By B. Ganzwa H. Gumbo L.

Chikomo

Properties of enzymes Types of enzymes Michaeli - Mentens equation Enzyme kinetics Lineweaver - Burke plot Eadie-Hofstee plot Enzyme inhibition Enzyme immobilisation

Louis Pasteur was among the first to study enzyme action in 1865. In 1897 the German biochemist Eduard Buchner (1860-1917) isolated the enzymes which catalyze alcoholic fermentation from living yeast cells

Enzymes are biological catalysts: this means that they speed up the chemical reactions in living things. Proteins in nature. A catalyst is any substance which makes a chemical reaction go faster, without itself being changed.

Specificity;- the main property which make the enzymes so important. 1. Absolute specificity - the enzyme will catalyze only one reaction. 2. Group specificity - the enzyme will act only on molecules that have specific functional groups, such as amino, phosphate and methyl groups
a)

3. Linkage specificity - the enzyme will act on a particular type of chemical bond regardless of the rest of the molecular structure. 4. Stereochemical specificity - the enzyme will act on a particular steric or optical isomer.

(b) Solubility: Enzymes as proteins are soluble in water or dilute salt solution (c)Molecular weight :Enzymes have Mw (varying from 10000 -several thousands) (d) Enzymes are charged molecules: Due to the presences of amino acids, each enzyme has a charge.

(e) Enzymes have buffering capacity (acid-base): They are amphoteric molecules i.e. behave both as acids and bases. (f)Denaturation: When proteins are heated , or subjected to extremes of temperature, high salt, organic solvents etc., the non-covalent bonds break, changing the native structure to random coil.

Many enzymes have been named by adding the suffix aseto the name of the substrate or to a word describing the action or activity: e.g. protease, sucrase, lipase, amylase, dehydrogenase, oxidase, carboxylase etc

developed a system of nomenclature: (i)The enzyme name has 2 parts: The First names the substrate or substrates. The Second ending in -ase, indicates the type of reaction catalyzed.

(ii)The system give each enzyme a code number (EC) [called Enzyme Commission numerical code] and it contains 4 digits separated by points: First digit : Class Second digit : Sub-class Third digit :sub-sub-class Fourth digit : Serial number of the enzyme

[on the basis of the nature of reaction catalyzed]

(1)Oxido-reductases- catalyse oxidation and reduction reactions (2)Transferases-transfer one group from donor to acceptor (3)Hydrolases-break bonds by adding water (4)Lyases-break bond but do not use water (5)Isomerases-change one isomer to another (6)Ligases-bring about formation of a bond (biosynthetic reactions)

Enzyme Action: Lock and Key Model

An enzyme binds a substrate in a region called the active site Only certain substrates can fit the active site Amino acid R groups in the active site help substrate bind Enzyme-substrate complex forms Substrate reacts to form product Product is released
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Lock and Key Model

P + S S + P

ES complex

P
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Enzyme Action: Induced Fit Model

Enzyme structure flexible, not rigid Enzyme and active site adjust shape to bind substrate Increases range of substrate specificity Shape changes also improve catalysis during reaction

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Enzyme Action: Induced Fit Model

P S S P

ES complex

P
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Factors Affecting Enzyme Action: Temperature

Little activity at low temperature Rate increases with temperature Most active at optimum temperatures (usually 37C in humans) Activity lost with denaturation at high temperatures

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Factors Affecting Enzyme Action : Temperature

Optimum temperature

Reaction Rate

Low High Temperature

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Factors Affecting Enzyme Action: Substrate Concentration

Increasing substrate concentration increases the rate of reaction (enzyme concentration is constant) Maximum activity reached when all of enzyme combines with substrate

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Factors Affecting Enzyme Action : Substrate Concentration

Maximum activity

Reaction Rate

substrate concentration
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Factors Affecting Enzyme Action: pH

Maximum activity at optimum pH R groups of amino acids have proper charge Tertiary structure of enzyme is correct Narrow range of activity Most lose activity in low or high pH

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Factors Affecting Enzyme Action : pH

Reaction Rate
Optimum pH

5 pH

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