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 ORGANISM’S METABOLISM TRANSFORMS MATTER AND ENERGY, SUBJECT TO THE LAWS OF THERMODYNAMICS

4. METABOLISM THE TOTALITY OF AN ORGANISM’S 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

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 SYSTEM’S 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 DOESN’T 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

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