Enzymes Flashcards

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1
Q

General Info about Enzymes

A
  • All enzymes are proteins, but not all proteins are enzymes
  • Biological catalysts that consist of complex protein structures
  • speed up or slow down reactions by lowering the activation energy
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2
Q

What does catalyst mean

A
  • Tend to speed up reactions
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3
Q

Why are enzymes important to biological systems?

A
  • Because other factors that increase reaction rate (such as temp or concentration) are also known to denature biological proteins
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4
Q

Important note about enzymes

A
  • Enzymes do not get used up in reactions themselves
  • They are reusable
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5
Q

Substrate

A
  • A molecule or compound that is acted upon by the enzyme
  • It often fits into the entire enzyme itself and fits in the active site
  • Ex. Starch
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6
Q

Active Site

A
  • The physical opening in which the substrate attaches
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7
Q

Induced Fit Model

A
  • Model explains how some substrates are able to alter and improve the shape of an active site so that the enzyme functions better
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8
Q

What does the induced fit model suggest?

A

That the “lock and key fit” is not necessarily accurate

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9
Q

Cofactors

A
  • Inorganic substances that aid in the enzyme’s function
  • Minerals
  • Ex: Ca2+, Na+, Mn2+
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10
Q

Coenzymes

A
  • Organic substances that aid enzyme function
  • Ex: Any type of vitamin
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11
Q

Allosteric Sites

A
  • Receptor sites on an enzyme where the controlling molecule can plug in and affect enzyme function
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12
Q

What is a receptor site?

A

A site on a membrane of a molecule where small attachments can join

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13
Q

Graph A

A
  • Linear reaction/relationship
    -As the enzyme concentration increases so does the rate of reaction
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14
Q

Graph B

A
  • Curved graph
  • When the substrate concentration is too high, active sites get saturated since enzyme stays the same
  • Substrate concentration gets too high when you over eat
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15
Q

3 ways to control enzyme functions

A
  1. Competitive Inhibitors
  2. Allosteric Regulators
  3. Feedback Inhibition
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16
Q

Competitive Inhibitors

A
  • Molecules that mimic substrate molecules and end up blocking the normal substrate
  • Makes competition for the active site
  • This can slow down or sometimes stop enzyme function
17
Q

Note about competitive inhibitors

A
  • Can be a natural occurrence but it can also happen because of toxins that enter cell’s
18
Q

Allosteric Regulators

A

Molecules that bind to allosteric sites of an enzyme

19
Q

What are the two types of allosteric regulators?

A
  1. Non-competitive inhibitors
  2. Allosteric Activators
20
Q

Activator

A

Turn on enzymes

21
Q

Inhibitor

A

Turn off enzymes

22
Q

Noncompetitive Inhibitors

A
  • Inhibit the enzymes from functioning by having a non-substrate molecule attach to an allosteric site so that the enzyme no longer functions
23
Q

Example of an artificial noncompetitive inhibitor

A

Pesticide DDT

24
Q

Allosteric Activators

A
  • Molecules that bind to allosteric sites of enzymes and can alter the protein conformation
  • Inactive enzymes become activated and the new active site becomes more stabilized
25
Q

Feedback Inhibition

A
  • Process by which an enzyme is inhibited by a product that has formed after a series of other enzymatic reactions
  • Self-regulating
  • If the end product accumulates in high quantities, it will inhibit the first enzyme
26
Q

Note about feedback inhibition

A

Good way of regulating the production of molecules so you don’t make too much of a product within a cell

27
Q

Example of feedback inhibition

A

ATP allosterically inhibits more making of itself