Biochemistry Lecture 10 PDF

Summary

This document is a lecture on biochemistry covering enzyme kinetics. It explains factors affecting enzyme activity including substrate concentration, enzyme concentration, temperature and pH. It also discusses the concept of the Michaelis constant (Km) and enzyme inhibitors.

Full Transcript

Biochemistry Enzymes LECTURE (10) DR. El-Sawy 1 Biochemistry Enzymes 1. Enzyme concentra...

Biochemistry Enzymes LECTURE (10) DR. El-Sawy 1 Biochemistry Enzymes 1. Enzyme concentration 5. Time 2. Substrate concentration 6. Temperature 3. Concentration of coenzymes 7. pH 4. Concentration of ion activators 8. Inhibitors Coenzymes/ ion activators/ inhibitors S+E P+E PH/ temp/ time  Rate of enzyme action is directly proportional to enzyme concentration provided sufficient supply of substrate & constant conditions.. Enzyme concentration  Rate of reaction increases as the substrate concentration increases up to certain point at which the. Substrate reaction rate is maximal (Vmax.) concentration  At Vmax, enzyme is completely saturated with substrate, Then any increase in substrate concentration don't affect the reaction rate. DR. El-Sawy 2 Biochemistry Enzymes Michaelis constant (Km) : Definition:  Substrate concentration that produces 1/2 maximum velocity of enzyme (1/2 Vmax)  Km = 1/2 Vmax Enzymes with low Km Enzymes with high Km affinity  High affinity to substrate  Low affinity to substrate velocity  Maximal  Maximal substrate  low  high concentration  Hexokinase  Glucokinase Acts on glucose at low Acts on glucose at high Example concentration (fasting concentration (fed state). state) DR. El-Sawy 3 Biochemistry Enzymes  Rate of reaction increases gradually with ↑↑ in temperature until reach a maximum at optimum temperature (37-40°C).  After optimum temperature, the rate of reaction decrease due to denaturation of the enzyme (60-65°C).  The effect of temperature on reaction rate is due to: A. ↑ Initial energy of substrate →↓ activation energy. B. ↑ collision of molecules.. Temperature  In conjugated enzymes:. Coenzymes Concentration ↑↑ coenzyme concentration → ↑↑ reaction rate.  ↑↑ in metal ion activator → ↑↑ reaction rate.  Many enzymes are activated by ions : A. Chloride ion activate salivary amylase. Ion B. Calcium ion activate thrombokinase enzyme activators Concentration DR. El-Sawy 4 Biochemistry Enzymes  Each enzyme has an optimum PH at which its activity is maximal. Optimum PH of pepsin = 1.5-2 (Acidic) Optimum PH of pancreatic lipase = 7.5-8 (Alkaline) Optimum PH of salivary amylase = 6.8 (Slightly acidic). PH  Change of PH above or below optimum PH ↓ rate of enzyme action due to: 1. Change in PH will affect ionization state of both enzyme & substrate. 2. Marked change in PH will cause enzyme denaturation.  Rate of reaction is decreased by time.  Due to:. Time A. ↓↓ substrate concentration. B. Accumulation of products. C. Change in PH.  Presence of enzyme inhibitor → decreases or stops the enzyme activity.. Enzymes  Enzyme inhibitors may be: inhibitor 1- Competitive inhibitors. 2- Non competitive inhibitors. DR. El-Sawy 5 Biochemistry Enzymes DR. El-Sawy 6

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