Chemical Reaction & Enzymes Flashcards

(48 cards)

1
Q

Metabolism

A

in any living thing thousands of chemical reactions take place at the same time to support life

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2
Q

Chemical reaction

A

the process of breaking existing bonds, rearrangement of atoms and formation of new bonds

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3
Q

What are the three parts of a chemical reaction?

A

breaking, rearrangement, and formation

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4
Q

What do all chemical reactions need to start?

A

Activation energy

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5
Q

Activation energy

A

the energy required to break existing chemical bonds

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6
Q

What are the three ways to speed up a chemical reaction?

A

heat, motion, and catalysts

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7
Q

Catalysts

A

substances that accelerate or promote chemical reactions

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8
Q

Enzymes

A

the biological active catalysts that facilitate chemical changes in the human body by lowering the activation energy

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9
Q

Uncatalyzed reaction

A

a chemical reaction without an enzyme

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10
Q

Catalyzed reaction

A

a chemical reaction with an enzyme

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11
Q

Enzymes are what kind of organic molecule?

A

proteins

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12
Q

Enzymes exist as what?

A

polymers

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13
Q

Why are enzymes polymers?

A

because they are proteins

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14
Q

Active site

A

region of an enzyme where the substrate binds

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15
Q

What is temporarily formed when a substrate binds to an active site?

A

an enzyme-substrate complex

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16
Q

What is the importance of the specificity of an active site?

A

only allows one type of substrate to bind to the enzyme; catalyzing only one specific reaction

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17
Q

How are enzymes formed?

A

through protein synthesis

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18
Q

Enzyme mechanisms steps

A

the substrate binds to the enzyme forming an enzyme-substrate complex, the enzyme changes shape resulting in an induced fit, the substrate is broken down, and finally the products are released

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19
Q

Cofactors

A

an inorganic chemical structure attached to an enzyme that aids in enzyme function

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20
Q

Inorganic cofactors

A

are attached to the enzyme and are required for their normal function

21
Q

Organic cofactors

A

are not attached to enzymes and have specific functions in assisting enzymes

22
Q

What are the six major classes of enzymes?

A

oxidoreductase, transferase, hydrolase, isomerase, ligase, and lyase

23
Q

Oxidoreductase

A

transfers electrons from one substance to another

24
Q

Transferase

A

transfers a functional group

25
Hydrolase
splits a chemical bond using water
26
Isomerase
Converts isomer to another
27
Ligase
bonds two molecules together
28
Lyase
splits a chemical bond in the absence of water
29
Which class of enzymes participate in oxidation-reduction?
Oxidoreductase
30
The rate of a chemical reaction may be accelerated by what?
an increase in enzyme concentration or substrate concentration
31
Saturation
occurs when so much of a substarte is present that all enzyme molecules are actively engaged in the chemical reaction, resulting in no furthable (notable) increase in reaction rate
32
Inhibitors
substances that bind to an enzyme and turn it off, preventing it from catalyzing the reaction
33
Competitive inhibitor
interferes with active site of an enzyme so substrate cannot bind
34
Allosteric inhibitor
changes shape of enzyme active site so substrate cannot bind to enzyme
35
What determines the likelihood of competitive inhibitor occupying the active space?
the concentration of the substrate
36
Inhibition
a molecule that binds o an enzyme and blocks its activity
37
How are enzymes named?
root + -ase
38
Enzymes are highly what?
highlt specific
39
How do enzymes break down substrates?
they put stress in the substrate bonds
40
Why are enzymes needed in small quantities?
becuase enzymes are reused
41
What kind of conditions are required for enzymes to maintain their functional shape?
optimal conditions (temperature, pH)
42
What are the two forms of enzyme regulation?
activation and inactivation
43
Activation
binds a specific cofactor to an enzyme
44
What kind of molecules are cofactors usually?
metals (Zn, Fe, Mg) and vitamins (B, C, K)
45
Inactivation
binds inhibitors
46
How do allosteric inhibitors differ from competitive inhibitors?
competitve inhibitors compete for the active site while allosteric inhibitors alter the overall shape of the enzyme
47
The prefix allo- means what?
wrong
48
The suffix"-steric" means what?
shape