Chapter 8 Flashcards

1
Q

Metabolism

A

All the chemical reactions in an organism

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2
Q

Catabolic pathways

A

-breakdown of molecules into smaller compounds.
-release the energy stored in complex molecules

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3
Q

Anabolic pathways

A

-Building smaller molecules into larger
- Require/absorb energy

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4
Q

Energy

A

capacity to cause change

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5
Q

Kinetic energy

A

the energy of motion

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6
Q

Thermal energy

A

Heat - the kinetic energy of randomly moving atoms or molecules.

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7
Q

Potential energy

A

Stored energy due to arrangement and placement. Ex: a ball at the top of a hill has high potential energy. Because of its position at the top of the hill, the ball can be push and will roll down.

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8
Q

Chemical energy

A

energy stored within bonds, which can be released to do work. Ex: The body breaks apart glucose, the energy released from breaking the bond is used by the body as energy.

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9
Q

First law of thermodynamics

A

Energy cannot be created or destroyed. It can be transformed.

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10
Q

Second law of thermodynamics

A

every energy transformation increases the entropy of the universe

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11
Q

Entropy

A

measure of disorder

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12
Q

Free energy

A

system’s energy available to perform work

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13
Q

Exergonic reactions

A

Energy is released

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14
Q

Endergonic Reaction

A

Energy is absorbed

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15
Q

ΔG

A

Free energy change

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16
Q

ΔH

A

change in Enthalpy

17
Q

ΔS

A

Change in Entropy

18
Q

Enzymes

A

Biological catalysts. They speed up metabolic reaction by lowering the activation energy (energy needed to start reaction)

19
Q

Spontaneous

A

a reaction that occurs without an input of energy. Exergonic reactions are spontaneous

20
Q

energy coupling

A

the use of exergonic processes to drive endergonic ones

21
Q

Substrates

A

The substrate binds to the active site of the enzyme

22
Q

Active site

A

a “pocket” found on the surface of the enzyme. Every active site has a specific substrate that can fit in it.

23
Q

Induced fit

A

SIMPLY EXPLAINED: the active site “hugs” the substrate. The “hug” puts them closer together, making the enzyme work better.

Actual explanation: Interactions between substrates and active sites causes the enzyme to slightly change shape. This enhances the ability of the enzyme to catalyze the chemical reaction

24
Q

Catalysis in the Enzyme’s Active Site

A

Some of the surrounding amino acids in the active site have side chains (R chains) that help turn the substrate into the product.

25
Q

denaturing of enzymes

A

Each enzyme has certain environments that it works best in. Change in pH and temperature can denature the enzyme, meaning it changes its shape, decreasing its function.

MAIN FACTORS
-Temperature
-pH
-Chemicals

26
Q

Cofactors

A

SIMPLE DEFINITION: Cofactors are helper molecules or ions that enzymes need to work properly

Actual definition: Cofactors are non-protein molecules or ions that assist enzymes in performing their catalytic functions

27
Q

Coenzymes

A

organic cofactors ex. vitamins

28
Q

Competitive inhibitors

A

Binds to the active site of an enzyme. Competes with substrate. Increasing the amount of substrate may overcome this type of inhibition.

29
Q

Noncompetitive inhibitors

A

binds to another part of an enzyme, causing the enzyme to change shape, and the active site stops working.

30
Q

Allosteric Regulation

A

Some enzymes have a site called the allosteric site. This is NOT the active site, it is an ADDITIONAL site on the enzyme.

An activator binds to the allosteric site to increase the enzyme’s activity, while an inhibitor binds to decrease or block the enzyme’s activity.

31
Q

Why is allosteric regulation important?

A

Allosteric regulation turns the enzyme “on” and “off”. This regulates metabolic reactions, preventing too much or too little products from being produced.

32
Q

cooperativity

A

SIMPLER DEFINTION: the binding of one molecules “unlocks” the other active sites on the molecule, increasing enzyme activity

ACTUAL DEFINITION: when one molecule binding to an enzyme makes it easier (or harder) for more molecules to bind, affecting how active the enzyme is.

33
Q

Feedback inhibition

A

SIMPLE DEFINTION: product binds to enzyme, changing its shape, preventing the enzyme from creating more products. The prevents too many products being made.

ACTUAL DEFINITION: The end product acts as an allosteric inhibitor of an enzyme early in the metabolic pathway. This prevents overproduction.

34
Q

ATP to ADP

A

In ATP, a phosphate breaks away, and ATP is now ADP. This releases 7.3 k/cal of energy to be used by the body to do work.