Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Cellular Biology > Enzymes > Flashcards

Enzymes Flashcards

You may prefer our related Brainscape-certified flashcards:
AP® Biology flashcards Biology 101 flashcards
1
Q

What is fermentation

A

Transformation of RAW material such as starch, sugar, etc., into industrial mixtures such as liquors

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Biotransformation

A

transformation of defined precursors to desired target product (environmental friendly processes to treat waste)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Pharmaceutical industry

A

Synthesis and modification of antibiotics

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

product: HF corn syrup

A

Enzyme: Glucose isomerase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Product: Lactose-Free Milk

A

Lactase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Product: Acrylamide

A

Enzyme: Nitrilase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Product: Cocoa butter

A

Enzyme: Lipase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Product: Ampicillin

A

Enzyme: Penicillin Amylase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Product: L-methionine; L-valine

A

Enzyme: Aminoacylase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Product: L-cartidine

A

Enzyme: dehydrate/hydroxylase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Product: L-dopa

A

Enzyme: beta-tyrosinate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Binding sites are

A

Specific and reversible

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Reversible binding

A

Equilibrium between the free and bound ligand

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What are Enzymes

A

Protein catalyst that increase the rate of reaction without being changed in the process

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Rate

A

Velocity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Substrate is

A

Enzyme reactant

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Recommended names for enzymes (3)

A

Short, most commonly used
Suffix -ase attached to substrate of reaction
OR to description of reaction performed

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Systematic names of enzymes (3)

A

More complete, complex, used when an enzyme has to be identified without ambiguity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Oxidoreductase

A

Catalyze reactions where a molecule is being reduced and one being oxidized (oxidation-reduction reactions)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Transferases

A

Transfer Carbon, Nitrogen, Phosphate containing groups

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Hydrolases

A

Catalyze a hydrolysis cleavage reaction

Adds water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Lyases

A

Cleavage of C-C, C-S, C-N bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Isomerases

A

Rearrangement of bonds within a single molecule

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Ligases

A

Join together (ligate) two molecules together in an energy dependent process (DNA Ligase joints two DNA molecules) between S,C,N,O

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

Polymerases

A

Polymerization reactions such as SNA or RNA synthesis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

Proteases

A

Break down proteins by hydrolyzing bonds between amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

Kinases

A

Addition of phosphate groups to molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

ATPases

A

Hydrolyzes ATP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

Synthases

A

Synthesize molecules in anabolic reaction by condensing two smaller molecules together (ATP SYNTHASE)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

ACTIVE SITE increases what

A

Special pocket called the active site which increases specificity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

ENZYME-SUBSTRATE COMPLEX

A

Substrates binds to the enzyme, forming the complex ES causing confirmations change in the enzyme that allows a catalysis … an EP is formed

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

EFFICIENCY (catalyzed vs uncatalyzed)

A

Reactions catalyzed by enzymes are 10^3-10^8 faster than uncatalyzed reactions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

SPECIFICITY

A

Enzymes interact with 1 of few substrates and catalyze only one type of reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

T or F

Holoenzymes do not need cofactors

A

False some do need cofactors

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

E+CE= ?

A

ACTIVE (HOLOENZYMES)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

E -CF= ?

A

INACTIVE (APOENZYME)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

T OR F

ENZYME ACTIVITY CAN BE REGULATED SO THAT THE RATE OF PRODUCTS RESPONDS TO CELLULAR NEEDS

A

TRUE

IT CAN INCREASE OR DECREASE THE ENZYME ACTIVITY

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

Enzymes are located where?

A

In specific organelles in cell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

Compartmentalization

A

Some reactions are isolated from others avoiding competition for the substrate or enabling more favorable conditions

40
Q

Transition state

A

After the active site binds to substrate and initiates the conversion to products by transition state.
Stabilizing transition state an enzyme can greatly increase the concentration of reactive intermediate that can be converted to product accelerating the reaction

41
Q

How does an enzyme increase the concentration of an reactive intermediate?

A

Through transition state which is when the substrate is converted to a product by accelerating the reaction

42
Q

Enzymology

A

Measurement of the appearance of products as a function of time

43
Q

Leonor Michaelis-Maud equation (ENZYME VS SUBSTRATE CONCENTRATION)

A

Concentration of substrate is GREATER than the concentration of enzyme

44
Q

Leonor Michaelis-Maud equation describes what

A

describes how the velocity of reaction varies with the substrate concentration

45
Q

Leonor Michaelis-Maud equation TIME

A

Enzymatic reactions show a steady-state, ES complex does not change with time

The rate of formation of ES is equal to the rate of breakdown

46
Q

Leonor Michaelis-Maud equation VELOCITY

A

Initial velocity of reaction is used to analyze enzymatic reactions

Vo= (Vmax [S])/ (Km + [S])

47
Q

Initial velocity Michaelis

A

Vo= (Vmax [S])/ (Km + [S])

48
Q

Michaelis constant equation

A

Km= (k1+k2)/ k1

Reflects the affinity of the enzyme for substrate

49
Q

T OR F

Km is equal to the substrate concentration at which the reaction velocity is half

A

TRUE

Km= [S] THEN Vmax/2

50
Q

T OR F

Km varies with the enzyme concentration

A

FALSE

IS WITH THE SUBSTRATE CONCENTRATION

51
Q

ENZYME CONCENTRATION (MICHAELIS)

A

the rate of the reaction is DIRECTLY PROPORTIONAL to the enzyme concentration

52
Q

Order of reaction: 1st order

A

If [S] is LOWER than Km then the velocity of reaction is Nearly proportional to the concentration of substrate

53
Q

Order Zero

A

at high substrate concentration, VELOCITY of reaction is CONSTANT and EQUAL to Vmax

Rate of reaction is independent of substrate concentration

54
Q

T OR F

The plot of initial reactions velocity against substrate concentration is hyperbolic

A

TRUE

55
Q

T OR F

Allosteric enzymes show a sigmoidal curve

A

True, they do not show a Michaels kinetics

56
Q

Lineweaver-Burke plot

A

1/Vo= (Km/ Vmax[S]) + 1/Vmax

57
Q

Factors that affect reaction velocity

A

Substrate concentration
Temperature
pH
Inhibitors

58
Q

How does [S] affect velocity of reaction

A

The rate of an enzyme/catalyzed reaction increases with the substrate concentration until a maximal velocity is reached… SATURATION

59
Q

TEMPERATURE vs velocity

A

Velocity increases with temperature until a peak is reached.

Further elevation of temperature will result in decrease of velocity … DENATURATION

60
Q

DENATURATION IS?

A

when the temperature elevation is too high that it causes the velocity of the reaction to decrease

61
Q

The optical temp for most mammalian enzymes is

A

35-40 C

62
Q

pH and velocity (3)

A

Extreme pH conditions can affect reaction velocity

It affects the ionization state of active site

Denatured enzymes

63
Q

Inhibitors

A

Any substance that can diminish the velocity of an enzyme catalyzed reaction

64
Q

Reversible inhibitors

A

Bind to enzyme through NON COVALENT bonds

65
Q

Competitive inhibitors

A

Binds to the same site of substrate competing with it

66
Q

T OR F

CONPETITIVE INHIBITORS REDUCE AFFINITY, DECREASE Km, Vmax is changed

A

FALSE

REDUCE AFFINITY, INCREASE KM AMD VMAX IS UNCHANGED

67
Q

SATING DRUGS ARE AN EXAMPLE OF WHAT TYPE OF INHIBITOR?

A

COMPETITIVE, IT OCCUPIES THE ACTIVE SITE OF E HYDROXYMETHYLGLUTANYL COA REDUCTASE

68
Q

The 1st step of cholesterol synthesis is inhibited by ?

A

Competitive inhibitor

69
Q

Non competitive inhibitor

A

Binds at a different site than the substrate can also bind to free enzymes

70
Q

T OR F

NON COMPETITIVE INHIBITORS INCREASE VMAX AND CHANGE KM

A

FALSE IT DECRESES VMAX AND KM IS UNCHANGED

71
Q

Catalytic activity of enzymes depend on small molecules called

A

COFACTORS

72
Q

Cofactors are

A

Non protein molecule that work as helpers for the enzyme

73
Q

COENZYMES

A

Small organic molecules derived from vitamins and can be tightly or loosely bound to enzyme

74
Q

When coenzymes are tightly bound they’re called

A

Prosthetic groups

75
Q

Loosely bound coenzymes are

A

Co-substrates because they bind to and are released from enzymes like substrates

76
Q

Inactive precursors are activated how

A

Activated by cleavage of one of the few peptide bonds

77
Q

Zymogens

A

Inactive precursors

78
Q

T OR F

PROTEOLYTIC ACTIVATION NEEDS ATP

A

FALSE

79
Q

What is the zymogens and active site of the synthesis in stomach

A

Pepsinogen, pepsin

80
Q

What is the zymogens and active site of the synthesis in pancreas (cc, tt, pc, pe)

A

Chymotrypsogen- chymotrypsin
Trypsinogen- trypsin
Procarboxypeptidase- carboxypeptidase
Protealatase- elatase

81
Q

Proteolysis: blood clotting is mediated by

A

A cascade of PROTEOLYTIC activations that ensure a rapid and amplified response to trauma

82
Q

Fibrous protein collagen

A

Major constituent of skin and bone, derived from procollagen a soluble precursor

83
Q

Example Developmental processes in proteolysis

A

Metamorphosis

84
Q

Apoptosis

A

Programmed cell death

85
Q

Enzyme activity regulation

A

Mechanisms for regulating enzyme activities, effector, results noted in enzyme action and time required to see the effect

86
Q

Allosteric activation

A

Active site becomes AVAILABLE to the substrate when regulatory molecules bind to a DIFFERENT site on enzyme

87
Q

Allosteric deactivation

A

Active site becomes INACTIVE to the substrate when regulatory molecules binds to different site on enzyme

88
Q

What happens when modifiers bind to the enzyme in a different site than the substrate

A

It changes the affinity of the enzyme substrate reaction or modifies the maximal catalytic activity of the enzyme

89
Q

Homotropic effectors

A

When substrate serves as an effector

90
Q

Heterotopic effector

A

Effector is different from substrate

91
Q

T OR F

FEEDBACK INHIBITION IS AM EXAMPLE OR HOMOTROPOC EFFECTORS

A

FALSE IS AN EXAMPLE OF HETEROTOPIC EFFECTORS

92
Q

Covalent modificators

A

Addition or removal of a phosphate group from a specific amino acid on the enzyme (ser, thru, tyr)

93
Q

T OR F

CELLS CANNOT REGULATE THE AMOUNT OF ENZYME ALTERING THE RATE OF ENZYME DEGRADATION OR THE RATE OF SYNTHESIS

A

FALSE
THEY CAN

INCREASE= KNDUCTION
DECREASE=Repression

94
Q

How can we use enzymes in clinical diagnosis

A

Through blood tests.

95
Q

High plasma levels means

A

Damage

Cellular Biology (13 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions