Presentation is loading. Please wait.

Presentation is loading. Please wait.

Introduction to Metabolism

Similar presentations

Presentation on theme: "Introduction to Metabolism"— Presentation transcript:

1 Introduction to Metabolism

2 Metabolism is the sum of an organism’s chemical reactions
Metabolism is an emergent property of life that arises from interactions between molecules within the cell

A metabolic pathway begins with a specific molecule and ends with a product The product of one reaction is substrate of the next Each step is catalyzed by a specific enzyme BIOCHEMICAL PATHWAY VIDEO

Concentrated in specific location Covalently bound in complex Soluble with free floating intermediates Attached to a membrane in sequence

5 CATABOLIC PATHWAY (CATABOLISM) Release of energy by the breakdown of complex molecules to simpler compounds EX: digestive enzymes break down food ANABOLIC PATHWAY (ANABOLISM) consumes energy to build complicated molecules from simpler ones EX: linking amino acids to form proteins

6 Krebs Cycle connects the catabolic and anabolic pathways

7 Forms of Energy ENERGY = capacity to cause change
Energy exists in various forms (some of which can perform work) Energy can be converted from one form to another

8 KINETIC ENERGY – energy associated with motion
HEAT (thermal energy) is kinetic energy associated with random movement of atoms or molecules POTENTIAL ENERGY = energy that matter possesses because of its location or structure CHEMICAL energy is potential energy available for release in a chemical reaction

9 Diving converts potential energy to kinetic energy. On the platform, the diver has more potential energy. In the water, the diver has less potential energy. Climbing up converts kinetic energy of muscle movement to potential energy.

10 THERMODYNAMICS = the study of energy transformations
CLOSED system (EX: liquid in a thermos) = isolated from its surroundings OPEN system energy + matter can be transferred between the system and its surroundings Organisms are open systems

11 The First Law of Thermodynamics
= energy of the universe is constant Energy can be transferred and transformed Energy cannot be created or destroyed The first law is also called the principle of CONSERVATION OF ENERGY

12 The Second Law of Thermodynamics
During every energy transfer or transformation entropy (disorder) of the universe INCREASES some energy is unusable, often lost as heat

Second law of thermodynamics First law of thermodynamics Chemical energy Heat CO2 H2O ORGANISMS are energy TRANSFORMERS! Spontaneous processes occur without energy input; they can happen quickly or slowly For a process to occur without energy input, it must increase the entropy of the universe

14 Free-Energy Change (G) can help tell which reactions will happen
∆G = change in free energy ∆H = change in total energy (enthalpy) or change ∆S = entropy T = temperature ∆G = ∆H - T∆S Only processes with a negative ∆G are spontaneous Spontaneous processes can be harnessed to perform work

15 Exergonic and Endergonic Reactions in Metabolism
EXERGONIC reactions (- ∆G) Release energy are spontaneous ENDERGONIC reactions (+ ∆G) Absorb energy from their surroundings are non-spontaneous

16 Mechanical Transport Chemical A cell does three main kinds of work:
Concept 8.3: ATP powers cellular work by coupling exergonic reactions to endergonic reactions A cell does three main kinds of work: Mechanical Transport Chemical In the cell, the energy from the exergonic reaction of ATP hydrolysis can be used to drive an endergonic reaction Overall, the coupled reactions are exergonic

17 ATP provides energy for cellular functions
ATP (adenosine triphosphate) is the cell’s renewable and reusable energy shuttle ATP provides energy for cellular functions Energy to charge ATP comes from catabolic reactions Adenine Phosphate groups Ribose

18 Adenosine triphosphate (ATP)
+ P P + Energy i Inorganic phosphate Adenosine diphosphate (ADP)

19 Energy for cellular work provided by the loss of phosphate from ATP
Energy from catabolism (used to charge up ADP into ATP ADP + P i

20 Glutamic acid Ammonia Glutamine ATP H2O ADP
Endergonic reaction: DG is positive, reaction is not spontaneous NH2 + NH3 DG = +3.4 kcal/mol Glu Glu Glutamic acid Ammonia Glutamine Exergonic reaction: DG is negative, reaction is spontaneous ATP + H2O ADP P + DG = –7.3 kcal/mol i Coupled reactions: Overall DG is negative; Together, reactions are spontaneous DG = –3.9 kcal/mol

21 Reactants: Glutamic acid
P i P Motor protein Protein moved Mechanical work: ATP phosphorylates motor proteins Membrane protein ADP ATP + P i P P i Solute Solute transported Transport work: ATP phosphorylates transport proteins P NH2 + NH3 Glu + P i Glu Reactants: Glutamic acid and ammonia Product (glutamine) made Chemical work: ATP phosphorylates key reactants

22 Every chemical reaction between molecules involves
bond breaking and bond forming ACTIVATION ENERGY = amount of energy required to get chemical reaction started Activation energy is often supplied in the form of heat from the surroundings Free energy animation IT’S LIKE PUSHING A SNOWBALL UP A HILL . . . Once you get it up there, it can roll down by itself

23 The Activation Energy Barrier
D Transition state A B EA Free energy C D Reactants A B DG < O C D Products Progress of the reaction

24 CATALYST = a chemical agent that speeds up a reaction without being consumed by the reaction ENZYMES = biological catalysts Most enzymes are PROTEINS Exception = ribozymes (RNA)

Course of reaction without enzyme EA without enzyme EA with enzyme is lower Reactants Free energy Course of reaction with enzyme DG is unaffected by enzyme Products Progress of the reaction ENZYMES work by LOWERING ACTIVATION ENERGY;

Orienting substrates correctly Straining substrate bonds Providing a favorable microenvironment Enzymes change ACTIVATION ENERGY but NOT energy of REACTANTS or PRODUCTS

27 ENZYMES Most are proteins Lower activation energy Specific
Shape determines function Re-usable Unchanged by reaction

28 The REACTANT that an enzyme acts on = SUBSTRATE
Enzyme + substrate = ENZYME-SUBSTRATE COMPLEX Region on the enzyme where the substrate binds = ACTIVE SITE Substrate held in active site by WEAK interactions (ie. hydrogen and ionic bonds)

29 TWO MODELS PROPOSED LOCK & KEY Active site on enzyme fits substrate exactly INDUCED FIT Binding of substrate causes change in active site so it fits substrate more closely

30 Enzyme Activity can be affected by:
General environmental factors, such as temperature, pH, salt concentration, etc. Chemicals that specifically influence the enzyme See a movie Choose narrated

Each enzyme has an optimal temperature at which it can function (Usually near body temp)

32 Increasing temperature increases the rate of an
enzyme-catalyzed reaction up to a point. Above a certain temperature, activity begins to decline because the enzyme begins to denature.

33 pH and ENZYME ACTIVITY Each enzyme has an optimal pH at which it can function

34 COFACTORS = non-protein enzyme helpers
EX: Zinc, iron, copper COENZYMES = organic enzyme helpers Ex: vitamins

V MAX Adding substrate increases activity up to a point

GENE REGULATION cell switches on or off the genes that code for specific enzymes

FEEDBACK INHIBITION end product of a pathway interacts with and “turns off” an enzyme earlier in pathway prevents a cell from wasting chemical resources by synthesizing more product than is needed FEEDBACK INHIBITION

38 NEGATIVE FEEDBACK An accumulation of an end product slows the process that produces that product B A C D Enzyme 1 Enzyme 2 Enzyme 3 Negative feedback Example: sugar breakdown generates ATP; excess ATP inhibits an enzyme near the beginning of the pathway

39 POSITIVE FEEDBACK (less common)
The end product speeds up production W X Y Z Enzyme 4 Enzyme 5 Enzyme 6 Positive feedback EXAMPLE: Chemicals released by platelets that accumulate at injury site, attract MORE platelets to the site.

ALLOSTERIC REGULATION protein’s function at one site is affected by binding of a regulatory molecule at another site Allosteric regulation can inhibit or stimulate an enzyme’s activity Allosteric enzyme inhibition

Each enzyme has active and inactive forms The binding of an ACTIVATOR stabilizes the active form The binding of an INHIBITOR stabilizes the inactive form

42 Binding of one substrate molecule to
active site of one subunit locks all subunits in active conformation. Substrate Inactive form Stabilized active form COOPERATIVITY another type of allosteric activation

43 COOPERATIVITY = form of allosteric regulation that can amplify
enzyme activity Binding of one substrate to active site of one subunit locks all subunits in active conformation

44 Enzyme Inhibitors COMPETITIVE inhibitor REVERSIBLE; Mimics substrate and competes with substrate for active site on enzyme ENZYME ANIMATION

45 Enzyme Inhibitors NONCOMPETITIVE inhibitors bind to another part of an enzyme, causing the enzyme to change shape and making the active site less effective ENZYME ANIMATION


Download ppt "Introduction to Metabolism"

Similar presentations

Ads by Google