Enzymes are globular proteins that catalyze biochemical reactions. They have complex 3D structures and function to greatly accelerate reactions by lowering activation energy. Enzymes are highly specific and function optimally at physiological temperatures, pH levels, and ion concentrations. The mechanisms of enzyme action can be explained by either the lock and key or induced fit models, where the substrate binds and induces a conformational change in the active site for catalysis. Enzymes are classified based on the type of reaction catalyzed according to the IUB system.
Enzymes are globular proteins that catalyze biochemical reactions. They have complex 3D structures and function to greatly accelerate reactions by lowering activation energy. Enzymes are highly specific and function optimally at physiological temperatures, pH levels, and ion concentrations. The mechanisms of enzyme action can be explained by either the lock and key or induced fit models, where the substrate binds and induces a conformational change in the active site for catalysis. Enzymes are classified based on the type of reaction catalyzed according to the IUB system.
Enzymes are globular proteins that catalyze biochemical reactions. They have complex 3D structures and function to greatly accelerate reactions by lowering activation energy. Enzymes are highly specific and function optimally at physiological temperatures, pH levels, and ion concentrations. The mechanisms of enzyme action can be explained by either the lock and key or induced fit models, where the substrate binds and induces a conformational change in the active site for catalysis. Enzymes are classified based on the type of reaction catalyzed according to the IUB system.
Enzymes are globular proteins that catalyze biochemical reactions. They have complex 3D structures and function to greatly accelerate reactions by lowering activation energy. Enzymes are highly specific and function optimally at physiological temperatures, pH levels, and ion concentrations. The mechanisms of enzyme action can be explained by either the lock and key or induced fit models, where the substrate binds and induces a conformational change in the active site for catalysis. Enzymes are classified based on the type of reaction catalyzed according to the IUB system.
• All enzymes are globular proteins. They have complex 3ry or 4ry structure in nature. • With the exception of self-splicing ribosomal RNA, all other enzymes are protein in nature. o The substance acted upon by the enzyme. In-vivo reactions the energy barrier separates the reactants and products (so preventing spontaneous uncontrolled reactions). • Enzymatic reactions are 103 to 1017 times faster than the corresponding un–catalyzed reactions. Enzymes are superior to other catalysts in several ways
1. Enzymes act at physiological temperatures.
2. Enzymes act in low ionic strength solution. 3. Enzymes act at near neutral pH. 4. Enzymes are highly specific with varying degrees of specificity. 5. The activity of enzymes is closely regulated, whereas the catalyst is difficulty to control. 6.
Carbonic anhydrase catalysis the hydration of 106 CO2 molecules
per second which is 107 faster than spontaneous hydration. 1 2 3 4 Enzyme Nomenclature 5. The International Union of Biochemistry (IUB) developed a system of nomenclature in which enzymes are divided into six major groups each with numerous sub-classes:
• The suffix “-ase” is attached to a fairly complete
description of the chemical reaction catalyzed, e.g.:
• The IUB names are informative, but are sometimes too
cumbersome ( )ثقيلto be of general use. IUB Classification of Enzymes No Group Name Type of Reaction Catalyzed
1 Oxidoreductases Oxidation–Reduction Reactions
2 Transferases Transfer of functional groups
3 Hydrolases Hydrolysis reactions
Addition to double bonds or its 4 Lyases reverse 5 Isomerases Isomerization reactions Ligases or Formation of bonds with ATP 6 Synthases cleavage into AMP + P~P. Chemical Structure of Enzymes • Enzymes are divided chemically into:
1. Simple protein enzymes: consisting only of proteins,
e.g. digestive enzymes: pepsin, maltase, etc...
2. Conjugated protein enzymes (Holoenzymes):
consisting of a protein part and a non–protein part.
• The protein part of the enzyme is heat labile and
known as apoenzyme.
• The non–protein part of the enzyme: Co–factor.
The non–protein part (Co–factor) can be:
A. Coenzymes (Co–substrate): • They are non–protein, dialyzable, thermolabile, organic part and loosely attached to the protein part.
• It comes in full contact during the
activity of the enzyme.
• Coenzymes are vitamins or vitamin
derivatives and help enzyme catalysis. The non–protein part (Co–factor) can be:
B. Prosthetic Group: • It is an inorganic metal which is firmly attached to the protein part. It is part of enzyme structure. e.g.:
1. Ascorbic acid oxidase contains copper.
2. Carbonic anhydrase & Matrix metalloproteinases
(MMPs) contain zinc.
3. Super oxide dismutase contains copper and zinc.
4. Cytochrome oxidase contains iron.
Forms of Enzymes
1. Zymogens. 2. Zymase. 3. Isoenzymes. Forms of Enzymes 1. Zymogens (Pro-enzymes or Pre-enzymes):
• Enzymes secreted as inactive form especially
proteolytic enzymes.
a) They are extracellularly.
b) Inactive to prevent destruction of the proteins of the cells that synthesize them.
• The activation may involve the removal of a
polypeptide chain that is blocking or masking the active site of the apoenzyme. Activation of Gastric Zymogen 1 Proton activation: H+ Pepsinogen Pepsin + Peptide (Proton)
Carboxypeptidase + Peptides Trypsin Proelastase Elastase + Peptide Forms of Enzymes
2. Zymase:
• An enzyme that is secreted ready for
action, such as salivary amylase (Ptyalin).
3. Isoenzymes or isozymes:
• Enzymes that catalyze the same reaction
but differ in their physical properties, chemical structure and activity, i Lactate Dehydrogenase (LDH) Lactate Dehydrogenase (LDH) Lactate DH in Heart & Muscles Heart (H4) Muscle (M4) LD1 LD5 H H M M H H M M Lactate DH in different tissues H3M H2M2 HM3 LD2 LD3 LD4 H H H H H M H M M M M M Absolute 1 2. Group Specificity • Group or Relative specificity: The enzyme acts on substances which are "similar" in structure & posses the same type of bonds.
a) Lipase which hydrolyzes ester bonds of lipids
(Fatty acid with alcohol).
b) Trypsin hydrolyzes peptide bond whose –COOH
group belongs to one of the basic amino acids only, (Tryptic fragments). 2
C- b) Enzyme Specificity 3. Absolute specificity: The enzyme acts on ONE substrate only e.g. arginase, histidase, urease, uricase, sucrase, maltase, lactase. 4. Dual Specificity • The enzyme may act upon:
