Brainscape's Knowledge GenomeTM

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


See full index

Biochemistry Lab > Enzymes > Flashcards

Enzymes Flashcards

1
Q

Biomolecules that function as catalysts

A

Enzymes

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

All enzymes are ___

with an exception to ____

A

proteins

Some RNAs can catalyse their own self-cleavage

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

Enzymes can increase the rate of a reaction by

A

10^20

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

rate of reactions

catalyzed:
uncatalyzed:

A

catalyzed: 10^20
uncatalyzed: 10^9

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

Lowers the activation energy

A

enzymes

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

a higher curve in the graph means

A

uncatalyzed because requires more activation energy

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

a lower curve in the graph means

A

catalyzed because there is a low activation energy required

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

For an enzyme to function optimally, you have to satisfy these conditions:

A

All the active sites of the enzyme is saturated with the substrate

Optimum pH

Optimum temperature

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

helps us approximate the original dynamics under the assumption that the concentration of the enzyme remains constant

A

Michaelis-Menten equation plot

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

As the enzyme gets consumed

A

the more steeper the curve is but at the same time the lesser concentration is needed

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

shows that the concentration of the substrate when the reaction velocity is equal to half of the maximum velocity of the reaction

A

Km

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

When enzyme gets consumed, the more steeper the curve is and

A

the faster the reaction

Higher binding affinity means lower Km and
lower substrate concentration is needed

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

Relationship of binding affinity and substrate concentration

A

inversely proportional

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

a measure of how well the substrate complexes with the given enzyme
binding affinity

A

Michaelis-menten equation

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

used for analyzing how enzymes kinematics change in the presence of either competitive or noncompetitive inhibitor

A

Lineweaver-Burk Plot

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

What are the classification of enzymes

A 
Oxidoreductase
Transferases
Hydrolases
Lyases
Isomerases
Ligases
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Transfer of hydrogen and oxygen atoms or electrons from one substrate to another

A

Oxidoreductase

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

Transfer of electrons (hydride ions or H atoms and O atoms) from one substrate to another

A

Oxidoreductase

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

Examples of Oxidoreductase

A

Oxidases,
Reductases,
Dehydrogenases

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

important reaction in anaerobic glycolysis

A

Lactate dehydrogenase

Oxidoreductase

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

Catalyze transfer of a group from one substrate (donor) to another (acceptor)

A

Transferases

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

Transfer of specific group (a phosphate or methyl et.) from one substrate to another

A

Transferases

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

Examples of Transferases

A

Kinases (phosphate grp),

Transaminases (amino grp)

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

Enzyme that undergoes transferases of phosphate group

A

Kinases

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

Enzyme that undergoes transferases of amino group

A

transaminases

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

Catalyzes hydrolysis (which is the addition of H2O) of C-C, C-O, C-N and bonds like phosphoanhydride

A

Hydrolases

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

Examples of Hydrolases

A

Estrases, Digestive enzymes (trypsin, chymotrypsin) Acetylcholinesterase

Proteases (peptide bonds), 
Phosphatases (Phosphoester bond), 
Glycosylases (glycosidic bond), 
Nucleases (phosphosugar bond), 
Esterases (ester bonds)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

A cholinergic enzyme

Found at post-synaptic neuromuscular junctions and muscles and nerves

A

Acetylcholinesterase

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

Catalyze addition (other than H2O) of groups to double bonds of removal of groups to form double bonds

A

Lyases

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

Nonhydrolytic removal of a group or addition of a group to a substrate

A

Lyases

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

Examples of Lyases

A

Decarboxylases (removal of CO2)
Dehydratases (removal of H2O)
Aldolases (cleavage of aldol)

32
Q

Convert the substrate into an isomer

A

Isomerase

33
Q

Transfer of groups within molecules to form isomers

A

Isomerase

34
Q

change of the molecular form of the substrate

A

Isomerase

35
Q

Examples of Isomerase

A 
Racemases (D-L isomers)
Epimerases (sugar epimers)
Cis-trans-Isomerases
Tantomerases (keto-enol groups)
Mutases (functional/positional isomers)
36
Q

Joining 2 molecules with the hydrolysis of ATP

A

Ligases

37
Q

joining of two molecules by the formation of new bonds

A

Ligases

38
Q

Examples of Ligases

A

Carboxylase
Synthetase
tRNA synthetase
Citric acid synthetase

39
Q

Assists movement of another molecule across a cell membrane

A

Translocases

40
Q

Movement of ion or molecules across a membrane or their separation within a membrane

A

Translocases

41
Q

Involved in fatty acid metabolism

A

Carnitine acylarnitine translocase (CACT)

42
Q

Example of Translocases

A

Carnitine translocase

Adenine nucleotide transclocase (ANT)

Carnitine acylarnitine translocase (CACT)

43
Q

Helps convert long chain fatty acids into energy

A

Carnitine acylarnitine translocase (CACT)

44
Q

Used by the cells to produce fats and energy
Without this, it will lead to low blood sugar (wont breakdown the fats) and ketone bodies within the first 48 hours for infants (?) and development of (?), seizures, sudden infant death.

A

Carnitine acylarnitine translocase (CACT)

45
Q

EC NUMBER 1.2.3.4

1=
2=
3=
4=

A 
1= main class
2= specific functional groups
3= # cofactors ?
4= specific to substrates
46
Q

reducing Sugars Assay Using

A

Dinitrosalicylic (DNS) Colorimetric Method

47
Q

Chemical nature of enzymes

A

Majority are proteins

some are RNA ~ ribozymes

48
Q

Functions at milder reaction conditions

A

enzymes

49
Q

Efficient in catalyzing high reaction rate than a chemical catalyst

A

enzymes

50
Q

Some catalyze the reaction of only one stereoisomer; others catalyze a family of similar reactions

A

Greater reaction specificity

51
Q

biological catalysts accelerate rate of biochemical reactions

A

enzymes

52
Q

It accelerates the rate of a reaction by

A

reducing free energy activation.

A factor of up to 1020 over an uncatalyzed reaction

53
Q

TRUE OR FALSE

Enzymes are not regenerated after the reaction

A

FALSE

It is regenerated after the reaction.

54
Q

TRUE OR FALSE

Enzymes does not change the equilibrium of the reaction.

A

TRUE

55
Q

biomolecule acted upon by the enzyme

A

Substrate

56
Q

specific region of the enzyme that creates a 3D surface complementary to the substrate

A

Active site

57
Q

pH at which an enzyme exhibits maximum activity (achieves Vmax)

A

Optimal pH

58
Q

maximum reaction rate

A

Vmax

59
Q

what will happen when there is a Slight change in pH

A

alters the charge of acidic and basic amino acid residues found in active site.

60
Q

What will happen in Extreme pH (too acidic/basic)

A

denatures enzyme irreversibly; loss of catalytic activity.

61
Q

temperature at which an enzyme exhibits maximum activity

A

Optimal temperature

62
Q

at higher temperature, molecules are at their excited state =

A

more kinetic energy = faster reaction rate = more products

63
Q

beyond optimum Temperature what is disrupted

A

disrupts tertiary structure of enzyme = substrate may not fit the active site = impedes catalytic reaction

64
Q

TRUE OR FALSE

alteration in enzyme conformation by change in temperature is reversible

A

FALSE

alteration in enzyme conformation by change in temperature may be reversible or irreversible (point of no return)

65
Q

yeast-derived enzyme

A

invertase

66
Q

IUPAC name of invertase and EC number

A

β-fructofuranosidase (EC 3.2.1.26)

67
Q

β-fructofuranosidase is considered a what type of enzyme

A

Hydrolase

catalyzing hydrolysis of the terminal non-reducing β-fructofuranoside residues

68
Q

Invertase hydrolases

A

α1 - β2 glycosidic bond in sucrose

69
Q

Invertase splits what

A

sucrose to glucose and fructose

70
Q

Mechanism of Invertase

A

α1-β2 linkage cleaved off by invertase to produce glucose and fructose

71
Q

used to monitor enzyme activity

A

dinitrosalicylic acid method

72
Q

MEchanism of DN

A

3,5-dinitrosalicylic acid (DNS) reacts with reducing sugars to form 3-amino-5-nitrosalicylic acid (ANS) Gluconic acid

73
Q

TRUE OR FALSE

DNS does not react with sucrose

A

True

Sucrose is a non-reducing sugar

74
Q

Red coloration means

A

higher concentration of glucose and fructose = higher invertase activity

75
Q

Sucrose + DNS = what color

A

No color change

76
Q

Sucrose + Sucrase + DNS = what color

A

Red brown coloration

Biochemistry Lab (2 decks)

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