Enzymes are

biologic catalysts.  Catalysts are substances that increase the speed of a chemical reaction by lowering the energy requirement.  Although a catalysts influences a chemical reaction, it is not itself permanently changed, nor does it cause the reaction to occur, that is, a catalysts can increase the speed of a reaction but cannot cause that reaction if it would not occur in the absence of that catalyst.  Since catalysts are not used up, can be used over and over again.

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Colloidal, thermo labile Protein in nature with large molecular weight Remarkable molecular devices that determine the pattern of chemical transformation Striking characteristic catalytic power specificity Accelerate reaction at least million to thrillion times

Substances on which enzymes act to convert them into product.

Energy of activation before a chemical

reaction can occur, the molecules are required to gain a minimum amount of energy. For enzymes it need lower activation energy.

Enzymes are highly specific with varying degrees of specificity. Some enzymes exhibit absolute specificity.


Absolute specificity they act on one substrate and only on that substrate. such enzymes can detect the difference between optical isomers (mirror images) and select only one or such isomers. Linkage specific they catalyze the reaction that breaks the bonds only between specific groups.

 Stereospecificity

 Reaction

specificity- they catalyze certain types of

reactions.
 Group

specificity- chymotrypsin catalyzes the hydrolysis of only those proteins that contain phenylalanine, tryptophan or tyrosine. The activity of enzymes is closely regulated, whereas that of catalysts is difficult to control. There are substances in cells that can increase or decrease the activity of an enzyme and thus control the rate of the particular reaction that a cell requires.

ENZYME REACTIONS ` Enzymes are proteins and therefore undergo all the reactions that proteins do. That is, enzymes can be coagulated by heat, alcohol, strong acids, and alkaloidal reagents. Many enzymes have now been prepared in crystalline form.

Temperature Requirement
Optimum temperature- the temperature at which the rate of a reaction involving an enzyme is the greatest.

Role of pH

optimum pH- range for that particular enzyme.

For example, the optimum pH of pepsin an enzyme found in gastric juice is approximately 2.0 whereas the optimum pH of trypsin, an enzyme found in pancreatic juice is near 8.2.

Effects of concentrations- the rate of the reaction will increase until the available enzyme becomes saturated with substrate.

ACTIVATORS AND INHIBITORS Activators- inorganic substances that tend to increase the activity of an enzyme. Inhibitor- is any substance that will make an enzyme less active or render it inactive. Irreversible inhibitors- form strong covalent bonds with the enzyme, rendering inactive.

Zalcitabin- is used in patients with advanced

HIV infection.

Poisons- enzyme inhibitors are oisonous

because of their effect on enzyme activity.

Cyclic AMP (cAMP) acts as a chemical

messenger to regulate enzyme activity within the cells that store carbohydrate and fat. Without cAMP the activity of all the enzymes working at maximum speed within the cells would soon create chaos.

Mode of Enzyme Activity Each enzyme contain an active site- that sector of the molecule at which combination with the substrate takes place. The active site consists of different parts of the protein chain (the enzyme). These parts are brought close together by the folding and bending of the protein chain (the secondary and tertiary structures), so that the active site occupies a relatively small area.

Apoenzymes and Coenzymes Apoenzyme- is protein part. Coenzyme- is the nonprotein (organic) part.

COENZYMES - Coenzymes are not proteins and so are not

inactivated by heat. Examples of coenzymes are the vitamins or compounds derived from vitamins.

The reaction involving a coenzyme can be written as follows: coenzyme + apoenzyme enzyme

Nomenclature  formerly enzymes were given names ending in in, with no relation being indicated between the enzyme and the substance it affects the substrate. The current system for naming enzymes uses the name of the substrate or the type of reaction involved, with the ending ase.

Classification -The Commission of Enzymes of the International Union of Biochemistry has classified enzymes into six divisions. Each of these divisions can be further subdivided into several classes. The following paragraphs indicate these divisions and some of the classes. The older names of the enzymes are still in common use and are given throughout this text merely for simplicity. It is much easier to write sucrase than a giucopyrano - b fructofuranohydrolase.

Enzymes and Substrates of Reaction Types

Enzyme Maltase Urease Proteases Carbohydrases Lipases Hydrolases Deaminases Dehydrogenases Substrate or Reaction Type Maltose Urea Proteins Carbohydrates Lipids Hydrolysis reactions Removing amines Removing hydrogens

Oxidoreductases

Are enzymes that catalyze oxidationreduction reactions between two substrates. ` The enzymes that catalyze oxidationreduction reactions in the body are important because these reactions are responsible for the production of heat and energy.
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Transferases
are enzymes that catalyze the transfer of a functional group between two substrates.

Hydrolysis - The Hydrolytic Enzymes

catalyze the hydrolysis of carbohydrates, esters, and proteins.  They are named for the substrate upon which they act.


Lysosomes  Some hydrolases are present in the cytoplasm in organelles. Carbohydrates  are enzymes that catalyze the hyrodlysis of carbohydratesinto simple sugars.

Ptyalin or salivary amylase - for the hydrolysis of starch to dextrins and maltose. 2. Sucrase - for the hydrolysis of sucrose to glucose and fructose; sucrase occurs in the intestinal juice 3. Maltase - for the hydrolysis of maltose to glucose; maltase occurs in the intestinal juice 4. Lactase - for the hydrolysis of lactose to glucose and galactose; lactase occurs in the intestinal juice 5. Amylopsin, or pancreatic amylase - for the hydrolysis of starch to dextrins and maltose, pancreatic amylase occurs in the pancreatic juice
1.

Esterases - are enzymes that catalyze the hydrolysis of esters into acids and alcohols.

The various types of esterases are as follows: 1) Gastric lipase for the hydrolysis of fats to fatty acids and glycerol. 2) Steapsin, or pancreatic lipase for the hydrolysis of fats to fatty acids and glycerol. 3) Phosphatase for the hydrolysis of phosphoric acid esters to phosphoric acid.

` Proteases are enzymes that catalyze the

hydrolysis of protein to derived protein and amino acids.

These are of two types: o proteinases o peptidases

The proteinase of hydrolysis of proteins to peptides, are as follows:
1.

Pepsin
- found in the gastric juice, for the hydrolysis of protein to polypeptides

2.

Trypsin - found in the pancreatic juice, for the hydrolysis of protein to polypeptides Chymotrypsin - found in the pancreatic juice, for the hydrolysis of protein to polypeptides The peptides, for the hydrolysis of polypeptides to amino acids; are as follows:

3.

1. 2.

Aminopeptidases from the intestinal juice Carboxypeptidases from the pancreatic juice

Nucleases are enzymes that catalyze the

hydrolysis of nucleic acids. ` Examples are: Ribonuclease Deoxyribonuclease

Lyases
- are enzymes that catalyze the removal of groups from substrates by means other than hydrolysis, usually with the formation of double bonds.

Example: Fumarase which catalyzes the change of fumaric acid to t malic acid in the krebs cycle. Isomerases - are enzyme that catalyze the interconversion of cis trans isomers. Example: Retinal isomerase which catalyzes the conversion of 11-trans- retinal to 11-cis-retinal.

Ligases or synthetases - are enzymes that catalyze the coupling of two compounds with the breaking of pyrophosphate bonds. Example: - Is the enzyme that catalyzesthe formation of malonyl CoA during lipogenesis.

The end THANK YOU

Prepared by: Mary Ann Ouano Marilou Plateros BSND