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Biochemistry Module 2 > Powerpoints - Module 2 > Flashcards

Powerpoints - Module 2 Flashcards

1
Q

What is the role of Ribozymes in intron and tRNA processing?

A

Gene Therapy

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2
Q

Autocatalytic RNA molecules that can adopt complex tertiary structures like proteins. It does not have proteins and mostly made up of nucleotides.

A

Ribozymes

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3
Q

A reaction that needs high activation energy for a reaction to occur.

A

Endergonic Reaction

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4
Q

True or False. Energy release from an exergonic reaction is used to start an endergonic reaction.

A

True. Endergonic and exergonic reactions are coupled together.

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5
Q

Which of the following is not a characteristic of Biological Catalysis?
A. Temp, pressure pH sensitive
B. Greater specificity (minimal side reactions)
C. Lower reaction rates
D. Capacity for control

A

C. Higher reaction rates

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6
Q

True or False. Proteins are not subjected to denaturation and can be affected by UV radiation.

A

False. Subjected to denaturation and cannot be affected by UV radiation (non-nucleotide)

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7
Q

Catabolic enzymes that uses water to cleave linkage (ex. Pacreatic lipase - breaks down triecylglycerol)

A

Hydrolases

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8
Q

Drug that inhibits pancreatic lipase synthesis of triecylglyceride.

A

Orlistat (Xenical)

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9
Q

Reaction that facilitates atomic rearrangement within the same molecule (ex. Phosphoglucoisomerase).

A

Isomerase

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10
Q

Joining two or more chemical together (anabolic) coupled with ATP hydrolysis (Ex. Acetyl-CoA)

A

Ligase

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11
Q

Splitting a chemical into smaller parts without use of water via elimination (ex. Fructose 1,6-biphosphate aldolase)

A

Lyase

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12
Q

Transfer of electrons or hydrogen atoms from one molecule to another (ex. Lactic acid dehydrogenase)

A

Oxidoreductase

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13
Q

Moving a functional group from one molecule to another (ex. Hexokinase)

A

Transferase

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14
Q

What single bonds is broken down by Hydrolases?

A

Ester, ether, peptide or glycosidic.

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15
Q

What do you call the site other than the active site of an enzyme?

A

Allosteric site - can change the configuration of the whole enzyme including the active site

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16
Q

True or False. Urease uses the postulate Lock and Key Model.

A

True

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17
Q

True or False. Hexokinase undergo a lock and key model.

A

False. Induce fit model

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18
Q

What consists an active holoenzyme?

A

Apoenzyme and non-protein co-factor

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19
Q

True or False. Metal ions is an example of a prosthetic group.

A

True

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20
Q

Most of cofactors that participates in catalysis are derived from

A

Vitamin B

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21
Q

Coenzyme A comes from what Vitamin B?

A

Vitamin B5/B3 (Pantothenic Acid)

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22
Q

Deficiency in Vitamin B12 (Cyanocobalamin) will result to.

A

Megaloblastic anemia

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23
Q

Vitamin B that is important in the synthesis Thymidine?

A

Folic Acid

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24
Q

Carboxypeptidase cleaves

A

Carboxy- terminal of proteins

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25
Q

A metal that is important in the stabilization of ATP

A

Magnesium

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26
Q

What metal is important in neutralizing free radicals converting it to hydrogen peroxide to water?

A

Mn (Superoxide dismutase)

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27
Q

Vitamin B that increases HDL (high density lipoprotein - good cholesterol)

A

Vitamin B3 - Niacin

28
Q

Yes or No. Are the following tetrahydrobiopterin in correct relationship?

Phenylalanin -> Tyrosine
Tyrosine -> DOPA
Tryptophan -> 5-HO-Tryptophan
Arginine -> Citruline + Nitric Oxide
Etherlipid -> Aldehyde + Glycerol
A

Yes

29
Q

True or False. Magnesium acts as a positive charge shield to orevent the disintegration of ATP

A

True

30
Q

True or False. Enzymes form transition states at a HIGHER activation energy thru strategic binding and catalytic residue/cofactors

A

False. LOWER ACTIVATION ENERGY

31
Q

The following are reaction mechanisms of enzymes except:

A. Ionic Bonds
B. Electronegativity
C. Lewis acids/bases
D. Non-bonded electrons
E. Bond polarity
A

A. COVALENT bonds

32
Q

Nucleophiles : attracted to positively charge

___________. : attracted to negatively charge

A

Electrophiles

33
Q

Proteases work via covalent or acid-base catalysis, both formung an unstable ________ intermediate.

A

Tetrahedral

34
Q

What metal competes with the blood in the body and is use to treat for infection?

A

Zinc+

35
Q

What is the catalytic triad forming a charge relay network (passing of electrons)?

A

Serine (strong nucleophile that attack carbonyl C)
Histidine (accepts proton from Serine)
Aspartatic acid (stabilize protonated histidine)

36
Q

Inactive enzymes

A

Zymogens - activated by prteolysis (regulation of enzyme)

37
Q

Deep, narrow pocket with a negatively charged carboxylate.

A

Trypsin

38
Q

Wide hydrophobic pocket complements of aromatic side chains of Phe, Tyr & and aliphatic side chains of Leu & Met.

A

Chymotrypsin

39
Q

Enzymes lower the _______ of a reaction that makes them efficient catalyst.

A

Activation energy

40
Q

Its change determine the direction and equilibrium states of the reaction but NOT the speed of the reaction.

A

Free Energy

41
Q

True or False. Enzymes denature at high temperature so rate falls rapidly.

A

True

42
Q

True or False. Heat energy causes less collision between enzyme and substrate.

A

False. It causes MORE collisions.

43
Q

Optimum pH for Chymotrypsin?

A

pH 8

44
Q

True or False. Optimum pH is related to the ionization of specific amino acid residues that constitute the substrate binding site.

A

True

45
Q

Until what temperature range will the rate of enzyme-catalyzed reactions in human that generally doubles with every increase of 10 deg celsius?

A

45-55 deg Celsius (Q10 = 2)

46
Q

True or False. In a low substrate concentration, increasing its amount will increase the reaction rate.

A

True

47
Q

True or False. In a concentration with high amount of saturated enzyme, a reaction will take place if substrate are added.

A

False. Reaction WILL NOT take place (zero order kinetics)

48
Q

Substrate concentration versus reaction rate produces a rectangular _____ curve, plateauing towards enzyme saturation.

A

Hyperbolic

49
Q

It denotes a substrate concentration at half the maximal velocity

A

Michaelis constant km

50
Q

True or False. Most enzymes in the bidy are at the level of Km (first level).

A

True

51
Q

Large kM - _____ substrate affinity in forming products.

A

LOW

52
Q

Small Km - ______ substrate affinity in forming a product.

A

High

53
Q

A large Km may result from either:

A

Product is formed rapidly (Large K2) and enzyme-substrate complex dissociates rapidly (Large K1).

54
Q

It allows precise determination of Km and Vmax at less than saturating concentrations. It will convert the hyperbolic line to a straight line.

A

Double reciprocal or Lineweaver-Burk

55
Q

Alternative singe-reciprocal plots.

A

Eadie-Hofstee and Hanes-Woolf plots

56
Q

True or False. Km/Vmax corresponds to the slope

A

True

57
Q

Used to determine the concentration of enzyme and its relative activity. Use to predict the speed of reactions or catalytic efficiency.

A

Specific activity - predicts the activity of enzyme (Vmax/Protein)
Turnover number - the larger the number, the faster the reaction (Vmax/mol enzyme)
Catalytic constant - (Vmax/St)

58
Q

The equation that describes the behavior of enzymes exhibiting cooperativity.

A

Hill equation

59
Q

The best measure of catalytic efficiency

A

Kcat/Km

60
Q

Clearly show the Vmax and Km

A

Lineweaver-Burk plot

61
Q

______ inhibitor are unreactive outside the confines of the enzyme’s active site.

A

Suicide

62
Q

______ inhibitors binds to the active site preventing enzyme-substrate complex formation; lineweaver-burk plots intersect at y-axis

A

Competitive

63
Q

True or False. In competitive inhibitor, if substrate is increase it can replace the inhibitor.

A

True

64
Q

______ inhibitor will not bind to the active site but binds to the allosteric site that changes the shape of the enzyme; lineweaver-burk plots intersect at x-axis

A

Non-competitive

65
Q

True or False

Competitive Inhibitor : increase Km, unaffected Vmax
Noncompetitive Inhibitor : unaffected Km, decrease Vmax

A

True

66
Q

_____ inhibitor bind to the enzyme-substrate complex lowering both Vmax and Km; lineweaver-burk plots shows no intersection

A

Uncompetitive inhibitor

Biochemistry Module 2 (3 decks)

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