4 Flashcards

(60 cards)

1
Q

What are the Biological Molecules?

A
  1. Lipids
  2. Carbohydrates
  3. Proteins
  4. Nucleic acid
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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 and sterols

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5
Q

polyhydroxyl aldehyde and ketones with the general formula of (CH2O)n.

A

Carbohydrates

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6
Q

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

A

Proteins

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7
Q

carries coded information

A

DNA

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8
Q

DNA carries coded information,
arranged into ________

A

genes

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9
Q

DNA carries coded information, arranged into genes, that is passed from each cell to its daughter cells and from one generation to the next; RNA instrumental in translating the coded message of DNA into sequences of amino acids during synthesis of protein molecules

A

Nucleic acid

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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)
➢neither used up in the reaction nor do they appear as reaction products
➢are proteins of very specific amino acid composition and sequence
➢ denatured and precipitated with salts,
solvents and other reagents
➢ 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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13
Q

Activation energy/free energy of activation

the kinetic energy required to bring the _____ into position to interact.

A

reactants

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14
Q

Activation energy/free energy of activation

➢measured as the number of calories required to bring all the molecules in a mole of reactant at a given temperature to a __________

A

reactive (or activated) state.

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15
Q

How do enzymes hasten the reaction?

A

enzyme lowers the activation energy

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16
Q

How do enzymes hasten the reaction?

enzyme (E) binds with a substrate (S) to form an __________

A

activated enzyme substrate complex (ES*)

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17
Q

How do enzymes hasten the reaction?

ES* state, the path to the product (P) has a __________ than the nonenzymatic reaction.

A

lower activation energy

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18
Q

How do enzymes hasten the reaction?

reactions catalyzed by enzymes are usually _______ faster than uncatalyzed reactions.

A

103 to 1017 times

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19
Q

General Propertied of Enzymes

**Enzyme Specificity

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

A

substrate

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20
Q

General Propertied of Enzymes

specificity of enzymes varies

A

e.g.
stereo-specific
single product
specific bonds

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21
Q

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

A

active site

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22
Q

___________ of certain amino acid residues that are brought into proximity by this tertiary structure, even though they may be widely separated in the
amino acid sequence of the enzyme.

A

side groups

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23
Q

Mechanism of catalysis by enzymes

A

enzyme activity
turnover number –

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24
Q

Mechanism of catalysis by enzymes

catalytic potency of an enzyme

A

enzyme activity

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25
**Mechanism of catalysis by enzymes** number of reactions catalyzed per second by the enzyme
turnover number
26
How enzymes accerlerate reactions?
➢ holds substrates 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
27
**Temperature and Reaction Rates** rate of chemical reaction depend on ________.
temperature
28
**Temperature and Reaction Rates** ↑ temperature - ↑ average molecular velocity - ↑ number of molecular collisions per unit ↑ probability of successful interaction of the reactant molecules.
- as their velocities increase, the molecules possess higher kinetic energies and thus are more likely to react upon collision. - as temperature increases, reaction rate initially increases (increased kinetic energy of the substrate molecule) - as temperature increases further, reaction rate decreases (onset of denaturation) - reaction rate is maximal at the optimal temperature
29
_____ in pH exposes more positive sites on an enzyme for interaction with negative groups on a substrate molecule.
drop
30
______ in pH facilitates the binding of positive groups on a substrate to negative sites on the enzymes.
rise
31
**Enzymes and Cofactors** enzymes require ____ for activity
cofactors
32
**Enzymes and Cofactors** small organic molecules that act as cofactors
coenzymes
33
**Enzymes and Cofactors** enzyme minus its cofactor; cannot function without its cofactor/coenzyme
apoenzyme
34
**Enzymes and Cofactors** covalently attached cofactors, part of the enzyme molecule metal ions
e.g. vitamins
35
Many enzymes require the presence of other ____
compounds
36
(coenzyme, prosthetic group or metal ion)
Cofactor
37
Cofactor (coenzyme, prosthetic group or metal ion) + apoenzyme = _______
holoenzyme
38
Classified according to the types of reaction they catalyze
➢Oxidoreductase ➢Transferase ➢Hydrolase ➢Lyase ➢Isomerase ➢Ligase
39
Oxidation-reduction
Oxidoreductase
40
Group transfer
Transferase
41
Hydrolysis reactions (transfer of functional groups to water)
Hydrolases
42
Addition or removal of groups to form double bonds
Lyases
43
Isomerization (intramolecular group transfer)
Isomerases
44
Ligation of two substrates at the expense of ATP hydrolysis
Ligase
45
The rate at which an enzymatic reaction proceeds depends on the concentrations of substrate, product, and active enzymes
Enzymes Kinetics
46
➢used in the living cell as a means of controlling enzymatic reactions ➢discovered important features of the active sites and of the mechanisms of enzyme action ➢enzymes can be irreversibly (toxins) or reversibly inhibited
Enzyme Inhibition
47
Two types of Enzyme Inhibition
1. competitive inhibition 2. noncompetitive inhibition
48
➢caused by molecules that react directly with the active site of the enzyme ➢can be reversed by an increase in substrate concentration ➢most competetive inhibitors are substrate analogs
Competitive inhibition
49
➢caused by molecules that bind to a region(s) of the enzym eoutside the active site ➢reversed by dilution or removal of the inhibitor ➢chemical structure of noncompetitive inhibitors typically differs from that of the substrate.
Noncompetitive inhibition
50
What are the Regulation of Metabolic Reactions
1. Control of Enzyme Synthesis 2. Control of Enzyme Activity
51
➢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) ➢enzymes are only synthesized when needed
Control of Enzyme Synthesis
52
➢regulated by modulator molecules (interact with a part of the enzyme molecule – allosteric site - distinct from the active site) ➢allosteric site - alters the tertiary structure of the enzyme thus changing the conformation of the active site ➢the affinity of the enzyme for its substrate decreases or increases
Control of Enzyme Activity
53
alters the tertiary structure of the enzyme thus changing the conformation of the active site
allosteric site
54
distinct from the active site
allosteric site
55
➢ first enzyme of the sequence that acts as the regulatory enzyme ➢ end product of the pathway feeds back to inhibit the activity of this first enzyme ➢ limits the rate of accumulation of the end product by slowing the entire sequence from the beginning
End-product (Feedback) Inhibition
56
interaction of the end product occurs in the allosteric site, making the end product an ______________
allosteric inhibitor
57
**Enzyme Activation** several cat-ion cofactors act as __________ for some enzymes
allosteric activators
58
Two kinds of energyyielding metabolic pathways in animal tissues:
1.aerobic metabolism 2. anaerobic metabolism
59
food molecules are completely oxidized to carbon dioxide and water by molecular oxygen; energy yield is far greater
aerobic metabolism
60
food molecules are oxidized incompletely to lactic acid (lactate); absence of oxygen
anaerobic metabolism