Mr. Shardul S.


Enzymes are biocatalysts. They increase the rate of chemical reaction taking place within living cells without themselves suffering any overall change.

The name µenzyme¶ (enG = in; zymeG = yeast) means µin yeast¶ ‡Enzymes are protein in nature. ‡They enhance the rate of reaction by lowering the activation energy. ‡pH and temperature sensitive. ‡Specific in nature.

Enzyme exploration was influenced by modern scientific approach of fermentation industry. The name µenzyme ¶ was coined by observing conversion of fruit juice (sugar) in to fine wine (alcohol) and release of Co2 .

you may have to delete the image and then insert it again. and then open the file again. or the image may have been corrupted. . Restart your computer. Your computer may not have enough memory to open the image. [E] + [S] [ES] [P] + [E] The image cannot be displayed. acting on a particular substrate to produce a particular product or products.How Enzymes work????????? The reactants of enzyme ±catalyzed reaction are termed substrates and each enzyme is quite specific in character. If the red x still appears.

Complexity of Biochemical Pathways .


How to remember and name these enzymes?????? .

1.B. I. 4. 2. Substrate that is synthesized. Chemical composition of the enzyme. 3. . 6. 7.U. 5. Substrate acted upon and type of reaction catalyzed.Enzyme Nomenclature and Classification With continuous increase in knowledge of enzymology. classification. Substance hydrolyzed and group involved. various systems have evolved to name and classify the enzymes. Substrate acted upon by the enzyme. Type of reaction catalyzed.

1. The substance upon which an enzyme acts is called the substrate. Duclaux (1883) named the enzyme by adding the suffix ± ase in the name of the substrate catalyzed. Examples: Carbohydrate ± Carbohydrase Protein ± Proteinase Lipid ± Lipase Maltose ± Maltase Sucrose ± Sucrase . Substrate acted upon by the enzyme.

Transaminases ± transamination. Oxidase ± oxidation. Dehydrogenases ± dehydrogenation. . Isomerases ± isomerization.  The enzymes are highly specific as to the reaction they catalyzed.  Hence this classification is based on adding suffix ± ase in the name of reaction they catalyzed. Examples: Hydrolase ± hydrolysis.2. Type of Reaction catalyzed.

Succinic dehydrogenase :. . Substrate acted upon and type of reaction catalyzed. L± glutamic dehydrogenase :.dehydrogenation of L ±glutamic acid.3. Eg. The name of some enzymes give clue of both the substrate utilized and the type of reaction catalyzed.catalyzes dehydrogenation of substrate succinic acid.

4.forms fumarate irreversibly by L ± malate. Few enzymes named by adding the suffix . . Fumarase :. Eg. Substrate that is synthesized.ase to the name of the sustenance synthesized.

( Zn2+)  Enzyme containing protein & non protein:.(Prosthetic group) Iron porphyrin enzyme:. Urease. Examples:  Enzyme containing protein only :. Chemical composition of the enzyme. Classification based on chemical composition.Catalase. Cytochrome c peroxidase I & II .Pepsin.carbonic anhydrase. Trypsin.  Enzyme containing protein & cation :.5.

Amylase. exopeptidase.6. Esterase .Lipase. Substance hydrolyzed and group involved.Endopeptidases.glucorinidase Protein hydrolyzing enzymes :. Lipid:. Examples: Carbohydrate :. Sucrase. F.Cellulase.

The major features of this system are:Reactions are divided in to 6 major classes. Additional information regarding nature of reaction. 2. 1. I. Classification 1961 The chemical reaction catalyzed is specific property which distinguishes one enzyme from another. Eg. Each with 4 to 13 subclasses.B.) L.U. Each enzyme has 2 parts ± the first part is the name of substrate & second with suffix ± ase.B.Malate +NAD+ Pyruvate +Co2 +NADH+H+ .U. indicate type of reaction catalyzed.malate : NAD oxidoreductase. used this criterion as a basis for classification and naming of enzymes. (L.7. I. Malate dehydrogenase.

B. Alcohol Dehydrogenase.U.C.1.) 1.Each enzyme has been allotted systemic code called Enzyme commission number (E.I.) it consist of series of 4 digits.1.1. (E. Class Sub Class (acting on CH ± OH group of electron donor) Sub Sub Class (electron acceptor) Enzyme Number . Example. Classification contd« 4.C.

Isomerases (Isomers) Class 6. Hydrolase (Hydrolysis) Class 4. Ligases (To joint) . Transferase (Transfer of Group) Class 3. Oxidoreductase (Oxidation n Reduction) Class 2.Class 1. Lyases (Lysis) Class 5.

1. (Alcohol Dehydrogenase) Enzyme serial Number.1. Acting on (CH ± OH) alcohol group of electron donor.Class 1. Other example is Lactate Dehydrogenase (E.atoms or electrons from one substrate to another.C. Eg. 1.27) . O. Oxidoreductase (Oxidation n Reduction) These enzymes catalyze the transfer of H atoms. Electron acceptor.

CH3) (transfer from first Carbon) Eg.1) (Hexokinase) D. 2. ATP : D.Hexose ±6 ± phosphatases (2.1.7. Transferase (Transfer of Group) Catalyzes the reaction AX + B BX + A While giving name to particular enzyme Enzyme commission recommends that the name of transferase should end ³X ± Transferase´ where X ± is the group transferred.2.1.1 methyltransferases ( . Eg.hexose + ATP D ± Hexose ± 6 ± (P) + ADP .

A ± X + H2O X ± OH + HA These types of enzymes catalyzes the reaction of hydrolysis of ester. Eg.1) (Alkaline phosphatase) Organic (P) inorganic (P) . glycosyl by addition of water molecule. Orthophosphoric monoester phosphohydrolase (E. Hydrolase (Hydrolysis) Enzymes catalyzes hydrolytic reaction.C.1.3.Class 3. 3.

Class 4.4. .1.1.22) (Histidine ± decarboxylase) Histidine Histamine. L ± Histidine carboxy ± lyase (E. Eg. Lyases (Lysis) These enzymes catalyses the non hydrolytic removal of groups from substrates often leaving double bonds.C.

1) L.alanine D ± alanine.Class 5.C.1. 5. Isomerases (Isomers) Enzymes catalyzing isomerization reaction Eg. . Alanine racemase (E.1.

3. Acid .C.Class 6. .1. 6.ammonia ligases. X + Y + ATP X ± Y + ADP + Pi E. Ligases (To joint) Enzymes catalyzed the synthesis of new bonds coupled to the breakdown of ATP or other nucleoside triphosphates.

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