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General Physiology > Lecture 4: Molecules, energy, and Biosynthesis > Flashcards

Lecture 4: Molecules, energy, and Biosynthesis Flashcards

1
Q

____ - diverse group of water-insoluble
biological molecules;

A

Lipids

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2
Q

energy stores

A

fats

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3
Q

Major components of membrane

A

phospholipids and sterols

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4
Q

Addition of 3h2o to triglyceride results to what products??

A

Glycerol and fatty acids

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5
Q

_ polyhydroxy aldehydes and ketones with the general formula of (CH2O)n

A

Carbohydrates

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6
Q

examples of monosaccharide sugars

A
  1. Glucose
  2. Galactose
  3. fructose
  4. ribose
  5. 2-deoxyribose
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7
Q

examples of disaccharide sugars

A
  1. sucrose
  2. lactose
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8
Q

____ – most complex and most abundant
organic molecules containing at least one
carboxyl group and one amino group.

A

Proteins

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9
Q

____ carries coded information,
arranged into genes

A

DNA

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10
Q

DNA carries coded information,
arranged into ____

A

genes

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11
Q

_____ instrumental in translating the coded message of DNA into sequences of amino acids during synthesis of protein molecules

A

RNA

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12
Q

difference between DNA and RNA ?

A

2’ H in DNA , 2’ OH in 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 upon addition to a certain
reaction .

A

Catalyst

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15
Q

____ catalyst of biochemical reactions (biological catalysts)

A

enzymes

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16
Q

___ neither used up in the reaction nor do they appear as reaction products

  • are proteins of very specific amino acid
    composition and sequence
A

Enzymes

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17
Q

Substrate + enzyme (enzyme substrate complex) = ______

A

Product + enzyme

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18
Q

enzymes can be denatured and precipitated with ____, ____, ____

A

salts, solvents, and other reagents

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19
Q

____ catalyze all the synthetic and metabolic
reactions of the cell
- allows for a faster speed of reaction
- increases the reaction rates by means of
lowering the energy of activation

A

Enzymes

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20
Q

enzymes increases the reaction rates by means of _______

A

lowering the energy of activation

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21
Q
  • the kinetic energy required to bring the
    reactants into position to interact.
  • measured as the number of calories required to bring all the molecules in a mole of reactant at a given temperature to a reactive (or activated) state.
A

Activation energy/free energy of activation

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22
Q

How do enzymes hasten the reaction?

A

enzymes lowers the activation energy

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23
Q

___ each enzyme is specific for a certain substrate (reactant molecule)

A

enzyme specificity

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24
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.

  • where the substrate can fit like a lock-and-key mechanism
A

Active site

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25
Q
  • enzyme molecule is made up of one or more peptide chains folded to form a more or less globular protein of a specific conformation
A

Enzyme Specificity

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26
Q

two types of enzyme model

A
  1. lock-and-key model
  2. Induced-fit model
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27
Q

____ – catalytic potency
of an enzyme

A

enzyme activity

28
Q

_____ – number of reactions catalyzed per second by the enzyme

A

Turnover number

29
Q

enzymatic reaction

A
  • substrate interacts with the active site of the
    enzyme
  • forming an enzyme-substrate complex (ES)
  • product separates from the enzyme
  • free enzyme can form an ES complex with a
    new substrate molecule
30
Q

Factors affecting enzyme activity

A
  1. Temperature and reaction rates
  2. pH
31
Q

The higher the temp., the higher the average molecular velocity, the higher the number of molecular collision per unit, the higher the probability of successful interaction of the reactant molecules.

A
32
Q

as their velocities ____, the molecules
possess higher kinetic energies and thus are
more likely to react upon collision.

A

increase

33
Q

Drop in __ exposes more positive sites on an enzyme for interaction with negative groups on a substrate molecule

A

pH

34
Q

rise in ____facilitates the binding of positive groups
on a substrate to negative sites on the enzymes.

A

pH

35
Q

enzyme require ___ for activity

A

cofactor

36
Q

____ - small organic molecules that act as cofactors

A

coenzyme

37
Q

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

A

Apoenzyme

38
Q

Cofactor (coenzyme, prosthetic group or metal ion) + apoenzyme =

A

holoenzyme

39
Q

Six major classes of enzymes

A
  1. Oxidoreductase
  2. Transferase
  3. Hydrolase
  4. Lyase
    5.Isomerase
    6.Ligase
40
Q

Type of reaction of oxidoreductase

A

Oxidation-reduction

41
Q

Type of reaction for tranferase

A

group transfer

42
Q

Type of reaction for hydrolayses

A

Hydrolysis reactions (transfer of functional groups to water)

43
Q

Type of reaction for lyases

A

Addition or removal of groups to form double bonds

44
Q

Type of reaction for isomerases

A

isomerization

45
Q

Type of reaction for ligase

A

Ligation of two substrates at the expense of ATP hydrolysis

46
Q

The rate at which an enzymatic reaction proceeds depends on the concentrations of substrate, product, and active enzymes

A

Mag lesser ang substrate as time goes by habang ga taas ang ma produce na product

47
Q

________- Used in the living cell as a means of controlling enzymatic reactions

A

Enzyme inhibition

48
Q

Two types of enzyme inhibition

A
  1. competitive inhibition
    2.noncompetitive inhibition
49
Q

_____ -Caused by molecules that react directly with the active site of the enzyme

A

Competitive Inhibition

50
Q

_____-Øcan be reversed by an increase in substrate concentration

A

Competitive inhibition

51
Q

The competitive inhibition can be reversed by ___

A

increasing the substrate concentration

52
Q

Ømost competitive inhibitors are ______

A

substrate analogs

53
Q

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

A

Non-competitive inhibition

54
Q

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

A

Non-competitive inhibition

55
Q

_____ reversed by dilution or removal of the inhibitor

A

Non-competitive inhibition

56
Q

Chemical structure of noncompetitive inhibitors typically _____ from that of the substrate.

A

differs

57
Q

Regulation of Metabolic Reactions

A
  1. Control of Enzyme Synthesis
  2. Control of Enzyme Activity
58
Q
  • Certain conditions that reduce protein synthesis generally
  • regulated at the molecular level by modulation of the rate of transcription of the gene encoding it (DNA is packaging; rate at which RNA is translated into proteins)
    Øenzymes are only synthesized when needed
A

Control of Enzyme Synthesis

59
Q

it is regulated by modulator molecules (interact with a part of the enzyme molecule )

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

interaction of the end product occurs in the allosteric site, making the end product an _____

A

allosteric inhibitor

62
Q
  • several cat-ion cofactors act as allosteric activators for some enzymes
A

enzyme activation

63
Q

Two kinds of energy- yielding metabolic pathways in 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 metabolism

65
Q

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

A

anaerobic metabolism

General Physiology (4 decks)

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