1. Enzymes are biological catalysts that increase the rate of chemical reactions in living organisms and in vitro. They are typically proteins but some are RNA molecules called ribozymes.
2. Enzymes lower the activation energy needed for chemical reactions to occur by binding to reactants and transition states. This allows reactions to proceed more quickly under mild conditions.
3. Enzymes achieve catalysis through their three-dimensional structures, and some require non-protein cofactors like vitamins and inorganic ions to function optimally.
1. Enzymes are biological catalysts that increase the rate of chemical reactions in living organisms and in vitro. They are typically proteins but some are RNA molecules called ribozymes.
2. Enzymes lower the activation energy needed for chemical reactions to occur by binding to reactants and transition states. This allows reactions to proceed more quickly under mild conditions.
3. Enzymes achieve catalysis through their three-dimensional structures, and some require non-protein cofactors like vitamins and inorganic ions to function optimally.
1. Enzymes are biological catalysts that increase the rate of chemical reactions in living organisms and in vitro. They are typically proteins but some are RNA molecules called ribozymes.
2. Enzymes lower the activation energy needed for chemical reactions to occur by binding to reactants and transition states. This allows reactions to proceed more quickly under mild conditions.
3. Enzymes achieve catalysis through their three-dimensional structures, and some require non-protein cofactors like vitamins and inorganic ions to function optimally.
1. Enzymes are biological catalysts that increase the rate of chemical reactions in living organisms and in vitro. They are typically proteins but some are RNA molecules called ribozymes.
2. Enzymes lower the activation energy needed for chemical reactions to occur by binding to reactants and transition states. This allows reactions to proceed more quickly under mild conditions.
3. Enzymes achieve catalysis through their three-dimensional structures, and some require non-protein cofactors like vitamins and inorganic ions to function optimally.
Enzymology Presented by Prof Dr. Suzan M .AbdEl -Tawab Salama Biochemistry Department Faculty of Medicine Hail University (1) Lecture Aims ❖ By the end of this lecture you will be able to:- • Summarize the importance of enzymes in many aspects in health and disease • Describe general properties of enzyme molecule and the process of enzyme catalysis • Define terms used in enzymology • Compare and contrast between enzymes and inorganic catalysts • Identify the nomenclature of enzymes • Outline the classification of enzymes • Distinguish the different types of enzyme specificity Enzymes Enzymes are biological materials with catalytic properties.
Enzymes increase the rate of chemical reactions in
biological and in vitro (in the laboratory) system. ❖ Biochemical nature of enzyme All enzymes are proteins except a small group of RNA molecules, ribozymes, which act as enzymes catalyzing the cleavage and synthesis of phosphodiester bond in RNA molecules.
Enzymes are distinguished from other proteins that are not
enzymes by their catalytic action.
The catalytic behaviour of any enzyme is dependent on the
primary, secondary, tertiary and quaternary structure of the protein molecule.
Changes in any one of their structures can affect the
enzymatic activity of the protein. catalyst
enzyme 1- Enzymes, are the catalysts of biological systems. They mediate the transformation of one form of energy into another.
2- All known enzymes are proteins (except ribozymes).
3- Enzymes have a high degree of specificity both for the
types of reaction catalyzed and for their substrates.
4- They accelerate specific chemical reaction without
formation of by-products, and they function in dilute aqueous solutions under very mild conditions of temperature and pH. enzyme
Almost all enzymes are make up of proteins
❖ Ribozymes (Catalytic RNAs):- 1- Ribozymes are the RNA molecules that can act as catalysts. 2- Ribozymes cleave RNA phosphodiester bonds at specific sites in the RNA molecular, serving as ribonucleases and as peptidyl transferase, the enzyme in protein synthesis that catalyzes the formation of peptide bond.
❖ Clinical importance of Ribozyme:-
Ribozymes are therapeutic agents for disorders that caused by the inappropriate expression of an RNA or the expression of a mutated RNA. ❖ Zymogen or Proenzyme or Precursor enzyme:- 1- A number of proteolytic enzymes found in the blood or in the digestive tract are present in an inactive (precursor) form, called Zymogen or Proenzymes, which must be cleaved to be activated.
2- Their synthesis in a zymogen or proenzyme (inactive)
form prevents them from catalyzing reactions in the cell where they are synthesized.
3- For example, chymotrypsin is secreted by the pancreas as
chymotrypsinogen. It is activated in the digestive tract by the proteolytic enzyme trypsin, which cleaves off a small peptide from N-termianl region of chymotrypsinogen. 4- The cleavage changes the conformation of the enzyme and creates a binding site for the substrate.
5- Precursor proteins or inactive enzyme names have the
prefix “pro” like prothrombin, proelastase, ect. Or suffix “ogen” like chymotrypsinogen, trypsinogen, pepsinogen, which are produced and stored as inactive proenzymes or zymogen form. ❖ Cofactors (Coenzyme and activator):- Some enzymes require an additional non-protein chemical component for its optimum activity. This additional component is called cofactor which may be either loosely or tightly bound to the protein portion of the enzyme.
These cofactors may be either:-
1- Organic compounds, called coenzymes. 2- Inorganic ions, called activators. Mg+2 Glucose +ATP Glucose-6-Phosphate Hexokinase Enzymes without its cofactor is called apoenzyme. The complete catalytically active enzyme is called holoenzyme.
• Apoenzyme + cofactor = holoenzyme.
The lists of coenzyme and activators are given in Tables 1
and 2 respectively. Coenzymes function as transient carriers of specific functional groups. Many vitamins are precursors of coenzymes. NADH+ H+ NAD+
Pyruvate Lactate Lactate dehydrogenase Coenzymes: ❖ Table 1:- Some common coenzymes and their functions Vitamin Coenzyme Function Thiamine (Vit B1) TPP (Thiamine pyrophosphate) Oxidative decarboxylation and transketolase reaction Riboflavin (Vit B2) FAD and FMN (Flavin Adenine Oxidation and reduction Dinucleotide and Flavin reactions Mononucleotide) Niacin NAD (Nicotinamide Adenine Oxidation and reduction Dinucleotide), reactions NADP (Nicotinamide Adenine Dinucleotide Phosphate) Pyridoxine (Vit B6) PLP (Pyridoxal phosphate) Transamination, deamination dexcarboxylation reactions of amino acids. Biotin Biocytin Carboxylation reactions
Folic acid THF (Tetrahydrofolate) Carrier of one carbon group
❖ Table 2:- Enzymes requiring or containing inorganic elements as cofactors (activators):- Enzyme Cofactor (activator) Ferroxidase (ceruloplasmin), copper Tyrosinase Ascorbic acid oxidase, Carbonic anhydrase, Zinc DNA-polymerase, RNA-polymerase, Porphobilinogen synthase, Carboxipeptidase, Alcohol dehydrogenase. Cytochrome oxidase, Iron Catalase, peroxidase. Gluose-6-Phosphatase, Magnesium Hexokinase. Glutathione peroxidase Selenium ❖ Localization of Enzymes:-
Enzymes are located either:-
I- Intracellularly. II- Extracellularly. ❖ I- Intracellularly Enzymes: Many enzymes are localized in specific organelles within cell.
Figure 1:- The intracellular location of some important
pathway ❖ II- Extracellular Enzymes:- Extracellular enzymes are secreted out from the cell and function outside the cell origin, consist of digestive enzymes.
❖ For example:- α- Amylase secreted by salivary glands. Pepsin and rennin secreted by gastric glands. Lipase, trypsin, chymotrypsin, α-amylase secreted by pancreas. Aminopeptidase, dipeptidase, lactase, sucrase, maltase isomaltase are secreted by intestinal glands. ❖ How Enzymes work Energy changes occur during the reaction.
All chemical reactions have an energy barrier, separating
the reactants and the products.
This barrier, called the free energy of activation, “is the
energy difference between the energy of the reactant and high energy intermediates that occurs during the formation of a product”. Figure 2:- shows the changes in energy during the conversion of a molecule of reactant (S) to product (P) through the transition state S*.
S S* P (Reactant) (Product) Figure 2:- comparison of the free Energy of Activation of a Catalysed and Uncatalysed Reaction, S*= Transition State. The peak of free energy activation, represents the transition state, in which the high energy intermediates (S*) are formed during the conversion of a reactant to a product.
Because of activation energy, the rates of uncatalysed
chemical reactions are slow.
An enzyme lowers the energy required for activation to the
transition state.
Without a catalyst, the reaction will occur only if enough
heat energy is added to the reaction system.
With an enzyme as a catalyst, the reaction may easily
