Chp. six Flashcards

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1
Q

____ tells if a reaction can thermodynamically happen, but it doesn’t say that it will happen. Rate of reaction is a function of specialized enzymes.

A

delta G

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2
Q

Molecules that should react with one another often _____ because they lack sufficient energy.

A

do not

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3
Q

___ is the minimum amount of energy that 2 molecules must have in order to react.

A

activation energy Ea

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4
Q

For a reaction to occur you must have a ______ and

A

favorable delta G and enough energy to reach Ea

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5
Q

The rate of enzymatic reaction is proportional to _____ that have an evergy content >=

A

fraction of molecules

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6
Q

Under most biologically normal conditions, the Ea is ___ that few molecules have that much energy.

A

so high

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7
Q

The rates of uncatalyzed reaction in cells are ____

A

very slow.

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8
Q

non-reacting molecules are ____ unstable but ____ stable in a metastable state.

A

thermodynamically, kinetically

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9
Q

life depends on the high Ea to ____ cellular reactions from happening at appreciable rates ____ in the presence of a suitable catalyst.

A

prevent, except

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10
Q

Providing a reactive surface is the task of a_____`

A

catalyst

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11
Q

Protein catalysts are called

A

enzymes

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12
Q

RNA catalyst are called

A

ribozymes

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13
Q

3 basic properties of catalysts

A
  1. All catalysts increase the rate of a reaction by lowering the Ea requirement.
  2. All catalysts act by forming transient intermediate complexes with the substrate molecules and thus position them in a manner that facilitates their interaction.
  3. All catalysts change only the rate at which equilibrium is reached; no effect on the position of the equilibrium.
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14
Q

Every enzyme contains, somewhere within its 3 prime structure, a characteristic cluster of ______ forming an _____.

A

amino acids, active site

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15
Q

What is the location of domain on the enzyme’s structure where the actual catalytic action occurs

A

active site

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16
Q

what is usually a groove or pocket with chemical or structuaral properties that accommodate the intended substrate with high specificity

A

active site

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17
Q

Active site involves only about ____ of the surface area of the enzyme.

A

5%

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18
Q

Amino acids most commonly found at an active site

A

cysteine, histidine, serine, aspartate, glutamate, lysine

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19
Q

The amino acids that make up the active site of an enzyme are not usually contiguous along the ___ sequence of a polypeptide. Instead, they are brought into the right conformation by the specific ____ folding of the polypeptide chain and by additional conformational change when the substrate binds.

A

1 prime, 3-D

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20
Q

The reaction seen in peroxisomes is _____ favorable… yet hydrogen peroxide exists in nature in a _____ state.

A

thermodynamically, metastable

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21
Q

When ferric ions are added to the solution it increases the reaction rate about

A

30,000X

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22
Q

fe+3 reacts with O2 to form iron oxides and drive the break down of

A

H2O2

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23
Q

If ____ is present the reaction occurs about 1x10^9 X faster than if uncatalyzed

A

catalase

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24
Q

if a catalase is present the reaction occurs about ____ faster than if uncatalyzed.

A

1x10^9 X

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25
Q

ion groups that are integral parts of enzyme structure

A

prosthetic groups

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26
Q

Prosthetic groups can be ___ organic molecules or ___ ions or combination of ____

A

small, metal

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27
Q

Prosthetic groups function as ____ acceptors since none of the a.a. are good _____ acceptors.

A

electron, electron

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28
Q

Prosthetic groups are usually associated with the ____ and are indispensable for ____.

A

active site, catalytic activity

29
Q

Not all enzymes have prosthetic groups; ones that do RedOx reaction ____

A

require one

30
Q

While all of the vitamins may have been discovered, new catalytic cofactors and prosthetic groups are ______.

A

still being found. They are too numerous to mention.

31
Q

The coenzyme ____ is a hydrogen carrier that replaces ____ in certain bacterial alcohol dehydrogenases.

A

PQQ, NAD

32
Q

____ is a cofactor for amino oxidases found in bacterial, plan, and human tissues. It is a prosthetic group that is formed by oxidation of a specific tyrosine in the active site.

A

Topaquinone

33
Q

Topaquinone functions together with a nearby ___ ion which binds the ___ substrate. The same copper center and ___are apparently involved in ____ synthesis of the prosthetic group.

A

copper, O2, O2

34
Q

Formation of topaquinone is only one case of many, in which _____ groups are self-assembled using components of the ___ that carries the group.

A

prosthetic, protein

35
Q

A recently discovered example of formation is ______, from glycine and serine units of protein. The prosthetic group is involved in a previously hard-to-explain isomerization of histidine and phenylalanine.

A

4-methylidene-imidazole-5-one

36
Q

Enzyme must bind the substrate then ____ the reaction.

A

catalyze

37
Q

A consequence of the structure of the active site is that the enzymes display a high degree of substrate specificity.

A

Enzyme specificity

38
Q

Enzyme specificity can discriminate between very _____ molecules.

A

similar

39
Q

Enzyme specificity has a difference between an ____ catalyst vs. an ____ one

A

inorganic, organic

40
Q

Are all enzymes specific as others?

A

no

41
Q

Some enzymes accept a ____ of ____ related substrates.

A

number, closely

42
Q

Which enzymes tend to accept entire groups of substrates as long as they posses some common structural feature.

A

enzymes involved in synthesis or degradation of polymers.

43
Q

How many major classes are based on function, with subgroups used to define their function more precisely.

A

6

44
Q

maintains a narrow range of cellular temps

A

homeotherms

45
Q

Within this narrow range, the rate of an enzyme-catalyzed reaction increases with temp Why?

A

increases the kinetic energy of the molecules and their reactivity.

46
Q

Outside of this temp range the enzyme begins to fall apart or _____.

A

denature

47
Q

The temp range over which an denatures varies _____ from enzyme to enzyme and especially from organism to organism.

A

greatly

48
Q

organisms that live in an environment with a higher than average temperature for biotic life such as bacteria that thrive in environments that average 70 degrees C.

A

thermophiles

49
Q

They have essentially the same genes as other bacteria, however, the alleles for their proteins encode heat tolerate varieties of enzyme.

A

thermophiles

50
Q

Thermophiles enzymes operate at _____ teps and are critical to bio-technology.

A

high

51
Q

______ is an ex. DNA polymerase (replicates DNA) from Thermus aquaticus is the driving force of PCR and DNA sequencing.

A

thermophiles

52
Q

Most enzymes are active within a range of only _____pH units.

A

3-4

53
Q

The pH dependence is usually due to the need for one or more charged _______ at the active site.

A

amino acids.

54
Q

_____ dependence usually reflects the environment in which an enzyme is normally active

A

pH

55
Q

The active site of ______ involves the caroxyl groups from each of 2 glutamates (positions 72, 270)

A

carboxypeptidase A

56
Q

reaction type: oxidation-reduction reactions

A

class: oxidoreductases

57
Q

Reaction type: Transfer of functional groups from one molecule to another.

A

transferases

58
Q

Reaction type: Hydrolytic cleavage of one molecule into two molecules

A

classes: hydolase

59
Q

Reaction type: Removal of a group from, or addition of a group to , a molecule with rearrangement of electrons.

A

Classes: lyases

60
Q

Reaction type: Movement of a functional group within a molecule

A

classes: isomerases

61
Q

Reaction type: Joining of two molecules to form a single molecule

A

classes: Ligases

62
Q

List the six enzyme classes.

A

oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases

63
Q

Enzyme name: alcohol dehydrogenase

A

oxidoreductases

64
Q

Enzyme name: Glycerokinase

A

transferases

65
Q

Enzyme name: Carboxypeptidase A

A

hydrolases

66
Q

Enzyme name: Pyruvate decarboxylase

A

lyases

67
Q

Enzyme name: Maleate isomerase

A

Isomerases

68
Q

Enzyme name: Pyruvate carboxylase

A

Ligases