ENZYMES and their importance in body systems.pptx

enzymes

1. ENZYME GUNJAN PANT MSC ZOOLOGY I –SEM

2. ENZYME HISTORY OF ENZYME ENZYME STRUCTURE ENZYME NOMENCLUTURE CLASSIFICATION OF ENZYME MODE OF ENZYME ACTION FACTOR AFFECTING THE ENZYME ACTIVITY ENZYME IHIBHITION

3. HISTORY OF ENZYME SCIENTIST ANSELME PAYEN FIRSTLY DISCOVERED DIASTASE THE TERM ENZYME GIVEN BY SCIENTIST KUNHE ENZYME IS A GREEK WORD WHICH MEANS IN YEAST SCIENTIST SUMNAR DISCOVER UREASE ENZYME AND SCIENTIST BUKNER EXTRACT ZYMASE ENZYME FROM JACKBEAN

4. ENZYME STRUCTRE SIMPLE ENZYME COMPOSED ONLY OF PROTEIN CONJUGATED ENZYME COMPOSED OF : _ APOENZYME .EACH ENZYME MADE OF PROTEIN AND THIS PROTEIN PART IS CALLED IS CALLED AS APOENZYME WHILE IN SOME ENZYME COFACTOR ARE ATTACHED _COFACTER .ANY NON PROTEIN PART OF ENZYME IS CALLED AS COFACCTOR AND ATTACHED TO ENZYME THEY ARE OF 3 TYPE ACTIVATOR CO-ENZYME PROSTHETIC GROUP ACTIVATOR : THEY ARE SUCH SUBSTRATE GROUP WHICH WORK TO ACTIVATE THE ENZYME CO-ENZYME :NON PROTEIN PART DO NOT ATTACHED TO PROTEIN ONLY HELP THE PROTEIN PROSTHETIC GROUP :WHEN OGRANIC GROUP ATTACHED TO ENZYME

5. ENZYME NOMENCLUTURE INNOMENCLUTURE OF ENZYME OF SUFFIX ARE ATTACHED TO SUBSTRATE GROUP IN SOME ENZYME ‘AS’ IS USED AS SUFFIX FOR SUBSTRATE FOR EXAMPLE SUCROSE – SUCRASE PROTEIN –PROTEASE IN SOME ENZYME ‘IN’ IS USED AS SUFFIX FOR SUBSTRATE FOR EXAMPLE PEPSIN TRYPSIN AMYLASIN In some enzyme ‘lytic’ is used as suffix for substrate For example Proteolytic

6. Classification of enzyme Classification of enzyme done by INTERNATIONAL UNION OF BIOCHEMISTRY AND ACCORDING TO THEIR REACTION THEY DIVIDED INTO FOLLOWING CLASS OXIDOREDUCTASE ENZYME TRANSFERASE ENZYME HYDROLASE ENZYME LYASE ENZYME ISOMERASE ENZYME

7. Mode of enzyme action Action of enzyme can be understand with the Help of 2 mechanism Lock and key mechanism –on enzyme different active Site are present on it specific substrate can be attached Which is specific substrate of active side Enzyme and substrate combine together and form Intermediate complex or called as enzyme Substrate complex but after it it change into enzyme And product

8. Induced fit mechanism THIS IS GIVEN BY KOSH LAND IN 1959 ACCORDING TO THE THEM AT THE ACTIVE SITE OF ENZYME TWO GROUP ARE ATTACHED WHICH IS CALLED AS BUFFERING CATALYTIC GROUP BUFFERING GROUP SUPPORT SUBSTRATE WHILE CATALYTIC GROUP MAKE BINDING SITE WEAK

9. FACTOR AFFECTING THE ENZYME ACTIVITY OPTIMUM TEMP OPTIMUM PH E-S COMPLEX CONCENTRATION OPTIMUM TEMP-ACTIVITY OF EACH ENZYME INCREASES AT OPTIMUM TEMP.USUALLY OPTIMUM TEMP.OF ENZYME 25-40C ON THIS TEMP. ENZYME ARE MORE ACTIVE AT HIGH TEMP ENZYME STARTED DEGERNATING 2. OPTIMUM PH – EACH ENZYME WORK AT SOECIFIC PH WHICH IS CALLED AS OPTIMUM PH IT RANGE IS 6-7.5 SOME DIGESTIVE ENZYME ENZYME ALSO WORK AT ALAKLINE MEDIUM AND SOME ON ACIDIC MEDIUM FOR EXAMPLE – PEPSIN -PH- TRYPSIN – PH-8.5

10. Concentration of substrate When concentration of substrate increases than rate of reaction Also increases but when molecules fill the active site of Enzyme than on increases of substrate rate of reaction Does not increases On than substrate concentration the max velocity Of reaction become half that is called as constant this value is different for different substrate

11. ENZYME INHIBHITION A DECREASES IN ENZYME PROCESS ,ENZYME PRODUCTION ,OR ENZYME ACTIVITY IS REFFERED AS A ENZYME INHIBHITION THERE ARE FOLLOWING TYPE OF ENZYME INHIBHITION REVERSIBLE INHIBHITION NON REVERSIBLE INHIBHITION FEED BACK INHIBHITION ALLOSTERIC INHIBHITION

12. REVERSIBLE INHIBHITION IN THIS INHIBHITION FROM SUBSTRATE ENZYME STOP REACTION IN WHICH PRODUCT REACTION . IN WHICH PRODUCT DOES NOT FORM ARE OF TWO WHEN INHIBHITION IS REMOVE SO THAN ACTIVITY OF ENZYME COME AT RESTING THIS TYE OF INHIBHITION ARE OF TWO TYPE COMPETATIVE NON COMPETATIVE

13. COMPETATIVE INHIBHITION WHEN ANY ORGANIC MOLECULES COMPPETATE WITH SUBSTRATE THEY START COMPETATION FOR ACTIVE SITE OF ENZYME AND INHIBHIT TO ATTACHED IT IS CALLED AS COMPETATIVE INHIBHITION FOR EXAMPLE -SUCCINIC DEHYDROGENASE ENZYME INHIBHIT BY MALLONIC ACID IT STRUCTURE IS SIMILAR TO SUCINNIC ACID AND DOES NOT FORM PROPER PRODUCT NON COMPETATIVE INHIBHITION COEMPETATION FOR ACTIVE SITE IS NOT HAPPEN E-S COMPLEX DOES NOT FORM

14. 3.FEED BACK INHIBHITION 4. ALLOSTERIC INHIBHITION

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