Enzymes Flashcards

1
Q

Each ___ have multiple domains

A

Unit

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2
Q

Part that have prosthetic group/co-factor attached, that help shape the enzyme; have own non-polar region

A

Domain

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3
Q

Can develop the secondary characteristic (coiled structure)

A

Twist and turn

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4
Q

Composed of beta structure

A

Flat-like/ribbon-like shape

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5
Q

Structure that deals with both coiled and beta shape structures

A

Tertiary structure

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6
Q

Involved in the electron transport chain. It is found in complex #3 where it is embedded in mitochondria

A

Cytochrome C Oxidase

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7
Q

A biological catalyst

A

Enzyme

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8
Q

Enzymes can increase the rate of a reaction by a factor of ___ to ___ over an uncatalyzed reaction

A

10^9 to 10^20

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9
Q

Refers to the D and L isomeric form of substrate

A

Stereoselective

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10
Q

Important in nitrogen fixation; relevant in providing food for plants and animals

A

Urease

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11
Q

Digestive enzyme that is secreted in pancreas and incorporated in pancreatic juice and released in the small intestine

A

Trypsin

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12
Q

Targets within the sequence of proteins iteself

A

Endopeptidase

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13
Q

Targets terminal acid of both ends of the sequence

A

Exopeptidase

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14
Q

Enzymes responsible for oxidation-reduction reactions

A

Oxidoreductases

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15
Q

Enzymes responsible for group transfer reactions

A

Transferases

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16
Q

Enzymes responsible for hydrolysis reactions

A

Hydrolases

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17
Q

Enzymes responsible for the addition of two groups to a C-C double bond, or the removal of two groups to create a C-C double bond

A

Lyases

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18
Q

Enzymes responsible for isomerization reactions

A

Isomerases

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19
Q

Enzymes responsible for the joining of two molecules

A

Ligases (or synthases)

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20
Q

Involves the transferring of reactions, or group that is typically a phosphate group

A

Transferases

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21
Q

Uses water to cleave a bond. It is also used to deactivate certain molecules

A

Hydrolases

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22
Q

A part of the axon terminal

A

Presynaptic cleft

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23
Q

Where dendrites can be found

A

Postsynaptic cleft

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24
Q

A space covered with a very thin membrane

A

Synaptic gap

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25
Important in physiological function since it attaches to a specific receptor that will activate it. Once it is activated, it will activate other neurons
Acetyl Choline
26
Responsible for degrading acetyl choline into acetic acid and choline in synaptic gap to prevent overstimulation
Acetyl Choline Esterases
27
Converts one compound into another functional group and usually partnered with an isomerase
Lyases
28
Transports shape or structure of a particular isomer into another form, or rearranges form to fit the target molecule. Tautomerization
Isomerase
29
Forms particular bonds. Typically happens during anabolic reactions
Ligase
30
The protein part of an enzyme
Apoenzyme
31
A nonprotein portion of an enzyme that is necessary for catalytic function
Cofactor
32
A nonprotein organic molecule that acts as a cofactor
Coenzyme
33
The compound/s whole reaction an enzyme catalyzes
Substrate
34
The specific portion of an enzyme to which a substrate binds during reaction
Active site
35
Requires a cofactor or coenzyme to be activated
Apoenzyme
36
A measure of how much a reaction rate is increased
Enzyme activity
37
"Asymptote" which means that you can never achieve theoretical value of Vmax because of the rate of dissociation of enzyme to your product (k3)
Zero order
38
Enzyme + Substrate
= Enzyme Substrate Complex
39
Enzyme substrate complex will produce ___ ___ ___
Enzyme Product Complex
40
Enzyme Product Complex will dissociate into ___ + ___
Enzyme + Product
41
k1
Rate of formation
42
k2
Rate of dissociation
43
k3 or kcat
An Important rate
44
Any process that initiates or increases the activity of an enzyme
Activation
45
Any process that makes an active enzyme less active or inactive
Inhibition
46
A substance that binds to the active site of an enzyme thereby preventing binding of substrate
Competitive Inhibitor
47
Any substance that binds to a portion of the enzyme other than the active site and thereby inhibits the activity of the enzyme
Noncompetitive Inhibitor
48
Another name of the lock and key model
Fischer model
49
Induced fit model is also known as?
Koshland model
50
The point of substrate concentration. It determines substrate affinity. The lower the value, the higher the affinity and the other way around
Km
51
It gives tight binding to the active site. The tight bonding loses when substrate is converted into product
Sulfhydryl group
52
An enzyme regulation process where the product of a series of enzyme-catalyzed reactions inhibits an earlier reaction in the sequence
Feedback control
53
Also called as "Feed Forward Reaction". As you accumulate more product, it will induce or activate further the enzyme to increase binding affinity of enzyme to substrate, leading to a higher rate of velocity of the reaction
Positive Feedback Control
54
Incomplete enzyme
Apoenzyme
55
You have already produced a complete enzyme but it is in an inactive form, which needs modification
Zymogen
56
Enzyme regulation based on an event occurring at a place other than the active site but that creates a change in the active site
Allosterism
57
Inhibition of an allosteric enzyme
Negative modulation
58
Stimulation of an allosteric enzyme
Positive modulation
59
A substance that binds to an allosteric enzyme
Regulator
60
The process of affecting enzyme activity by covalently modifying it
Protein modification
61
An enzyme that occurs in multiple forms; each catalyzes the same reaction
Isoenzyme/Isozymes
62