Metabolism I Flashcards

1
Q

define Catabolic

A

large molecules break down into smaller ones

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2
Q

Is Catabolism exergonic and endergonic?

A

energy being released- exergonic

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3
Q

Anabolism also known as synthesis requires

A

energy input–endergonic

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4
Q

Define Anabolism

A

small molecules are made into larger and more complex molecules

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5
Q

How does Substrate limeted reaction regulate itself

A

regulation by changing [A], [B], [C] and [D

product inhibiton and feedback are two types

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6
Q

Substrate limited reaction is often a what inhibition

A

allosteric inhibition

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7
Q

Substrate-limited reaction is often at a highly

A

exergonic steps

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8
Q

,** feedback inhibition** is inhibited by

A

the final product

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9
Q

Homeostatsis

A

balancing the final product with the cell’s needs

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10
Q

When it comes to substrate limited reaction, product inhibition is inhibited by

A

an immediate product

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11
Q

Enzyme limited reaction is regulated by

A

modulating corresponding enzymes

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12
Q

At what step does Enzyme limited reaction happen?

A

rate-limiting steps

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13
Q

Changing enzyme availability increases or decreases the

A

rate of synthesis or degradation

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14
Q

Spatial organization also known as

A

compartmentalization

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15
Q

How can you change enzyme active in an enzyme limited reaction? Name 4

A

Allostery, reverasible covalent modification, reverasal binding, irreversible covalent modification,

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16
Q

Where does Allostery inhibitors often bind to?

A

often binding a place that is not the active site

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17
Q

What are the 4 levels of spatial organizations in enzymes

A

Seperate individual enzymes, multi0enzymes complex, substrate channeling, and mebrane-bound enzyme system

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18
Q

In terms of spatial organization, What can individal enzymes do

A

they have independent enzymatic reactions

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19
Q

in seperate individual enzymes, substrates and intermediaties

A

must diffuse

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20
Q

Multi-enzymes complex are enzymes that need to

A

diffuse and form complexs

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21
Q

For multi-enzyme complex, substrate and intermediates

A

do not need to diffuse

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22
Q

Substrate channeling is easy to

A

regulate coordinately

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23
Q

What does Substrate channeling do the enzyme reaction rate

A

boosts the reaction rate

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24
Q

Membrane bound enzyme system has

A

minimal diffusion and many are large complexes

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25
Q

the most common form of energy is

A

adenosine triphosphate (ATP

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26
Q

What is the metabolic pathway

A

The transformation of ingested food to energy and simple compounds, or the synthesis of complex molecules, is performed by a series of enzymatic reactions. Collectively, these enzymes, and their substrates and products

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27
Q

Glycolysis is

A

first pathway used to degrade sugars and it is located in the cytoplasm

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28
Q

pyruvate

A

a 3 carbon keto acid that is the final product of glycolysis

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29
Q

Monod-Wyman-Changeaux model

A

concerted change

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30
Q

Koshland model shows

A

Sequential change:
subunits “flip”
individually

31
Q

biological oxidation often looses

A

2H+ and 2e-

32
Q

the citric acid or tricarboxylic acid cycle (TCA), i

A

second pathway in the degradation of sugars.

33
Q

Where is the citric acid cycle located in

A

in the matrix of the mitochondria

34
Q

What are the different types of modulators

A

activators, inhibitors, homotrophic, hetrotrophic

35
Q

Homotrophic

A

substrate= modulator, allosteric site= active site

36
Q

Allostery fine-tunes

A

enzyme activity

37
Q

most allosteric effectors affect

A

affect only K M , but some change Vmax

38
Q

when the allosteric enzymes are co cooperative the graph has a

A

sigmodial curve for V/[S]

39
Q

cooperative

A

phenomenon displayed by enzymes or receptors that have multiple binding sites where the affinity of the binding sites for a ligand is increased or dewcrease

40
Q

What does the binding of the binding of 1 subunit do?

A

other subunits affinity to the substrate increasing

41
Q

pancreatic trypsin inhibitor (6-kDa polypeptide tightly binds, where

A

to the active site

42
Q

What is an example of reversible binding of other proteins

A

pancreatic trypsin inhibitor (6-kDa polypeptide

43
Q

ancreatic trypsin inhibitor (6-kDa polypeptide) prevents

A

any trypsin that is prematurely activated in the pancreas from digesting it

44
Q

what are other metabolic pathways? Name 3

A

nonidentical foward and reverse pathways, compartmentalization, and commitment steps

45
Q

commitment steps are when

A

certain enzymes are key regulatory points

46
Q

How are Nonidentical forward and reverse pathways regulated?

A

when certain steps are independently regulated providing direction to the rest of pathway

47
Q

cascade of proteolytic activation is made

A

as inactive percusors

48
Q

biological oxidation is often catalyzed by

A

dehydrogenase

49
Q

Biolgical oxidation gains electrons

A

O

50
Q

every oxidation must be accompained by

A

a reduction

51
Q

Oxidation-reduction redox reaction involves

A

a electron transfer between 2 molecules

52
Q

a reduction gains

A

electrons, H and loses O

53
Q

CO2 is the most

A

oxidized from of carbon found in living organisms

54
Q

In C-H bonds, the more electronegative

A

C “owns” the 2e - shared with H.

55
Q

In C-O bonds,

A

O owns 2e-

56
Q

the catabolic pathways are

A

oxidative reaction sequences

57
Q

What are the functional groups of that can participate in redox reactions

A

hydroxyl
aldehyde
ketone
carbonyl
amino
amide
methyl
ether
disulfide
thioester
ester
sulfhydryl
phosphory

58
Q

Oxidation requires

A

specialized electron carriers

59
Q

H+ is soluble but e-

A

is insoluble in aqueous soltion

60
Q

During cellular respiration or oxidation what molecules act as electron carriers

A

NAD + (nicotinamide adenine dinucleotide) and FAD (flavin adenine dinucleotide)

61
Q

Lactater is oxidized to

A

pryuvate

62
Q

NAD + is reduced to

A

NADH

63
Q

Pyruvate is reduced to

A

lactate

64
Q

NADH is oxidized to

A

NAD+

65
Q

Which carbon is the 2H+ and 2 e- are removed from the lactate

A

2nd carbon

66
Q

What are 2 strategies to decrease ∆G

A

Make K eq &laquo_space;1
o Couple an endergonic rxn with an exergonic rxn

67
Q

Oxygenases is a subclasses of enzymes for what reactions

A

redox reactions

68
Q

Oxygenases uses oxygen as what

A

a substrate

69
Q

Oxygenases catalyze reaction where oxygen atoms are directly

A

incorporated into the product

70
Q

oxygenases forms what type of new group (hint: 2 groups)

A

a new hydroxyl or carboxyl group

71
Q

What reaction does Oxidases catalyzes

A

oxidation reactions

72
Q

Oxidases molecular oxygen serves

A

as the e- acceptor

73
Q
A