chapter 8 | Metabolism

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Last updated 8:53 PM on 7/12/26
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30 Terms

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Potential energy

Energy stored due to location/position!

  • held/stored ready to be used

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Kinetic energy

Energy associated with motion

  • In kinetic energy: working to get energy

  • Out kinetic energy: released energy out

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ATP

Energy currency of cells

  • One a denoting, robust sugar, and three phosphate groups

Adenosine Triphosphate

  • through hydrolysis it releases energy

  • The bond between the 2nd and 3rd phosphate s hydrolyzed

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First law of thermodynamics

Energy can be transferred but not created/destroyed

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Second law of thermodynamics

Transfer/transformation not 100% efficient

Energy transfer/transformation releases entropy (disorder) of the universe

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ATP

Phosphate groups are unstable

Hydrolysis reaction: makes ADP+energy

Reaction is reversible

ATP (charged) →H2O in (hydrolysis)→ADP (energy low)→H2O out (ATP is charged)

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Metabolism

All the reactions that a cell or organism makes to sustain life

  • Cells use the bonds in carbon and other molecules for energy

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Metabolism

How cells obtain carbon depends on type of cell

  • 2 types of this: autotrophs and heterotrophs

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Autotrophs

“Self” “Feed”

  • plants, algae, some bacteria

  • Chemosynthesis and photosynthesis

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Heterotrophs

“Other/different” “feed”

  • eukaryotes, animals

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Photoautotrophs

Convert sunlight energy into G3P (precursor to glucose)

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Heterotrophs

Hydrolyzed ingested polymers of organic molecules into monomers

  • dinner of steak and potato’s, protein hydrolyzed to amino acids, etc.

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Metabolism more info

Monomers can be further broken down to obtain energy or used to build new macromolecules

  • chemical energy in the bonds of polymers and monomers can be converted into ATP

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Metabolic pathways

Begins with a specific molecule (reactant) which is altered in a series of steps to result in a product

  • biological assembly line, sequence to make controlled steps!

  • Takes place in: building proteins/carbs, transporting material, muscle cells require energy to move, etc

  • 2 types! Catabolic and anabolic

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Anabolic(endergonic energy)

Synthesize and builds large molecules

  • requires energy, +G

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Catabolic (Exergonic)

Degradative, breaks large molecules

  • creates energy, -G

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Gibbs free energy

Amount of free energy available to the cell to do work and energy created from breaking chemical bonds

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Alpha Gibs

Change in free energy

= G of products- of reactants

  • 2 types spontaneous and requires energy(endergonic and exergonic)

  • All chemical reactions in the cell are coupled with ATP!

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Endergonic reaction

  • anabolic

  • Uphill reaction’requires energy, no spontaneous

  • Products have more potential energy than reactants

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Exergonic reactions

Catabolic

  • downhill spontaneous

  • Produce energy in form of ATP

  • -G

  • Products have less potential energy than reactants

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Activation of energy

  • prevents reactions from spiraling out of control (called energy of activation)

  • Requires stress to be placed on bonds to make them unstable

  • Small inputs of initial energy needed (even exergonic)

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Enzyme

A type of protein that catalyze chemical reactions by lowering EA

  • doesn’t make a reaction occur that would not normally occur

  • Does not add energy and does not change alpha gibs!

  • Only changes: lowering the energy activation level!

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Enzyme specificity (part of enzyme)

Binds to substrates (reactants)

  • active site (lock and keyhole)

  • Enzyme is unchanged and not consumed

  • Converts substrate to a different product

Used a million times, works as a place to make reactions faster

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Enzyme reaction

The process of a chemical reaction turning into a product

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Enzyme function

They are proteins

  • affected by temp, pH, salt

  • High temps and acid/basic pH will denature enzyme structure

  • Organisms in cold vs hot have ideal temperatures

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Anzyme activation

Activators help enzymes!

  • Co-factors help enzymes (dent in enzyme)

  • Activator attached itself to co factor

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Enzyme inhibitors

Blocks activity

  • 2 types; non-competitive and competitive inhibitors

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No competitive inhibitors

Bind to enzyme at site remote from active site (allosteric site)

  • alters shape and prevents from binding

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Competitive inhibitors

Mimics shape of substrate, binds to active site to block it

  • Pharmaceutical applications (cancer treatments)

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Feedback inhibitation

Type of enzymatic regulation/product acts as a non competitive inhibitor