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

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

A

Carbohydrates

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5
Q

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

A

Proteins

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6
Q

DNA and RNA

A

Nucleic Acid

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7
Q

carries coded information, arranged into genes, that is passed from each cell to its daughter cells and from one generation to the next

A

DNA

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8
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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9
Q

Proteins – most complex and most abundant organic molecules containing at least one ______ and ____.

A

carboxyl group
one amino group

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10
Q

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

A

Catalysis

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11
Q

any substance that increases rate of reaction upon addition to a certain reaction .

A

Catalyst

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12
Q

catalyst of biochemical reactions (biological catalysts)

A

Enzymes

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13
Q

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

A

Enzymes

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14
Q

are proteins of very specific amino acid composition and sequence

A

Enzymes

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15
Q

catalyze all the synthetic and metabolic reactions of the cell

A

Enzymes

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16
Q

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

A

Activation Energy

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17
Q

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

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18
Q

How do enzymes hasten the reaction?

A

enzyme (E) binds with a substrate (S) to form an activated enzyme-substrate complex (ES*).

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19
Q

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

A

Enzyme Specificity

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20
Q

hydrolyses any peptide bond in which the carbonyl group belongs to a phenylalanine, tyrosine, or tryptophan residue.

A

Chymotrypsin

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21
Q

(proteolytic enzyme present in the intestine - protein hydrolysing)

A

Chymotrypsin

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22
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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23
Q

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

A

Active Site

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24
Q

catalytic potency of an enzyme

A

Enzyme Activity

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25
Q

number of reactions catalyzed per second by the enzyme

A

turnover number

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26
Q

How enzymes accelerate reactions

A

-Holds substrate in close proximity to one another in order to enhance the probability of a reaction
-form an unstable intermediate that readily undergoes second reaction
-presence of proton donors and acceptors in the active site of the enzyme

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27
Q

Factors affecting enzyme activity

A

Temperature and Reaction Rates

28
Q

as ____ increases, reaction rate initially increases (increased kinetic energy of the substrate molecule)

A

temperature

29
Q

as temperature increases further, reaction rate decreases____ (onset of denaturation)

A

decreases

30
Q

reaction rate is maximal at the _____.

A

optimal temperature

31
Q

drop in pH exposes more _____ on an enzyme for interaction with _____ on a substrate molecule

A

positive sites
negative groups

32
Q

rise in pH facilitates the binding of ____ on a substrate to ____ on the enzymes.

A

positive groups
negative sites

33
Q

small organic molecules that act as cofactors

A

coenzymes

34
Q

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

A

apoenzyme

35
Q

Classified according to the types of reaction they catalyze

A

-Oxidoreductase
-Transferase
-Hydrolase
-Lyase
-Isomerase
-Ligase

36
Q

Oxidation-reduction

A

Oxidoreductase

37
Q

Group Transfer

A

Transferases

38
Q

Hydrolysis reaction

A

Hydrolases

39
Q

Addition or removal of groups to form double bonds

A

Lyases

40
Q

Isomerazation

A

Isomerases

41
Q

Ligation of two substrates at the expense of ATP hydrolysis

A

Ligases

42
Q

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

A

Enzyme Inhibition

43
Q

enzymes can be ___ (toxins) or ____ inhibited

A

irreversibly
reversibly

44
Q

Two types of Inhibition

A

Competitive and noncompetitive

45
Q

caused by molecules that react directly with the active site of the enzyme

A

Competitive Inhibition

46
Q

can be reversed by an increase in substrate concentration

A

Competitive Inhibition

47
Q

most competitive inhibitors are ____.

A

substrate analogs

48
Q

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

A

Noncompetitive Inhibition

49
Q

reversed by dilution or removal of the inhibitor

A

Noncompetitive inhibition

50
Q

chemical structure of noncompetitiveinhibitors typically differs from that of the substrate.

A

Noncompetitive Inhibition

51
Q

Regulation of Metabolic Reactions

A

1.Control of Enzyme Synthesis
2. Control of enzyme activity
3.End product inhibition

52
Q

Certain conditions that reduce protein synthesis generally

A

Control of enzyme synthesis

53
Q

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)

A

Control of Enzyme Synthesis

54
Q

regulated by modulator molecules (interact with a part of the enzyme molecule –allosteric site - distinct from the active site)

A

Control of Enzyme Activity

55
Q

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

A

Allosteric Site

56
Q

the affinity of the enzyme for its substrate decreases or increases

A

Control of Enzyme Activity

57
Q

first enzyme of the sequence that acts as the regulatory enzyme

A

End-product inhibition

58
Q

end product of the pathway feeds back to inhibit the activity of this first enzyme

A

End-feedback product Inhibition

59
Q

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

A

allosteric inhibitor

60
Q

limits the rate of accumulation of the end product by slowing the entire sequence from the beginning

A

End-product Inhibition

61
Q

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

A

Enzyme Activation

62
Q

Two kinds of energy yielding metabolic pathways in animal tissues

A

Aerobic Metabolism
Anaerobic Metabolism

63
Q

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

A

aerobic Metabolism

64
Q

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

A

Anaerobic Metabolism

65
Q

Cofactor + Apoenzyme

A

Holoenzyme