Enzymes and Chemical Reactions Flashcards

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1
Q

exergonic

A

more energy released than absorbed

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2
Q

endergonic

A

more energy absorbed than released`

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3
Q

potential energy

A

energy stored in chemical bonds

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4
Q

kinetic energy

A

energy being used. movement, light, sound

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5
Q

activation energy

A

energy input needed to start a reaction

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6
Q

catalyst

A

a substance that speeds up reaction rates without being used up

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7
Q

catabolic

A

release energy by breaking up complex molecules

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8
Q

anabolic

A

uses energy to create complex molecules

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9
Q

how are enzymes biological catalysts

A

they are proteins that speeds up reaction rates in biological processes without being used up

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10
Q

metabolism

A

sum of organism’s chemical reactions

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11
Q

why are ender- and exer- gonic reactions often coupled

A

Because metabolism is the sum of these reactions

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12
Q

Transition State

A

The transition state is when the bonds between molecules are at their weakest due to the potential energy being highest.

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13
Q

what is an active site?

A

where the enzyme bonds with the substrate

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14
Q

what bonds help bond the enzyme and substrate?

A

Hydrogen bonds
Ionic bonds
Hydrophobic interactions
Covalent bonds

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15
Q

what are the 2 theories on how enzymes and substrates bond?

A

lock and key, and induced fit.

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16
Q

what is lock and key?

A

It is a theory that enzymes are built geometrically and chemically to fit a substrate.

17
Q

what is induced fit?

A

It is a theory that an enzyme changes to fit the substrate

18
Q

What factors affect if a substrate can bond with a enyme?

A

competitive inhibitors, non-competitive inhibitors, and a change in pH or heat.

19
Q

How does substrate concentration affect enzyme reaction rates?

A

As substrate concentration increases, the reaction rate increases.
When the enzyme is saturated, the rxn rate will reach maximum.
It is saturated is when there are more substrates than enzymes.

20
Q

How does enzyme concentration affect enzyme reaction rates?

A

As enzyme concentration increases, the reaction rate increases(assuming substrate is abundant).
As enzymes increase, there are more collisions between substrates and enzymes, increasing the likelihood that an enzyme will collide.
There are theoretically no limits to the rate of rxn when adding enzymes, but in the body, the substrate becomes the limiting factor.

21
Q

How does temperature affect enzyme reaction rates?

A

As temperature increases, so does the rxn rate UNTIL the enzyme begins to unfold/denature. Every enzyme has an optimal temperature at which it works best. A Fever is created to denature bacteria when you are sick.

22
Q

How does pH affect enzyme reaction rates?

A

Every enzyme also has an optimal pH. This optimum is usually the pH where the enzyme functions in nature. Most mammals function best at a pH of about 7-8, similar to cellular environments.
Mouth = fairly neutral
Stomach = highly acidic
Small intestine = fairly basic

23
Q

What are cofactors and how do they affect enzyme reaction rates?

A

Many enzymes require the binding of smaller non-protein cofactors to function.Cofactors may be a small metal ion or vitamins.

24
Q

How do inhibitors affect enzyme reaction rates?

A

Enzyme inhibitors are chemicals which bind to enzymes and decrease the enzyme’s ability to catalyze its reactants.
Usually reversible, or can be irreversibly (covalent)

25
Q

what are non-competitive inhibitors

A

They bind (reversibly/irreversibly) to another part of the enzyme, causing protein to change shape making substrate catalysis less favorable.

26
Q

what are competitive inhibitors

A

They bind (reversibly/irreversibly ) to an enzyme’s active site and block the substrate from binding.

27
Q

what is a allosteric activator

A

Only On form has binding sites for both substrate and activator.
Activator locks enzymes in On form, making it easier for substrates to bind. Enzymes vibrate between Off and On.

28
Q

what is an allosteric inhibitor

A

The enzyme vibrates between Off and On forms. In the Off form of the enzyme cannot receive the substrate. The Inhibitor can bind and stabilize the off form. Allosteric inhibitors bind somewhere other than the active site and lock the enzyme into off form.

29
Q

what is negative feedback

A

Negative Feedback is when a molecule that occurs later in a metabolic pathway negatively affects a molecule earlier in the pathway. (inhibits)

30
Q

what is positive feed back

A

Positive feedback is when a molecule that occurs later in a metabolic pathway positively affects a molecule earlier in the pathway. (activates)

31
Q

what is positive feedfoward

A

Positive feedforward is when an earlier molecule affects a later one.(activates)

32
Q
A