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Biochemistry: Module 2 > Enzymes: Mechanism Of Action > Flashcards

Enzymes: Mechanism Of Action Flashcards

1
Q

Essential for the breakdown of nutrients to supply energy and chemical building blocks

A

Enzymes

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2
Q

Majority of the enzymes are

A

Proteins

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3
Q

Cause of genetic defects
Nutritional deficits
Toxins

A

Enzyme deficiency or catalytic activity

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4
Q

genetic mutation or infection by viral or bacterial pathogens

A

Defective enzymes

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5
Q

Enzymes that catalyze oxidation and reduction

A

Oxidoreductase

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6
Q

Enzymes that catalyze transfer of moieties such as
Glycosyl
Methyl
Phosphoryl group

A

Transferase

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7
Q 
Enzymes that catalyze hydrolytic cleavage:
C-C
C-O
C-N
Other covalent bonds
A

Hydrolases

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8
Q

Enzymes that catalyze cleavage of c-c, c-o, c-n and other covalent bond by atom elimination, generating double bonds

A

Lyases

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9
Q

Enzymes that catalyze geometric or structural change within molecule

A

Isomerase

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10
Q

Enzymes that catalyze the joining together f two molecules in reaction coupled to the hydrolysis atp

A

Ligases

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11
Q

Unambiguous system of enzyme nomenclature

A

International union of biochemist

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12
Q

Biological polymers that catalyze the chemical reaction

A

Enzymes

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13
Q

Tightly and stably incorporated into a protein structure by covalent and non covalent forces

A

Prosthetic groups

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14
Q

Most common prosthetic groups

A

Metals

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15
Q

One third of all enzymes that contain tigthly bound metal ions

A

Metalloenzymes

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16
Q

It may facilitate the binding and orientation of substrates, the formation of covalent bonds

A

Metals

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17
Q

Binds in transient, dissociable manner either to enzymes or to a substrate

A

Co factors

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18
Q

It must be present in the medium surrounding the enzyme for catalysis to occur

A

Cofactor

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19
Q

Most common cofactor

A

Metal ions

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20
Q

Enzymes that require a metal ion cofactor

A

Metal activated enzyme

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21
Q

Metal ions serves as prosthetic group

A

Metalloenzymes

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22
Q

A component of the redox coenzyme NAD and NADP

A

Nicotinamide

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23
Q

Component of the redox coenzyme FMN and FAD

A

Riboflavin

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24
Q

Component of the acyl group carrier co enzyme A

A

Pantothenic acid

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25
Q

Partipates in decarboxylation of a-keto acids

A

Thiamin

26
Q

Coenzymes function in one carbon metabolism

A

Folic acid and cobamide

27
Q

It has the capacity to shield substrates from water

A

Active site

28
Q

Catalysis occurs where?

A

Active site

29
Q

Creation of a region of high substrate concentration once binding begins

A

Catalysis by proximity

30
Q

Due to ionizable aminoacyl side chains or prosthetic groups contribute to the catalysis by acting as acid and base

A

Acid base catalysis

31
Q

Conformational change that weakens covalent bond, involves breaking covalent bond

A

Catalysis by strain

32
Q

Involves the formation of a covalent bond between the enzyme and one or more substrate

A

Covalent catalysis

33
Q

Catalysis where Enzymes temporarily becomes reactant

A

Covalent catalysis

34
Q

Is common among enzymes that catalyze group transfer reaction

A

Covalent catalysis

35
Q

It is the residues on the enzyme that participate in covalent catalysis

A

Cystein or serine and histidine

36
Q

It is accounted for the exquisite specificity of enzyme-substrate interaction

A

Lock and key model

37
Q

It states that when substrates approach and bind to an enzyme, they induce a conformational change analogous to placing a hand into a glove.

A

Induced fit model

38
Q

Alteration in the active site as enzymes and substrate bind

A

Induced fit model

39
Q

Involves direct hydrolytic attack of water on a peptide bond

A

Catalysis by aspartic protease

40
Q

Involves prior formation of a covalent acyl-enzyme intermediate

A

Serine protease chymotrypsin

41
Q

They constitute the charge relay network

A

Serine 195
Histidine 57
Aspartate 102

42
Q

Proteins in charge relay network

A

Aspartate 102
Histidine 57
Serine 195

43
Q

Binding of substrates initiates _____ that in effect transfer the hydroxyl proton of serine 195 to aspartate 102

A

Proton shift

44
Q

The enhanced nucleophility of the seryl oxygen facilitates its attack on the carbonyl carbon of the peptide bond of the substrate forming a covalent

A

Acyl-enzyme intermediate

45
Q

Regulatory enzyme of gluconeogenesis

A

Fructose 2-6 biphosphate

46
Q

It cleaves peptide bonds on the carboxyl terminal side of a large hydrophobic amino acid

A

Chymotrypsin

47
Q

It cleaves peptide bonds on the carboxyl terminal side of basic amino acids

A

Trypsin

48
Q

Proteins that diverge from common ancestor are said to be

A

Homologous

49
Q

Enzymes that arise through gene duplication

A

Isoenzyme

50
Q

An enzyme that provides a backup copy of an essential enzyme

A

Isoenzyme

51
Q

The rate of catalytic reaction being monitored is proportionate to…

A

Amount of enzyme present

52
Q

Measure the rate of single catalytic events and sometimes the individual steps in catalysis

A

Single molecule enzymology

53
Q

The first enzymes used to diagnose myocardial infarction

A

Aspertate aminotransferase AST
Alanine amino transferase ALT
Lacatate dehydrogenase

54
Q

It is a tetrameric enzyme consisting of 2 monomers types

A

Lactate dehydrogenase or LDH

55
Q

An isoenzyme that predominates the heart tissues

A

Isoenzyme I1

56
Q

An isoenzyme that predominates the liver

A

Isoenzyme I5

57
Q

Marker for myocardial infarction

A

Lactate dehydrogenase

58
Q

It is a complex of three proteins involved in muscle contraction in skeletal and cardiac but not in smooth muscle

A

Troponins

59
Q

troponin level rises for _____ after an MI and remain elevated for _____

A

2-6 hours, 4-10 days

60
Q

Marker of all heart muscle damage

A

Troponin

61
Q

It is used in the treatment of acute MI

A

Tissue plasminogen activator tPA or streptokinase

62
Q

It has been used to treat cystic fibrosis

A

Trypsin

Biochemistry: Module 2 (5 decks)

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