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SLE111 Cells And Genes > Module 6: Metabolism And Enzymes > Flashcards

Module 6: Metabolism And Enzymes Flashcards

1
Q

What are polypeptides?

A

Polymers of amino acids.

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2
Q

What is the first Law of Thermodynamics?

A

Energy can be transformed and transferred but it cannot be created or destroyed.

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3
Q

What is the second Law of Thermodynamics?

A

Every energy transfer or transformation increases entropy of the system that it is in.

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4
Q

What does ATP stand for?

A

Adenosine triphosphate

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5
Q

What is metabolism?

A

The chemical processing of substances within a living cell or organism.

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6
Q

What are catabolic reactions?

A

A type of metabolism.
Catabolic reactions break down complex molecules into simpler ones. This releases energy.

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7
Q

What are anabolic reactions?

A

A type of metabolism.
Anabolic reactions build complex molecules from simple ones.
This uses energy.

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8
Q

What is energy?

A

The ability/capacity to do work

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9
Q

What are the two types of energy?

A
  1. Kinetic energy. The energy of movement - objects in motion.
  2. Potential energy. The potential to do work.
    E.g. a suspended object.
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10
Q

What is chemical energy?

A

The potential energy within chemical bonds.

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11
Q

What is Gibbs free energy?

A

The energy available after entropy - usable energy that is available to do work.

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12
Q

What is the equation to calculate the change in free energy?

A

ΔG = ΔH - TΔS

Where ΔG (delta G) is the change in free energy.
ΔH is the total energy in the system (enthalpy).
ΔS is the energy lost to entropy.
And T is the absolute temperature in Kelvin.

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13
Q

What is enthalpy?

A

The sum of a thermodynamic system’s internal energy and the product of its pressure and volume.

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14
Q

What is entropy?

A

The state of disorder, randomness, or uncertainty in a thermodynamic system. A measure of the amount of energy not available to do work.

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15
Q

What is thermodynamics?

A

Physics that deal with the relationships and conversions between heat and other forms of energy.

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16
Q

What type of reactions has a ΔG<0

A

A reaction that releases energy has a negative ΔG.
This is an exergonic reaction.

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17
Q

What is an exergonic reaction?

A

A reaction where energy is exiting the system.
This is also known as a spontaneous reaction because they can occur without needing energy input.

18
Q

What is a endergonic reaction?

A

A reaction that stores energy.
Requires an energy input and has a positive ΔG value.
Non-spontaneous.

19
Q

What is activation energy?

A

The amount of energy input necessary does chemical reactions to occur.
Ea

20
Q

What is an open system?

A

A system where energy can transfer between the system and its surroundings.

21
Q

What is a closed system?

A

A system where energy can NOT transfer between the system and its surroundings.

22
Q

What is the structure of ATP?

A

Adenosine is bound to 3 phosphate groups.

23
Q

What is adenosine?

A

A nucleoside (nucleotide without a phosphate group) that consists of the nitrogenous base adenine and a 5-carbon sugar, ribose.

24
Q

What is the hydrolysis reaction of ATP?

A

ATP + H2O → ADP + Pi + free energy

Where Pi is an inorganic phosphate group.

25
Q

What is the equation of ATP formation?

A

ADP + Pi + free energy → ATP + H2O

Where Pi is an inorganic phosphate group.

26
Q

What is phosphorylation?

A

The attachment of a phosphate group to a molecule or ion.

27
Q

How does ATP provide energy?

A

Energy coupling and phosphorylation through an exergonic reaction.
ATP is a highly unstable molecule that dissociates quickly. It releases energy by breaking one of its phosphate bonds - the created products have much lower free energy than the reactants (ATP and H2O).
With most ATP hydrolysis cases, the ATP phosphate transfers onto another molecule, triggering a conformational change.

28
Q

What is an enzyme?

A

A molecule that catalyses biochemical reactions.
Almost all enzymes are proteins comprised of amino acid chains.
They lower activation energy for chemical reactions.

29
Q

What is a catalyst?

A

A substance that modifies and increases the rate of a reaction without being consumed in the process.

30
Q

Where does a substrate bind?

A

The enzyme’s active site.

31
Q

What factors affect enzyme regulation? What does this cause?

A

If an enzyme is outside optimal conditions, it may denature.

  1. Temperature.
  2. pH.
  3. Regulatory molecules (inhibitor or activator molecules).
  4. Cofactors (non-proteins helpers that activate enzymes).
  5. Compartmentalisation (enzymes stored in specific compartments can be prevented from acting on certain substances).
  6. Feedback inhibition (regulation using a product of the enzyme).
32
Q

How do enzymes facilitate reactions?

A

They bring the substrates together in the optimal orientation.
They create an optimal environment for the reaction to occur.
Enzymes can also take part in the chemical reaction themselves, further lowering activation energy.

33
Q

What complex lowers activation energy and promotes rapid reaction progression?

A

The enzyme-substrate complex.

34
Q

What is an allosteric site?

A

A site on the enzyme other than the active site.
Where non-competitive inhibitors bind.

35
Q

What are the types of enzyme inhibitors?

A
  1. Competitive inhibitors. Bind to the active site.
  2. Non-competitive inhibitors. Binds to an allosteric site, NOT the active site. Harder to remove.
36
Q

What is an allosteric activator?

A

An effector molecule that binds to an enzyme at a location away from the active site, inducing a conformational change that increases the enzyme’s affinity for its substrate/s.

37
Q

What is a cofactor?

A

An inorganic ion, or non-protein chemical compound, helper molecule that assists enzymes.
E.g. iron (Fe+) and magnesium (Mg+).

38
Q

What is a coenzyme?

A

An organic helper molecule required for enzyme action.
The most common coenzymes are dietary vitamins.

39
Q

What enzyme builds DNA molecules?

A

DNA polymerase.

40
Q

How does vitamin C acts as a coenzyme?

A

Vitamin C is a coenzyme for multiple enzymes that take part in building collagen (an important connective tissue component).

41
Q

What is the difference in structure for most allosterically regulated enzymes?

A

They are comprised of more than one polypeptide, meaning they have more than one protein subunit.

42
Q

What is feedback inhibition in metabolic pathways?

A

Feedback inhition involves using a reaction product to regulate its own further production.

SLE111 Cells And Genes (17 decks)

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