Unit 1 KA6 Metabolic Pathways Flashcards

Stuff gets broken and stuff gets made

1
Q

Define metabolism

A

All the chemical reactions that occur within the human body

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2
Q

What are anabolic pathways?

A

Enzyme pathways that require energy and involve biosynthetic (building up small molecules to larger ones) processes

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3
Q

What are catabolic pathways?

A

Enzyme pathways that release energy and involve the breakdown of molecules to smaller ones

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4
Q

What is activation energy?

A

The energy require to break chemcial bonds in the reactants to start a chemical reaction

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5
Q

What is the state at which chemical bonds become unstable due to absorbing too much energy called?

A

The transition state

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6
Q

What is a catalyst?

A

A substance that:
*Lowers the activation energy of a reaction by providing an alternative reaction pathway
* Speeds up the reaction rate
* Takes part in the reaction but remains unchanged by the end of it

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7
Q

What is a biological catalyst?

A

An enzyme

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8
Q

What are enzymes made of?

A

Protein

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9
Q

Why do enzyme active sites only bind to specific substrates?

A

The active site has a specific shape

due to the structure and bonding of the amino acids in the polypeptide chain

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10
Q

**

Substrate molecules have high ____ for the active site

A

affinity

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11
Q

The products have a ____ affinity for the active site

A

low

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12
Q

What does affinity mean?

A

The strength of attraction between the molecules.

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13
Q

What is induced fit?

A

When the enzyme’s active site changes shape to better fit the substrate

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14
Q

How does induced fit help the reaction?

A

It insures that the active site is very close to the substrate and thus increases the chance of the reaction taking place

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15
Q

How are the reactants’ orientation determined in enzyme reactions with multiple reactants?

A

The shape of the active site determines the orientation

This holds the reactants tightly together, in a way that ensures the reaction can take place

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16
Q

What factors affect enzyme reactions?

A
  1. Temperature
  2. pH
  3. Substrate concentration
  4. Enzyme concentration
17
Q

What do inhibitors do to the reaction rate?

A

slow it down or bring it to a halt

18
Q

What happens to the reaction rate as substrate concentration increases?

A

Increases, then eventually remains constant as the active sites are all occupied, meaning the enzyme concentration is now the limiting factor

19
Q

How can metabolic pathways be controlled?

A
  1. Presence of an enzyme
  2. Absence of an enzyme
  3. Key enzymes regulating the rate of a reaction within a metabolic pathway
20
Q

How are enzymes who’s genes are continually expressed controlled?

A

regulation of their rate of reaction

21
Q

Most enzyme reactions are reversible

What determines the direction of reaction?

A

The concentration of the substrates and products

22
Q

What is an inhibitor?

A

A substance that decreases the rate of an enzyme controlled reaction

23
Q

What is a competitive inhibitor?

A

An inhibitor that competes with the substrate for the enzyme’s active sites

It binds to the enzyme’s active site, preventing the substrate from binding to the active site, reducing enzyme activity and thus the rate of reaction

24
Q

What is the structure of competitive inhibitors?

A

Similar molecular structure to the enzyme’s substrate

25
How can the effect of competitive inhibitors be reversed?
By increasing the substrate concentration
26
What is a non-competive inhibitor?
An enzyme inhibitor that does not compete with the substrate for the active site ## Footnote The inhibitor instead competes for the allosteric (non-active) site
27
What is the site where non-competitive inhibitors bind to on an enzyme?
The allosteric (non-active) site
28
Once a non-competitive inhiitor has binded to the allosteric site, what is the effect on the enzyme?
The active site's shape changes, so it no longer fits the substrate, thus preventing it from binding
29
If substrate concentration is increased, what happens to the effect of the non-competive inhibitors?
Nothing, as they do not compete with the subtrate for the active site ## Footnote They bind to the allosteric site, instead of the active site