Enzymes Flashcards

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1
Q

Enzyme

A

A macromolecule that acts as a catalyst: A chemical agent that speeds up a reaction without being consumed by the reaction

–> Organic biological catalyst
–> Ends in -ase

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2
Q

Substrate

A

The molecule (reactant) on which the enzyme acts upon

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3
Q

Bond Breaking vs Forming

A

Bond Breaking = Input Energy

Bond Forming = Release Energy

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4
Q

Endergonic

A

Absorbs more energy than is released

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5
Q

Exergonic

A

Releases more energy than is absorbed

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6
Q

Activation Energy

A

(Ea) Energy required to initially break bonds (start the reaction) –> Get over the hump

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7
Q

Delta G

A

Net free energy released

Energy of Products - Energy of Reactants

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8
Q

Enzymes and Activation Energy

A

Enzymes lower activation energy for reactions, they DO NOT lower Delta G

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9
Q

Catalytic Cycle of an Enzyme

A

1) Enzyme and substrate are available

2) Substrate binds to enzyme –> (Forms “enzyme-substrate” complex)

3) Substrate is converted to products and products are released

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10
Q

Active Site

A

The specific region of an enzyme that binds the substrate and that forms the pocket in which catalysis takes place

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11
Q

Properties of Enzymes (4)

A

1) Enzymes lower activation energy

2) Enzymes are usually proteins

3) Enzymes are usually named by adding (-ase) to the end of substrate name

4) Enzymes are substrate specific

–> However, not lock and key model, follows induced fit model

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12
Q

How Enzymes Work: 3 possibilities

A

1) In reactions with 2 or more reactants: Active site provides template on which substrates can come together with proper orientation to react

2) Stretch and Strain Bonds: Active site clutches bound substrate and stretches them towards their transition state form (Lowers Ea)

3) Create Favorable Microenvironment (Ex: providing more acidic environment)

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13
Q

Vmax

A

Maximum reaction rate –> All enzymes “full and working”

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14
Q

Enzyme Saturation

A

All enzymes at full capacity:

Only way to increase reaction rate in this case is to increase number of enzymes

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15
Q

Km

A

Concentration of substrate at which enzyme works at 1/2 the max rate

–> Indicates how tightly the substrate is bound to the enzyme

1) Greater Km = Lower Binding Affinity

2) Lower Km = Higher Binding Affinity

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16
Q

Effects of Environmental Conditions

A

Changes to temp, pH, or salinity can alter enzymatic function

17
Q

Cofactors

A

INORGANIC –> Usually divalent cations (minerals—EX: Mg2+, Ca2+, Mn2+)

Any non-protein molecule or ion that is required for the proper functioning of an enzyme

18
Q

Coenzymes

A

ORGANIC –> Mostly vitamins

Supply reactive atoms that are necessary for the reaction but are not available at the active site

19
Q

Competitive Inhibitor

A

A molecule that directly competes with the substrate for the active site

BINDS TO THE CATALYTIC SITE

–> A physical block: Can be removed by adding more SUBSTRATE

20
Q

Non-Competitive Inhibitor

A

A molecule that binds outside the active site (NO PHYSICAL competition)

–> Inhibits by causing changes to the conformation of the active site (so that the substrate can’t bind)

21
Q

Allosteric Regulation

A

A reversible, non-competitive inhibitor (like a light switch)

–>Must have 2 sites: Active and allosteric

22
Q

Allosteric Regulators

A

Regulators bind to the allosteric site to change activity of enzyme

1) Activator = Stabilizes the active conformation of the active site

2) Inhibitor = Stabilizes the INactive conformation of the active site

23
Q

Cooperativity

A

A form of allosteric activation

–> The binding of one substrate molecule facilitates the binding of other substrate molecules

(Has multiple active sites)

24
Q

Feedback Regulation

A

The final product of a chain of enzymatic reactions allosterically inhibits the first enzyme of the chain

–> Essentially turns itself (the chain reaction) off

–> Prevents the uncontrollable accumulation of products