Lec 5: Molecules, energy and biosynthesis Flashcards

(65 cards)

1
Q

Types of biological molecules

A
  • Lipids
  • Carbohydrates
  • Proteins
  • Nucleic acids
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2
Q

diverse group of water insoluble biological molecules

A

Lipids

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3
Q

energy stores

A

fats

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4
Q

major components of membrane

A

-phospholipids
-sterols

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5
Q

are called polyhydroxy aldehydes and ketones

A

Carbohydrates

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6
Q

general formula for carbohydrates

A

(CH2O)n

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7
Q

most complex and most abundant organic molecules

A

Proteins

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8
Q

What does proteins contains

A
  • atleast one carboxyl
  • one amino group
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9
Q

contents of nucelic acid

A
  • 5 carbon sugar
  • phosphate grouo
  • nitrogenous base
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10
Q

Main classes of Nucleic acids

A
  • DNA (deoxyribonucleic acid)
  • RNA (ribonucleic acid)
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11
Q

carries coded information, arranged into genes

A

DNA

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12
Q

instrumental in translating the coded message of DNA into amino acid

A

RNA

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13
Q

The process of increasing the rate of reaction with the use of a catalyst

A

Catalysis

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14
Q

any substance that increases rate of reaction

A

catalyst

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15
Q

Catalyst of biochemical reactions

A

Enzymes

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16
Q

How does enzyme increase reaction rate

A

by means of lowering the energy of activation

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17
Q

reactions catalyzed by enzymes are usually
____ to ___times faster than uncatalyzed reactions.

A

10^3 to 10^17

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18
Q

The kinetic energy required to bring the reactants into position to interact

A

Activation energy/free energy of activation

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19
Q

molecule form when enzyme binds with substrate

A

Enzyme-sustrate complex

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20
Q

each enzyme is specific for a certain substrate

A

Enzyme specificity

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21
Q

The enzyme will act on a particular steric or optical isomer

A

Stereospecificity

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22
Q

The enzyme will act on a particular type of chemical bond

A

Bond specificty

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23
Q

highly specific nature of most enzymes arises from the close and complementary fit between enzymes and substrate in a special portion of the enzyme surface

A

Active site

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24
Q

Two models for enzyme action

A
  • Lock-and-key model
  • Induced fit model
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25
that the active site of an enzyme will undergo a conformational change when binding a substrate, to improve the fit
Induced fit model
26
The active site of an enzyme is structured to fit a specifically shaped substrate
lock-and-key model
27
Mechanism of catalysis by enzymes
- Enzyme activity - Turnover number
28
catalytic potency of an enzyme
Enzyme activity
29
number of reactions catalyzed per second by the enzyme
Turnover number
30
Substrate interacts with the active site of the enzyme, forming an enzyme-substrate complex
Enzymatic reaction
31
How does enzyme accelerate reactions?
- holds substrates in close proximity to one another - form an unstable intermediate - presence of proton donors and acceptors
32
Factors affecting enzyme activity
- Temperature - Reaction rates
33
small organic molecules that act as cofactors
Coenzymes
34
enzyme minus its cofactor; cannot function without its cofactor/coenzyme
Apoenzymes
35
whole enzyme
Haloenzyme
36
Classification of enzyme
- Oxidoreductase - Transferase - Hydrolase - Lyase - Isomerase - Ligase
37
Oxidation-reduction reactions
Oxidoreductase
38
Group transfer
Transferase
39
Hydrolysis reactions
Hydrolase
40
Addition or removal of groups to form double bonds
Lyase
41
Isomerization (intramolecular group transfer)
Isomerase
42
Ligation of two substrate at the expense of ATP hydrolysis
Ligase
43
Example of oxidoreductase
Lactate dehydrogenase
44
Example of transferase
Nucleoside monophosphate kinase
45
Example of Hydrolase
Chymotrypsin
46
Example of lyase
Fumarase
47
Example of Isomerase
Triose phosphate isomerase
48
Example of Ligase
Aminoacyl-tRNA synthease
49
The rate at which an enzymatic reaction proceeds depends on;
- concentrations of substrate, - product - active enzyme
50
used in the living cell as a means of controlling enzymatic reaction
Enzyme inhibition
51
a molecule that binds to an enzyme and blocks its activity
Enzyme inhibitor
52
Two types of enzyme inihibition
- Competitive inhibition - Noncompetitive inihibition
53
substrate molecule is prevented from binding to the active site of an enzyme by a molecule that is very similar in structure to the substrate
competitive inhibition
54
How to reverse competitive inhibition
increasing substrate concentration
55
Caused by molecules that bind to a region(s) of the enzyme outside the active site
noncompetitive inhibition
56
how to reverse noncompetitive inhibition
dilution or removal of inihibitor
57
Regulation of Metabolic Reactions
- Control of enzyme synthesis - Control of enzyme activity
58
enzymes are only synthesized when needed
Control of enzyme synthesis
59
regulated by modulator molecules
Control of enzyme activity
60
alters the tertiary structure of the enzyme thus changing the conformation of the active site.
Allosteric site
61
first enzyme of the sequence that acts as the regulatory enzyme - limits the rate of accumulation of the product by slowing the entire sequence from the beginning
End-product (feedback) inhibition
62
several cat-ion cofactors act as allosteric activators for some enzymes
Enzyme activitation
63
TWO KINDS OF ENERGY-YIELDING Pathways for Animal tissues
1. Aerobic metabolism 2. Anaerobic metabolism
64
food molecules are completely oxidized to carbon dioxide and water by molecular oxygen; energy yield is far greater.
Aerobic respiration
65
food molecules are oxidized incompletely to lactic acid (lactate); absence of oxygen
Anaerobic metabolism