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METABOLISM. YOU MUST KNOW… THE KEY ROLE OF ATP IN ENERGY COUPLING THAT ENZYMES WORK BY LOWERING THE ENERGY OF ACTIVATION THE CATALYTIC CYCLE OF AN ENZYME.

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Presentation on theme: "METABOLISM. YOU MUST KNOW… THE KEY ROLE OF ATP IN ENERGY COUPLING THAT ENZYMES WORK BY LOWERING THE ENERGY OF ACTIVATION THE CATALYTIC CYCLE OF AN ENZYME."— Presentation transcript:

1 METABOLISM

2 YOU MUST KNOW… THE KEY ROLE OF ATP IN ENERGY COUPLING THAT ENZYMES WORK BY LOWERING THE ENERGY OF ACTIVATION THE CATALYTIC CYCLE OF AN ENZYME THAT RESULTS IN THE PRODUCTION OF A FINAL PRODUCT THE FACTORS THAT INFLUENCE THE EFFICIENCY OF ENZYMES

3 CONCEPT 8.1 AN ORGANISMS METABOLISM TRANSFORMS MATTER AND ENERGY, SUBJECT TO THE LAWS OF THERMODYNAMICS

4 METABOLISM THE TOTALITY OF AN ORGANISMS CHEMICAL REACTIONS MANAGES THE MATERIAL AND ENERGY RESOURCES OF THE CELL

5 CATABOLIC PATHWAY LEADS TO THE RELEASE OF ENERGY BY THE BREAKDOWN OF COMPLEX MOLECULES TO SIMPLER COMPOUNDS EX. BREAKDOWN OF FOOD

6 ANABOLIC PATHWAY CONSUME ENERGY TO BUILD COMPLICATED MOLECULES FROM SIMPLER ONES EX. LINKING a.a. TO FORM MUSCLE PROTEIN IN RESPONSE TO PHYSICAL EXERCISE

7 ENERGY THE CAPACITY TO DO WORK KINETIC ENERGY – ENERGY DURING MOVEMENT POTENTIAL ENERGY – STORED ENERGY CHEMICAL ENERGY – A FORM OF POTENTIAL ENERGY WHERE ENERGY IS STORED IN MOLECULES AND THE AMOUNT DEPENDS ON ITS CHEMICAL BONDS

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9 THERMODYNAMICS STUDY OF ENERGY TRANSFORMATIONS THAT OCCUR IN MATTER FIRST LAW OF THERMODYNAMICS – THE ENERGY OF THE UNIVERSE IS CONSTANT AND THAT ENERGY CAN BE TRANSFERRED AND TRANSFORMED, BUT CANNOT BE CREATED OR DESTROYED

10 THERMODYNAMICS SECOND LAW OF THERMODYNAMICS – EVERY ENERGY TRANSFER, OR TRANSFORMATION INCREASES THE ENTROPY OR THE AMOUNT OF DISORDER OR RANDOMNESS, IN THE UNIVERSE

11 CONCEPT 8.2 THE FREE-ENERGY CHANGE OF A REACTION TELLS US WHETHER THE REACTION OCCURS SPONTANEOUSLY

12 FREE ENERGY THE PART OF A SYSTEMS ENERGY THAT IS ABLE TO PERFORM WORK WHEN THE TEMPERATURE OF A SYSTEM IS UNIFORM INCLUDES EXERGONIC AND ENDERGONIC REACTIONS

13 EXERGONIC REACTION ENERGY IS RELEASED OCCUR SPONTANEOUSLY (THAT DOESNT NECESSARILY MEAN QUICKLY) AND RELEASE FREE ENERGY TO THE SYSTEM

14 ENDERGONIC REACION REQUIRES ENERGY IN ORDER TO PROCEED ABSORB FREE ENERGY THEY REQUIRE FREE ENERGY FROM THE SYSTEM

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16 CONCEPT 8.3 ATP POWERS CELLULAR WORK BY COUPLING EXERGONIC REACTIONS TO ENDERGONIC REACTIONS

17 ENERGY COUPLING THE WAY CELLS MANAGE THEIR ENERGY RESOURCES TO DO CELL WORK THE USE OF AN EXERGONIC PROCESS TO DRIVE AN ENDERGONIC ONE

18 ATP THE PRIMARY SOURCE OF ENERGY FOR CELL IN ENERGY COUPLING MADE UP OF THE NITROGENOUS BASE ADENINE, RIBOSE, AND A CHAIN OF 3 PHOSPHATE GROUPS WHEN A PHOSPHATE GROUP IS HYDROLYZED, ENERGY IS RELEASED IN AN EXERGONIC REACTION

19 RELEASE OF ATP WORK IN THE CELL IS DONE BY THE RELEASE OF A PHOSPHATE GROUP FROM ATP THE EXERGONIC RELEASE OF THE PHOSPHATE GROUP IS USED TO DO THE ENDERGONIC WORK OF THE CELL WHEN ATP TRANSFERS ONE PHOSPHATE GROUP THROUGH HYDROLYSIS, IT BECOMES ADP

20 CONCEPT 8.4 ENZYMES SPEED UP METABOLIC REACTIONS BY LOWERING ENERGY BARRIERS

21 CATALYSTS SUBSTANCES THAT CAN CHANGE THE RATE OF REACTION WITHOUT BEING ALTERED IN THE PROCESS ENZYMES ARE MACROMOLECULES THAT ARE BIOLOGICAL CATALYSTS

22 ACTIVATION ENERGY THE AMOUNT OF ENERGY IT TAKES TO START A REACTION THE AMOUNT OF ENERGY IT TAKES TO BREAK THE BONDS OF THE REACTANT MOLECULES ENZYMES SPEED UP REACTIONS BY LOWERING THE ACTIVATION ENERGY OF THE REACTION BUT WITHOUT CHANGING THE FREE ENERGY CHANGE OF THE REACTION THE ENZYME ACTS ON A SUBSTRATE

23 ACTIVE SITE THE PART OF THE ENZYME THAT BINDS TO THE SUBSTRATE FORMS AN ENZYME- SUBSTRATE COMPLEX THAT IS HELD TOGETHER BY WEAK INTERACTIONS SUBSTRATE IS THEN CONVERTED INTO PRODUCTS THAT ARE RELEASED FROM THE ENZYME

24 WHAT AFFECTS ENZYME ACTIVITY? CHANGES IN pH AND TEMPERATURE 3-D SHAPE IS CHANGED SO THE ENZYME WILL NOT BE AS EFFECTIVE (DENATURES)

25 MANY ENZYMES REQUIRE NONPROTEIN HELPERS CALLED COFACTORS TO FUNCTION PROPERLY ORGANIC COFACTORS ARE REFERRED TO AS COENZYMES

26 COMPETITIVE INHIBITORS REVERSIBLE INHIBITORS THAT COMPETE WITH THE SUBSTRATE FOR THE ACTIVE SITE ON THE ENZYME SIMILAR CHEMICALLY TO THE SUBSTRATE REDUCE THE EFFICIENCY OF THE ENZYME AS IT COMPETES FOR THE ACTIVE SITE

27 NONCOMPETITIVE INHIBITORS DO NOT DIRECTLY COMPETE WITH THE SUBSTRATE IMPEDE ENZYME ACTIVITY BY BINDING TO ANOTHER PART OF THE ENZYME CAUSES ENZYME TO CHANGE SHAPE MAKING THE ACTIVE SITE NONFUNCTIONAL

28 CONCEPT 8.5 REGULATION OF ENZYME ACTIVITY HELPS CONTROL METABOLISM

29 ALLOSTERIC SITE A SPECIFIC BINDING SITE BUT NOT THE ACTIVE SITE ONCE BOUND, THE SHAPE OF THE ENZYME IS CHANGE AND IT CAN EITHER STIMULATE OR INHIBIT ENZYME ACTIVITY

30 FEEDBACK INHIBITION A TYPE OF ALLOSTERIC INHIBITION IT INCREASES THE EFFICIENCY OF THE PATHWAY BY TURNING IT OFF WHEN THE END PRODUCT ACCUMULATES IN THE CELL


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