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Biochemistry > Module 04: Enzymes (Comprehensive) > Flashcards

Module 04: Enzymes (Comprehensive) Flashcards

1
Q

These are specialized proteins with catalytic properties

A

Enzymes

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2
Q

This specificity pertains to stereoisomer

A

stereochemical specificity

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3
Q

This specificity pertains to substrate it will act upon

A

absolute specificity

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4
Q

This specificity pertains to the type of bond/linkage

A

linkage specificity

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5
Q

Chemical reactions need an initial input of energy to reach this.

A

Activation Energy

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6
Q

During the activation energy, the molecules are said to be in what?

A

Transition state

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7
Q

This provides an alternate route, one with lower energy of activation and it stabilizes the transition state

A

Enzyme Controlled Pathway

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8
Q

Describe the structure of the active site.

A

Cleft or pocket on the enzyme’s surface, With catalytic and binding sites, where catalysis occurs (at catalytic residues)

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9
Q

Where is the active site located?

A

Located at the interface between subunits of multimeric enzymes (Shields the substrate from solvent)

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10
Q

An additional non-protein molecule that is needed by some enzymes to help the reaction. These are small organic or metalloorganic molecules or metal ions.

A

Cofactor

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11
Q

Tightly bound cofactors are called _______________..

A

prosthetic groups (heme in hemoglobin)

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12
Q

Organic cofactors that are bound and released easily are called ____________ and are commonly activated by vitamins.

A

coenzymes

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13
Q

These can associate and disassociate from enzymes between reactions cycles thus behaving like substrates.

A

Weakly bound coenzymes (cosubstrates)

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14
Q

This is the protein part of an enzyme that is inactive. It requires a cofactor to be active.

A

Apoenzyme

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15
Q

This is the complete catalytically active enzyme

A

Holoenzyme

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16
Q

This is the enzymes requiring metal ions as cofactor

A

Metalloenzyme

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17
Q

These function as group transfer agents, Transport substrates from port of generation to port of utilization. They are usually derived from vitamins.

A

Coenzymes

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18
Q

These coenzymes transfer H atoms or Hydrides

A

NAD+ (Nicotinic acid/niacin/B3 )

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19
Q

These coenzymes transfer methyl group.

A

folates

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20
Q

These coenzymes transfer acyl group.

A

Pantothenic acid/B5 (Coenzyme A)

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21
Q

These coenzymes transfer oligosaccharides.

A

dolichol

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22
Q

These coenzymes transfer Electrons .

A

Riboflavin/B2 (FAD and FMN)

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22
Q

These coenzymes transfer aldehyde group transfer.

A

Thiamine/B1 (thiamin pyrophosphate/TPP)

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23
Q

These coenzymes transfer Activated CO2 group transfer

A

Biocytin (Biotin)

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24
Q

These coenzymes transfer One C group transfer

A

Folic acid (Tetrahydrofolate/THF)

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25
Q

These coenzymes transfer H and alkyl groups
Electrons & acyl groups

A

(1) Deoxyadenosyl cobalamin (B12)
(2) Lipoic acid (lipoate) is not required in the diet

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26
Q

These are the reactants that are acted upon/activated by the enzyme

A

substrates

27
Q

The specificity is determined by the “________________”

A

active site

28
Q

In this theory of specificity, the fit between the substrate and the active site of the enzyme is exact Like a key fits into a lock very precisely. The key is analogous to the substrate and the enzyme analogous to the lock

A

The Lock and Key Hypothesis

29
Q

What is the temporary structure of the lock and key hypothesis?

A

Temporary structure called the enzyme-substrate complex /ES complex formed

30
Q

What happens when the enzyme-substrate is formed/

A

Once formed, they are released from the active site leaving it free to become attached to another substrate

31
Q

Dehydrogenase, oxidase are examples of what

A

Oxidoreductase enzymes

32
Q

Kinase, amino transferase are examples of what

A

Transferase

33
Q

Esterase, glycosidase, peptidase, phosphatase, phospholipase are examples of what?

A

Hydrolase

34
Q

Decarboxylase, synthase are examples of what

A

Lyase

35
Q

Epimerase, mutase are examples of what

A

Isomerase

36
Q

Synthetase, carboxylase are examples of what

A

Ligase

37
Q

The substrate concentration in non-enzymatic reactions is directly proportional to what

A

The increase in velocity is proportional to the substrate concentration (Faster reaction but it reaches a saturation point when all the enzyme molecules are occupied)

38
Q

Faster reaction but it reaches a saturation point when all the enzyme molecules are occupied, this stage is called the

A

Vmax

39
Q

What happens when you alter the concentration

A

If you alter the concentration of the enzyme then Vmax will change too.

40
Q

What happens when there is Extreme pH levels

A

Extreme pH levels will produce denaturation (The active site is distorted and the substrate molecules will no longer fit in it)

41
Q

These changes affects binding of the substrate with the active site.

A

small changes in the charges of the enzyme and its substrate molecules will occur ( change in ionization)

42
Q

What is the temperature coefficient?

A

Q10 (the temperature coefficient) - the increase in reaction rate for every 10°C rise in temperature.

43
Q

What does the Q10 = 2 to 3 mean?

A

(the rate of the reaction doubles or triples with every 10°C rise in temperature)

44
Q

BUT at high temperatures (beyond the optimum) proteins denature at around _______

A

70°C

45
Q

In terms of enzyme concentration, the increase in velocity is proportional to what?

A

The increase in velocity is proportional to the enzyme concentration

46
Q

What are the uses of the double reciprocal plot?

A

(1) The biggest advantage to using the double reciprocal plot is a more accurate determination of VMax, and hence KM.
(2) The x intercept value is equal to -1/KM.
(3) It is also useful in characterizing the effects of enzyme inhibitors and distinguishing between different enzyme mechanisms.

47
Q

What are the different types of irreversible inhibition?

A

(1) group specific covalent modifying agents
(2) Affinity labels
(3) Transition state analogs
(4) Suicide inhibitors

48
Q

These react with specific type of functional group or any enzyme protein.

A

group specific covalent modifying agents

49
Q

These are enzymes in nucleotide biosynthesis (new nucleic acids required for cell division)

A

dihydrofolate reductase

50
Q

This inhibits vertebrae DHRF and selectively kills rapidly dividing cells.

A

Methotrexate

51
Q

This inhibits prokaryotic DHFR.

A

Trimethoprim

52
Q

This pertains as to how Eukaryotic cells are divided into organelles which often allows for separation of opposing processes.

A

Compartmentation

53
Q

Fatty acid oxidation occurs in the

A

mitochondria

54
Q

synthesis occurs in the .

A

cytosol

55
Q

These are different forms of an enzyme found in different organelles or different tissues but Catalyze the same reaction

A

Isozymes

56
Q

A tetramer whose subunits occur in two forms (H for heart) and (M for muscle)

A

Isozymes of Lactate DH(LDH)

57
Q

How do Isozymes differ?

A

(1) Substrate affinity (glucokinase and hexokinase)
(2) Sensitivity to regulatory factors

58
Q

This isozymes predominates in the heart

A

I1 or H4

59
Q

This isozymes predominates in the liver

A

I5 or M4

60
Q

Elevation in I1 or I5 is detected by

A

separating oligomers of LDH by electrophoresis

61
Q

Dimeric CK has two types of protomers:

A

muscle (M) and brain (B).

62
Q

Heart muscle has

A

CK2 (MB) and CK3 (MM).

63
Q

This is found exclusively in heart muscle.

A

CK2

64
Q

When is CK2 released?

A

CK2 is released 6 hrs. after chest pain and reaches a maximum after 18 hrs.

65
Q

These are enzymes tested for the diagnosis of MI

A

Troponin, lactate dehydrogenase and creatine kinase

66
Q

This is the more definitive diagnostic test because it is more cardiac specific than the others

A

Troponin

Biochemistry (16 decks)

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