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BIO108 - Gen. Physiology > Lec 5: Molecules, energy and biosynthesis > Flashcards

Lec 5: Molecules, energy and biosynthesis Flashcards

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
Q

that the active site of an enzyme will undergo a conformational change when binding a substrate, to improve the fit

A

Induced fit model

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26
Q

The active site of an enzyme is structured to fit a specifically shaped substrate

A

lock-and-key model

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27
Q

Mechanism of catalysis by enzymes

A
  • Enzyme activity
  • Turnover number
28
Q

catalytic potency of an enzyme

A

Enzyme activity

29
Q

number of reactions catalyzed per second by the enzyme

A

Turnover number

30
Q

Substrate interacts with the active site of the enzyme, forming an enzyme-substrate complex

A

Enzymatic reaction

31
Q

How does enzyme accelerate reactions?

A
  • holds substrates in close proximity to one another
  • form an unstable intermediate
  • presence of proton donors and acceptors
32
Q

Factors affecting enzyme activity

A
  • Temperature
  • Reaction rates
33
Q

small organic molecules that act as cofactors

A

Coenzymes

34
Q

enzyme minus its cofactor; cannot function without its cofactor/coenzyme

A

Apoenzymes

35
Q

whole enzyme

A

Haloenzyme

36
Q

Classification of enzyme

A
  • Oxidoreductase
  • Transferase
  • Hydrolase
  • Lyase
  • Isomerase
  • Ligase
37
Q

Oxidation-reduction reactions

A

Oxidoreductase

38
Q

Group transfer

A

Transferase

39
Q

Hydrolysis reactions

A

Hydrolase

40
Q

Addition or removal of groups to form double bonds

A

Lyase

41
Q

Isomerization (intramolecular group transfer)

A

Isomerase

42
Q

Ligation of two substrate at the expense of ATP hydrolysis

A

Ligase

43
Q

Example of oxidoreductase

A

Lactate dehydrogenase

44
Q

Example of transferase

A

Nucleoside monophosphate kinase

45
Q

Example of Hydrolase

A

Chymotrypsin

46
Q

Example of lyase

A

Fumarase

47
Q

Example of Isomerase

A

Triose phosphate isomerase

48
Q

Example of Ligase

A

Aminoacyl-tRNA synthease

49
Q

The rate at which an enzymatic reaction proceeds depends on;

A
  • concentrations of substrate,
  • product
  • active enzyme
50
Q

used in the living cell as a means of controlling enzymatic reaction

A

Enzyme inhibition

51
Q

a molecule that binds to an enzyme and blocks its activity

A

Enzyme inhibitor

52
Q

Two types of enzyme inihibition

A
  • Competitive inhibition
  • Noncompetitive inihibition
53
Q

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

A

competitive inhibition

54
Q

How to reverse competitive inhibition

A

increasing substrate concentration

55
Q

Caused by molecules that bind to a region(s) of the enzyme outside the active site

A

noncompetitive inhibition

56
Q

how to reverse noncompetitive inhibition

A

dilution or removal of inihibitor

57
Q

Regulation of Metabolic Reactions

A
  • Control of enzyme synthesis
  • Control of enzyme activity
58
Q

enzymes are only synthesized when needed

A

Control of enzyme synthesis

59
Q

regulated by modulator molecules

A

Control of enzyme activity

60
Q

alters the tertiary structure of the enzyme thus changing the conformation of the active site.

A

Allosteric site

61
Q

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

A

End-product (feedback) inhibition

62
Q

several cat-ion cofactors act as allosteric activators for some enzymes

A

Enzyme activitation

63
Q

TWO KINDS OF ENERGY-YIELDING Pathways for Animal tissues

A
  1. Aerobic metabolism
  2. Anaerobic metabolism
64
Q

food molecules are completely oxidized to carbon dioxide and water by molecular oxygen; energy yield is far greater.

A

Aerobic respiration

65
Q

food molecules are oxidized incompletely to lactic acid (lactate); absence of oxygen

A

Anaerobic metabolism

BIO108 - Gen. Physiology (18 decks)

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