ENZYMES: Nomenclature, Kinetics, and Mechanisms of Catalysis Flashcards

1
Q

These are biological catalysts which are predominantly protein in nature

A

Enzymes

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2
Q

How do enzymes speed up reactions?

A

Lowering of activation energy

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3
Q

The process of catalysis

A

Two-step process

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4
Q

The first process of catalysis

A

Enzyme-substrate complex formation

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5
Q

Second step in the process of catalysis

A

Conversion of substrate to product

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6
Q

How are enzymes classified?

A

They are classified in the type of reaction they catalyze.

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7
Q

Six classifications of enzyme reactions

A

Oxidoreductase, Transferase, Hydrolase, Ligase, Lyase, and Isomerase

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8
Q

Units involved in measuring enzyme activity

A

Km, Vmax, and Kcat

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9
Q

Factors affecting enzyme activity

A

Enzyme concentration, substrate concentration, temperature, pH, and the presence of inhibitors.

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10
Q

What competes against the substrate in binding to the active site.

A

Competitive inhibitors

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11
Q

What affects enzyme conformation and binding of substrate to the active site?

A

The binding of non-competitive inhibitors to allosteric region

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12
Q

Compounds which an enzyme catalyzes

A

Substrate

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13
Q

Non-protein organic molecule, frequently a B-vitamin, that acts as a co-factor

A

Coenzyme

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14
Q

Non-protein portion of an enzyme that is necessary for catalytic function.

A

Cofactor

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15
Q

The protein part of an enzyme

A

Apoenzyme

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16
Q

The coenzyme or cofactor that is tightly bound to the apoenzyme.

A

Prosthetic Group

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17
Q

The term called for the binding of am apoenzyme and prosthetic enzyme

A

Holoenzyme

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18
Q

A specific portion of the enzyme to which a substrate binds during reaction.

A

Active site

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19
Q

Any process that initiates or increases the activity of an enzyme

A

Activation

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20
Q

The portion on the enzyme surface where inhibitors or activators bind to regulate catalytic reactions.

A

Allosteric Site

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21
Q

Compounds that slow down the rate of reaction

A

Inhibitors

22
Q

A process that makes an active enzyme less active or inactive.

A

Inhibition

23
Q

Composition of ribozymes

A

Nucleic acid

24
Q

The binding of enzyme and subtrate

A

Enzyme-subtrate complex

25
TRUE OR FALSE. Enzymes are highly selective catalysts
TRUE
26
Enumerate the specificity of enzymes
Bond specificity, group specificity, substrate specificity, optical specificity, geometrical specifity, co-factor specificity.
27
The mechanisms of catalysis
Lock and Key and Induced fit
28
A classification of enzymes that involves the process of oxidation-reduction reactions.
Oxidoreductase
29
An enzyme classification that involves a group transfer process
Transferase
30
An enzyme classification that involves the breaking of bonds in the presence of water.
Hydrolase
31
An enzyme classification that involves the addition or removal of double and triple bonds.
Lyase
32
An enzyme classification that involves isomerization reactions
Isomerase
33
An enzyme classification that involves the formation of new bonds
Ligase
34
The measure of how fast an enzyme-catalyzed reaction happens.
Enzyme activity
35
Considerations in enzyme activity
How fast substrates are utilized and how fast products are formed
36
What happens when there is a proportional increase in enzyme concentration and rate of reaction.
More enzymes mean more molecules to convert substrate to products.
37
The rate of reaction wherein it is directly proportional to substrate concentration.
First order kinetics
38
At high substrate concentration, there is an increase reaction rate plateau because of saturation
Zero order kinetics
39
The basis of catalytic parameters
The effect of substrate concentration to enzyme activity
40
The relationship of Michaelis constant and affinity
Inversely proportional
41
The number of moles of substrate converted to products per mole of enzyme per unit time.
Turnover Number (Kcat)
42
The relationship of temperature and reaction rate
Directly proportional
43
Loss of catalytic activity of enzyme
Denaturation
44
Loss of catalytic activity of enzyme
Denaturation
45
The effect of change in pH on reaction rates
The change in pH alters the charge of amino acid residues found in active site.
46
At which an enzyme exhibits maximum activity (Vmax)
Optimal pH
47
What happens to enzyme activity when pH is not regulated?
Irreversible denaturation occurs causing loss of catalytic activity
48
Types of inhibitors
Competitive, Non-competitive, and Uncompetitive
49
It isva reversible inhibitor that competes against substrate in binding to the active site.
Competitive Inhibitor
50
An inhibitor that binds to allosteric sites and alters enzyme conformation.
Non-competitive Inhibitors