rates can vary significantly, from fractions of seconds to years. Third-order reactions involve three molecules and are also called termolecular reactions.
3. The rate of a reaction is affected by temperature - higher temperatures provide more energy and increase reaction rates by producing more effective collisions between reactant molecules.
Lect w3 152_d2 - arrhenius and catalysts_alg (1)
The document summarizes key concepts about the effects of temperature and catalysts on reaction rates:
1) Increasing temperature generally increases reaction rate because more molecules have enough energy to overcome the activation energy barrier.
2) Catalysts speed up reactions by lowering the activation energy needed, allowing reactions to occur more quickly via a different mechanism.
3) Enzymes are biological catalysts that regulate metabolic reactions in living organisms and act to reduce activation energies.
Enzyme Kinetics and thermodynamic analysis
Introduction
Kinetics and thermodynamicSG
Thermodynamic in enzymatic reactions
balanced equations in chemical reactions
changes in free energy determine the direction & equilibrium state of chemical reactions
the rates of reactions
Factors effecting enzymatic activity
(i) Enzyme concentration.
(ii) Substrate concentration.
(iii)Temperature
(iv) pH.
(v) Activators.
(vi)Inhibitors
Michaelis-menten equation
CONCLUSIONS
REFERENECES
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Enzyme catalysis
- 1. Enzyme Catalysis D. JIM LIVINGSTON FACULTY OF CHEMISTRY St. JOHN’S COLLEGE
- 2. ENZYMEKINETICS Enzyme kinetics is the study of the chemical reactions that are catalysed by enzymes. In enzyme kinetics, the reaction rate is measured and the effects of varying the conditions of the reactions are investigated. Enzyme kinetics reveals the catalytic mechanism of that enzyme, its role in metabolism, how its activity is controlled, and how a drug or an agonist might inhibit the enzyme.
- 3. MICHAELIS-MENTEN MODELFOR ENZYME KINETICS • Michaelis–Menten kinetics is one of the simplest and best- known models of enzyme kinetics. • This model explain how an enzyme can cause kinetic rate enhancement of a reaction and why the rate of a reaction depends on the concentration of enzyme present. Leonor Michaelis Maud Menten 1913 -Mech. Of Enzyme catalysis
- 5. • • Overall reaction is composed of two elementary reactions in which the substrate forms a complex with the enzyme that subsequently decomposes to products and enzymes. k1 k2 E + S ES P + E k-1 Here E, S, ES and P symbolize the enzyme, substrate, enzyme-substrate complex and products
- 6. • According to this model • When the substrate concentration becomes high enough to entirely convert the enzyme to the ES form, the second step of the reaction becomes rate limiting step. • The general expression of the (rate) of this reaction is 2 [ E S ] d t v d [ P ] k
- 7. Mechanism •Now: Based on steady state assumption, d[ES]/dt = 0 • d[ES]/dt = k1[E][S] –k-1[ES] – k2[ES] = 0 • • d[ES]/dt = k1{[E]0-[ES]}[S] –k-1[ES] – k2[ES] = 0 • k1[E]0[S]-K1[ES][S] –k-1[ES] – k2[ES] = 0 • k1[E]0[S]-K1[ES][S] = k-1[ES] + k2[ES] • k1[E]0[S] = k-1[ES] + k2[ES]+K1[ES][S] • k1[E]0[S] = {k-1+ k2+K1[S]}[ES] • [ES] = [E]0[S] k1/(k-1 + k2+K1[S]) [E]0 [E]+[ES] [E] [E]0 [ES] Enzyme conservation equation
- 8. Michaelis menten eqn. K1K2 [E]0[S] K-1+K2+K1[S] Dividing by K1, r = K2 [E]0[S] (K-1+K2)/K1+[S] r K2[E ]0[S] Km [S ] r Rate of the product formation r = K2 [ES] Km k1+K2 k1 Km – Michaelis constant
- 9. Plot of [S] vs rate If [E]0 = [ES] Then, rmax= K2[E]0 = Vmax Sub in MM eqn, r = Vmax[S] Km+[S] K2[E ]0[S] Km [S ] Rate of the product formation r = K2 [ES]
- 10. If Km = [S] Plot of [S] vs rate
- 11. MICHAELIS - MENTEN CONSTANT • It is the substrate concentration, [S] at which half maximum velocity of reaction is observed. • K m implies that half of the active sites on the enzymes arefilled. • It is the measure of the binding strength between substrate and the enzyme. (lower K m value indicates a strong affinity betweenthe substrate and enzymes. 40 M in 2 day 40 M in 12 days
- 12. Plot of [S] vs rate Case – I: If Km >>>> [S] Linear plot Case – II If [S] >>>> Km Plateau region First order Zero order
- 13. Vmax It is the maximum velocity of reaction or rate at which the enzyme catalyzed a reaction under given conditions. Vmax is reached when all enzyme sites are saturated with the substrate. This will happen when substrate concentration [S] is greater than K m.