Metabolism Flashcards

1
Q

Describe the second law of thermodynamics

A

The amount of disorder (entropy) in the universe always increases with any change that occurs, and at the same time the energy that can do useful work decreases (lost as heat)

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2
Q

Describe the first law of thermodynamics

A

Energy can be neither created nor destroyed, it can only be transformed from one form to another

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3
Q

When does entropy increase in chemical reactions?

A

When solids become liquids or gases, when fewer reactant molecules from a greater number of product molecules, when complex molecules are broken down into simpler subunits, when solutes move from diffusion

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4
Q

Describe activation energy

A

The amount of energy needed to strain and break the reactant bonds

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5
Q

Describe transition state

A

A temporary condition in which the bonds within the reactants are breaking and bonds between the products are forming. Energy is released when product bonds are formed

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6
Q

Describe an exothermic reaction

A

If more energy is released during bond formation then was absorbed during bond breaking, there is a net energy output. It occurs spontaneously, therefore it is favoured because it increases entropy. Its products contain less energy than the reactants, therefore they are more stable. And usable energy is released (decrease in free energy available)

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7
Q

Show an annotated diagram of an exothermic reaction

A
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8
Q

Describe an endothermic reaction

A

If the amount of energy absorbed from breaking reactant bonds is greater than the energy released in the formation of products, the result is a net absorption of energy. It does not occur spontaneously and is not favoured because they involve a decrease in entropy (second law of thermodynamics). Its products contain more energy than the reactants. And it requires an input of energy (ex. ATP needed to drive reactions)

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9
Q

Show an annotated diagram for an endothermic reaction

A
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10
Q

Describe enzymes

A

Biological catalysts, proteins that regulate all biological processes

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11
Q

What determines the speed of chemical reactions?

A

The amount of activation energy needed, the concentration and effectiveness of the catalyst

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12
Q

How do enzymes work?

A

The shape of the globular protein determines the function, they stress chemical bonds, lower the activation energy barrier

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13
Q

Show an annotated endergonic energy diagram with the addition of enzymes

A
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14
Q

Show an annotated exergonic energy diagram with the addition of enzymes

A
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15
Q

Describe how enzymes work

A

Surface depressions are active sites and represent the location of catalysis. The substrate (reactant molecule on which the enzyme acts) must fit the active site exactly. The enzyme stresses the chemical bond, thereby lowering its activation energy barrier

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16
Q

What factors affect enzyme activity?

A

Temperature, pH, and enzyme and substrate concentration They disrupt the bonds of the protein (enzyme) and denature it, changing its shape and thus, its function

17
Q

Describe enzymatic allosteric sites

A

Receptor sites some distance away from the active site that binds substances to the enzyme that may either inhibit or stimulate an enzyme’s activity

18
Q

How is enzyme activity regulated?

A

Inhibitors decrease the enzyme activity. Competitive inhibitors dont involve the allosteric site and are substances that compete with the substrate for an enzyme active site and block the substrate from binding

19
Q

Describe noncompetitive inhibitors

A

Substances that attach to a binding site on an enzyme other than the active site (pricking the factory worker metaphor). This causes a change in the enzymes shape, therefore regular substrates will not fit

20
Q

Describe an allosteric inhibitor

A

A substance that binds to an allosteric site on an enzyme, altering its active site and stabilizing the inactive form of the enzyme. This prevents the substrate from binding to it

21
Q

Describe enzymatic activators

A

Increases the enzymes activity, because an activator binds to an allosteric site which stabilizes the protein conformation and keeps all of the active sites available to their substrates. Both inhibitors and activators work because of allosteric changes of the enzyme as a result of the binding of a non-substrate molecule to the enzyme. Activator “effector” stabilizes or activates the enzyme, allowing it to bind to the substrate

22
Q

Define metabolism

A

The total amount of all anabolic and catabolic reactions in a cell or organism

23
Q

Define kinetic energy

A

The energy of moving particles or objects (heat contracting)

24
Q

Define potential energy

A

Stored energy; the energy of position (chemical bonds, the attraction of electrons to protons, etc.)

25
Give an example of an endothermic and exothermic reaction
Endothermic: photosynthesis Exothermic: cellular respiration
26
At which temperature do human enzymes work best?
37 degrees Celsius
27
Describe cofactors
Inorganic non-proteins, usually dissolved metal ions, that are needed for the enzyme to function and catalyze reactions
28
Describe coenzymes
Organic non-proteins, including derivatives of many vitamins, that are needed for the enzyme to function and catalyze reactions. Many shuttle molecules from one enzyme to another (Ex. NAD+ or nicotinamide adenine dinucleotide, a derivative of vitamin B3)
29
Give examples of enzyme use in commercial and industrial fields
Hydrolysis of starches into glucose (enzymes amylase and glucoamylase), fat-hydrolyzing enzymes (lipases used by dairy industry to develop strong flavoured cheeses), cleaning industry (proteases and amylases to help remove protein and carb stains from clothes), hydrolysis of lactose into monosaccharides because of lactose intolerances (lactase), animal feed, brewing, leather, wine and juice
30
Show an annotated diagram of allosteric activation
31
Show an annotated diagram of allosteric inhibition
32
Describe feedback inhibition
The regulation of a pathway by one of the products of this pathway
33
Describe the steps of allosteric activation
Enzyme binds allosteric activator, binding activator converts enzyme to high-affinity state, in high-affinity state, enzyme binds substrate
34
Describe the steps of allosteric inhibition
Enzyme binds allosteric inhibitor, binding inhibitor converts enzyme to low-affinity state and substrate is released
35
Describe allosteric regulation
Includes an allosteric activator which causes an enzyme to have a high affinity for the substrate it binds, and an allosteric inhibitor which causes an enzyme to have a low-affinity for a substrate, causing its release
36
Describe the induced-fit hypothesis
Enzymes are not rigid objects, like locks, but are flexible. Prior to substrate binding, the enzyme changes its shape (conformation) so that the active site becomes even more precise in its ability to bind to its substrate
37
Describe the enzyme cycle
Since enzymes remain unchanged after a reaction, enzyme molecules can rapidly bind to other substrate molecules, catalyzing the same reaction repeatedly. Typical rates vary between 100 and 10 million substrate molecules per second
38
Do all inhibitors work the same?
In reversible inhibition, the binding of the inhibitor to the enzyme is weak and reversible. Enzyme activity returns to normal. Some inhibitors bind so strongly to the enzyme through the formation of covalent bonds that they completely disable the enzymes. This is irreversible inhibition, such as cyanide.
39
Describe how penicillin works
The antibiotic acts by inhibiting the synthesis of peptidoglycan, a key component of the bacterial cell wall. The enzyme transpeptidase catalyzes the formation of a peptide bond between two amino acids responsible for making peptidoglycan. Since penicillin resembles the two amino acids, it can bind to transpeptidase and inhibit it