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Biochemistry Laboratory > Enzymes > Flashcards

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
Q

Important in physiological function since it attaches to a specific receptor that will activate it. Once it is activated, it will activate other neurons

A

Acetyl Choline

26
Q

Responsible for degrading acetyl choline into acetic acid and choline in synaptic gap to prevent overstimulation

A

Acetyl Choline Esterases

27
Q

Converts one compound into another functional group and usually partnered with an isomerase

A

Lyases

28
Q

Transports shape or structure of a particular isomer into another form, or rearranges form to fit the target molecule. Tautomerization

A

Isomerase

29
Q

Forms particular bonds. Typically happens during anabolic reactions

A

Ligase

30
Q

The protein part of an enzyme

A

Apoenzyme

31
Q

A nonprotein portion of an enzyme that is necessary for catalytic function

A

Cofactor

32
Q

A nonprotein organic molecule that acts as a cofactor

A

Coenzyme

33
Q

The compound/s whole reaction an enzyme catalyzes

A

Substrate

34
Q

The specific portion of an enzyme to which a substrate binds during reaction

A

Active site

35
Q

Requires a cofactor or coenzyme to be activated

A

Apoenzyme

36
Q

A measure of how much a reaction rate is increased

A

Enzyme activity

37
Q

“Asymptote” which means that you can never achieve theoretical value of Vmax because of the rate of dissociation of enzyme to your product (k3)

A

Zero order

38
Q

Enzyme + Substrate

A

= Enzyme Substrate Complex

39
Q

Enzyme substrate complex will produce ___ ___ ___

A

Enzyme Product Complex

40
Q

Enzyme Product Complex will dissociate into ___ + ___

A

Enzyme + Product

41
Q

k1

A

Rate of formation

42
Q

k2

A

Rate of dissociation

43
Q

k3 or kcat

A

An Important rate

44
Q

Any process that initiates or increases the activity of an enzyme

A

Activation

45
Q

Any process that makes an active enzyme less active or inactive

A

Inhibition

46
Q

A substance that binds to the active site of an enzyme thereby preventing binding of substrate

A

Competitive Inhibitor

47
Q

Any substance that binds to a portion of the enzyme other than the active site and thereby inhibits the activity of the enzyme

A

Noncompetitive Inhibitor

48
Q

Another name of the lock and key model

A

Fischer model

49
Q

Induced fit model is also known as?

A

Koshland model

50
Q

The point of substrate concentration. It determines substrate affinity. The lower the value, the higher the affinity and the other way around

A

Km

51
Q

It gives tight binding to the active site. The tight bonding loses when substrate is converted into product

A

Sulfhydryl group

52
Q

An enzyme regulation process where the product of a series of enzyme-catalyzed reactions inhibits an earlier reaction in the sequence

A

Feedback control

53
Q

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

A

Positive Feedback Control

54
Q

Incomplete enzyme

A

Apoenzyme

55
Q

You have already produced a complete enzyme but it is in an inactive form, which needs modification

A

Zymogen

56
Q

Enzyme regulation based on an event occurring at a place other than the active site but that creates a change in the active site

A

Allosterism

57
Q

Inhibition of an allosteric enzyme

A

Negative modulation

58
Q

Stimulation of an allosteric enzyme

A

Positive modulation

59
Q

A substance that binds to an allosteric enzyme

A

Regulator

60
Q

The process of affecting enzyme activity by covalently modifying it

A

Protein modification

61
Q

An enzyme that occurs in multiple forms; each catalyzes the same reaction

A

Isoenzyme/Isozymes

62
Q
A

Biochemistry Laboratory (6 decks)

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