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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
effects the removal of components of water from double bond
Dehydrase
26
effects addition of components of water to double bond
Hydratase
27
Catalyzes isomerisation ; converts it into molecule, isomeric (rearrangements)
Isomerase
28
catalyzes formation of bond between 2 mol with Atp
Ligase
29
part of enzyme structure involve in catalysis; folding & bending of protein
Active site
30
reaction species formed when substrate binds to active site
Enzyme-substrate complex
31
enzyme w fixed, rigid geometrical conformation ; substrates w complementary geometry
Lock & key model
32
active site allow small changes to accommodate substrate ; forced nga isulod
Induced fit model
33
Enzyme specificity
Absolute Group Linkage Stereochemical
34
most general of common specificities ; enzyme act on particular type of chemical bond
Linkage specificity
35
enzyme will act on particular stereoisomer ; inherent chirality
Stereochemical specificity
36
measure of rate which an enzyme converts substrate to product in biochem reaction
Enzyme activity
37
Factors that affect enzyme activity
Temperature pH Substrate concentration Enzyme concentration
38
causes molecules to move faster & collide frequently ; increase rate of reaction
Temperature
39
temperature at which enzyme exhibits maximum activity
Optimum temperature
40
optimum pH range for most enzymes are?
7.0 to 7.5
41
at a constant enzyme concentration, the enzyme activity___ with ____ substate concentration
increases with increased substate concentration
42
number of substrate molecules converted to product per minute by 1 mol of enzyme under optimum conditions of temp, ph & saturation
Turnover number
43
Are enzymes consumed in the reaction they catalyze?
No
44
The greater the enzyme concentration , _____ the reaction rate
greater
45
organisms that thrive in extreme environments
Extremeophiles
46
microbial enzymes that are active that would inactivate human enzymes
Extremozymes
47
substance that slows down catalytic function of enzyme ; binds it
Enzyme inhibitor
48
molecule that resembles enzyme substrate in shape & charge distribution
Competitive inhibitor
49
binds to enzyme at a location other than active site ; causes change to structure of enzyme
Noncompetitive inhibitor
50
inactivates enzymes ; forms strong covalent bond to amino acid side chain with enzyme active site
Irreversible enzyme inhibitor
51
the enzyme is permanently _____ in the irreversible inhibition
inactivated
52
examples of irreversible enzyme inhibitor
chemical warfare agents
53
mechanisms involved in regulations
Allosteric control Feedback control Covalent modification control
54
Allosteric enzymes have _____ structure
Quaternary structures
55
In a feedback control, the activation or inhibition of the first reaction is controlled by
the product of the sequence
56
regulators of an allosteric enzyme
- hormones - products of diff pathways of reaction within the cell
57
catalyzes breaking of peptide bonds
Proteolytic enzyme
58
proteolytic enzymes examples
Digestive & blood-clotting enzymes
59
involves adding or removing a chemical group within an enzyme (phosphate group)
Covalent modification
60
substance that kills bacteria/inhibits growth
Antibiotic
61
increases blood pressure (narrows blood vessels)
Angiotensin
62
competitive inhibitor of enzymes converts PABA to folic acid in bacteria
Sulfanilamide
63
retards bacterial growth & kills them
Folic acid deficiency
64
who discovered penicillins
Alexander Fleming
65
structure of Penicillins
4 membered beta-lactam ring ; 5 membered thiazolidine ring
66
Enzymes in organs indicate:
organ/tissue damage
67
how can blood clots in the heart be dissolved
activate plasminogen using TPA
68
converts urea into ammonia in blood
Enzyme urease
69
the human body can not synthesize vitamins
TRUE
70
Classes of vitamins
water-soluble lipid-soluble
71
in humans, ____mg/day saturates all body tissues
100mg
72
mg/day in britain: USA & Canada: Germany:
30 60 75
73
general antioxidant ; synthesize neurotransmitters ; co substrate in formation of structural protein collagen
Vitamin C
74
precursors for enzyme cofactors
Vitamin B
75
vitamins involved in processes in cell membranes
A, D, E & K
76
Vitamin A is derived from
beta carotene
77
Vitamin A combines with the ____ to form rhodopsin
Protein opsin
78
Rhodopsin participates in conversion of:
light energy into nerve impulse to the brain
79
process where immature cells change in structure to become specialize cells ; regulated by vitamin A
Cell differentiation
80
Vitamin A maintains health of ___ tissues
Epithelial
81
In vitamin A, reproduction and growth is involved
TRUE
82
Vitamin D is also knows as
Calciferol
83
Vitamin D that is synthesized by sunlight
D3
84
Vitamin D maintains normal blood levels of ______ for bones
calcium ion phosphate ion
85
most active biological Vitamin E
Alpha-tocopherol
86
Primary function of Vitamin E is
AntiOxidant
87
Vitamin k found in green vegetables
K1
88
Vitamin k synthesized by intestinal bacteria
K2
89
Vitamin K is essential for formation of:
Proteins

BIOCHEM (8 decks)

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