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BIOCHEM > ENZYMES > Flashcards

ENZYMES Flashcards

1
Q

these are proteins that act as catalysts for biochemical reaction

A

Enzymes

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2
Q

what do you call the substance that speed up the rate of reaction

A

Catalyst

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3
Q

Do enzymes undergo denaturation?

A

Yes

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4
Q

what are enzymes that have only proteins?

A

Simple enzyme

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5
Q

enzyme that has non-protein and protein parts

A

Conjugated enzyme

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6
Q

3 conjugated enzymes

A

Apoenzyme
Cofactor
Holoenzyme

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7
Q

what do you call the protein part of a conjugated enzyme

A

Apoenzyme

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8
Q

What do you call the non protein part of conjugated enzyme

A

Cofactor

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9
Q

This is the biochemically active conjugated enzyme

A

Holoenzyme

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10
Q

What enzyme provides chemically reactive functional groups

A

Cofactors

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11
Q

these are small organic molecules & the cofactor in conjugated enzyme

A

Coenzyme

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12
Q

These are synthesized in the human body using building blocks from nutrients

A

Coenzymes

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13
Q

this is the reaction catalyzed & substrate identity ; target area of enzyme

A

Focal points

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14
Q

what do you call the reactant in an enzyme-catalyzed reaction ; this is where the enzyme acts

A

Substrate

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15
Q

Classes of enzymes

A

Oxidoreductases
Transferases
Hydrolases
Lyases
Isomerase
Ligases

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16
Q

what enzyme requires a coenzyme that is oxidized or reduced as the substrate is reduced

A

Oxidoreductase

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17
Q

this enzyme catalyzes transfer of a functional group from 1 molecule to another

A

Transferase

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18
Q

what enzyme catalyzes transfer of amino group to another molecule

A

Transaminase

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19
Q

what enzyme catalyzes the transfer of phosphate group from ATP - ADP

A

Kinase

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20
Q

this enzyme involves addition of water mol to bond to break ; catalyze hydrolysis

A

Hydrolase

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21
Q

this enzyme hydrolyzes glycosidic bonds in oligo and polysacch

A

Carbohydrase

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22
Q

enzyme that effects breaking of peptide linkages in proteins

A

Protease

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23
Q

effects break of ester linkages in triacylglycerol

A

Lipase

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24
Q

additio/ removal group to form double bond ; no hydrolysis / oxidation

A

Lyase

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25
Q

effects the removal of components of water from double bond

A

Dehydrase

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26
Q

effects addition of components of water to double bond

A

Hydratase

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27
Q

Catalyzes isomerisation ; converts it into molecule, isomeric (rearrangements)

A

Isomerase

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28
Q

catalyzes formation of bond between 2 mol with Atp

A

Ligase

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29
Q

part of enzyme structure involve in catalysis; folding & bending of protein

A

Active site

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30
Q

reaction species formed when substrate binds to active site

A

Enzyme-substrate complex

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31
Q

enzyme w fixed, rigid geometrical conformation ; substrates w complementary geometry

A

Lock & key model

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32
Q

active site allow small changes to accommodate substrate ; forced nga isulod

A

Induced fit model

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33
Q

Enzyme specificity

A

Absolute
Group
Linkage
Stereochemical

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34
Q

most general of common specificities ; enzyme act on particular type of chemical bond

A

Linkage specificity

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35
Q

enzyme will act on particular stereoisomer ; inherent chirality

A

Stereochemical specificity

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36
Q

measure of rate which an enzyme converts substrate to product in biochem reaction

A

Enzyme activity

37
Q

Factors that affect enzyme activity

A

Temperature
pH
Substrate concentration
Enzyme concentration

38
Q

causes molecules to move faster & collide frequently ; increase rate of reaction

A

Temperature

39
Q

temperature at which enzyme exhibits maximum activity

A

Optimum temperature

40
Q

optimum pH range for most enzymes are?

A

7.0 to 7.5

41
Q

at a constant enzyme concentration, the enzyme activity___ with ____ substate concentration

A

increases with increased substate concentration

42
Q

number of substrate molecules converted to product per minute by 1 mol of enzyme under optimum conditions of temp, ph & saturation

A

Turnover number

43
Q

Are enzymes consumed in the reaction they catalyze?

A

No

44
Q

The greater the enzyme concentration , _____ the reaction rate

A

greater

45
Q

organisms that thrive in extreme environments

A

Extremeophiles

46
Q

microbial enzymes that are active that would inactivate human enzymes

A

Extremozymes

47
Q

substance that slows down catalytic function of enzyme ; binds it

A

Enzyme inhibitor

48
Q

molecule that resembles enzyme substrate in shape & charge distribution

A

Competitive inhibitor

49
Q

binds to enzyme at a location other than active site ; causes change to structure of enzyme

A

Noncompetitive inhibitor

50
Q

inactivates enzymes ; forms strong covalent bond to amino acid side chain with enzyme active site

A

Irreversible enzyme inhibitor

51
Q

the enzyme is permanently _____ in the irreversible inhibition

A

inactivated

52
Q

examples of irreversible enzyme inhibitor

A

chemical warfare agents

53
Q

mechanisms involved in regulations

A

Allosteric control
Feedback control
Covalent modification control

54
Q

Allosteric enzymes have _____ structure

A

Quaternary structures

55
Q

In a feedback control, the activation or inhibition of the first reaction is controlled by

A

the product of the sequence

56
Q

regulators of an allosteric enzyme

A
  • hormones
  • products of diff pathways of reaction within the cell
57
Q

catalyzes breaking of peptide bonds

A

Proteolytic enzyme

58
Q

proteolytic enzymes examples

A

Digestive & blood-clotting enzymes

59
Q

involves adding or removing a chemical group within an enzyme (phosphate group)

A

Covalent modification

60
Q

substance that kills bacteria/inhibits growth

A

Antibiotic

61
Q

increases blood pressure (narrows blood vessels)

A

Angiotensin

62
Q

competitive inhibitor of enzymes converts PABA to folic acid in bacteria

A

Sulfanilamide

63
Q

retards bacterial growth & kills them

A

Folic acid deficiency

64
Q

who discovered penicillins

A

Alexander Fleming

65
Q

structure of Penicillins

A

4 membered beta-lactam ring ; 5 membered thiazolidine ring

66
Q

Enzymes in organs indicate:

A

organ/tissue damage

67
Q

how can blood clots in the heart be dissolved

A

activate plasminogen using TPA

68
Q

converts urea into ammonia in blood

A

Enzyme urease

69
Q

the human body can not synthesize vitamins

A

TRUE

70
Q

Classes of vitamins

A

water-soluble
lipid-soluble

71
Q

in humans, ____mg/day saturates all body tissues

A

100mg

72
Q

mg/day in
britain:
USA & Canada:
Germany:

A

30
60
75

73
Q

general antioxidant ; synthesize neurotransmitters ; co substrate in formation of structural protein collagen

A

Vitamin C

74
Q

precursors for enzyme cofactors

A

Vitamin B

75
Q

vitamins involved in processes in cell membranes

A

A, D, E & K

76
Q

Vitamin A is derived from

A

beta carotene

77
Q

Vitamin A combines with the ____ to form rhodopsin

A

Protein opsin

78
Q

Rhodopsin participates in conversion of:

A

light energy into nerve impulse to the brain

79
Q

process where immature cells change in structure to become specialize cells ; regulated by vitamin A

A

Cell differentiation

80
Q

Vitamin A maintains health of ___ tissues

A

Epithelial

81
Q

In vitamin A, reproduction and growth is involved

A

TRUE

82
Q

Vitamin D is also knows as

A

Calciferol

83
Q

Vitamin D that is synthesized by sunlight

A

D3

84
Q

Vitamin D maintains normal blood levels of ______ for bones

A

calcium ion
phosphate ion

85
Q

most active biological Vitamin E

A

Alpha-tocopherol

86
Q

Primary function of Vitamin E is

A

AntiOxidant

87
Q

Vitamin k found in green vegetables

A

K1

88
Q

Vitamin k synthesized by intestinal bacteria

A

K2

89
Q

Vitamin K is essential for formation of:

A

Proteins

BIOCHEM (8 decks)

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