Control of Enzyme Activity—Introduction to Metabolism Flashcards

1
Q

What is metabolism ?

A

highly integrated network of chemical reactions

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2
Q

catabolism

A

catabolism : fuel to energy

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3
Q

anabolism

A

anabolism: energy + simple precursor to complex molecule

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4
Q

Ways of Regulating Metabolic Processes (Pathways)?

A

contolling amount of enzymes,catalytic activity and compartmentalization of substrates

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5
Q

5 Ways of Controlling Enzyme Activity

A
Amount of enzyme in the cell
Allosteric control of enzymes 
Through existence of ISOZYMES
Reversible covalent modification
Proteolytic activation
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6
Q

allosteric enzymes? (4 things it does)

A

exhibit cooperativity in responses to substrate
obey the Monod-Wyman-Changeux (MWC) model
Often serve as control points in pathways
Subject to feedback inhibition

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7
Q

Monod-Wyman-Changeux (MWC) model of allosteric behavior

A

Equilibrium between “T” and “R” states exists; allosteric effectors shift equilibrium

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8
Q

what Catalyzes first committed step of pyrimidine synthesis (in E. coli):

A

ATCase

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9
Q

in the 1st committed step of pyrimidine synthesis, what compound controls allosteric inhibition and activation? (2 separate things)

A

CTP inhibit

ATP activate

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10
Q

two subunits seen in Aspartate Transcarbamoylase, ATCase

A

C (catalytic site)and

R (regulatory site)

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11
Q

Which site does ATP and CTP bind too

A

R site

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12
Q

what is a Competitive inhibitor of both substrates, aspartate and carbamoyl phosphate?

A

PALA -N-(Phosphonacetyl)–L-Aspartate

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13
Q

Upon binding PALA will place ATCase in the __ state ?

A

R

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14
Q

in absence of substrate aspartate, ATCase will exist in what kind of state ?

A

Low activity T state

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15
Q

in the presence of CTP ATCase will exist in what kind of state ?

A

Low activity T state

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16
Q

Higher levels of aspartate increasingly shift equilibrium from

A

T” to “R”

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17
Q

Inhibitor CTP shifts equilibrium toward __ state ?

A

T

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18
Q

Activator ATP shifts equilibrium toward __ state?

A

R

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19
Q

Why ATP would activate ATCase?

why is ATP used in this reaction

A

Pyrimidine-purine balance needed for mRNA or DNA synthesis

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20
Q

Isozymes are Homologous enzymes that catalyze same reaction BUT

A

Are encoded by different genes
Hve similar AAs
Are often expressed in a tissue-specific or developmental stage-specific manner

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21
Q

An example of an isozyme is ?

A

LDH

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22
Q

Combitations of teramers possible by LDH

A

M4, M3H, M2H2, MH3, H4

23
Q

6 Different Post-Translational Covalent Modification of Enzymes/ Proteins?

A

phosphorylation, acetylation, carboxylation, ubiquitylation, lipidation, glycosylation

24
Q

in phosphorylation what catalyzes the attachment and removal of phosphate?

A

protein kinase

removal- protein phosphatase

25
In phosphorylatipn what different residues do phosphates attach too ?
serine, threonine, or tyrosine
26
Acetylation activates __?
gene transcription / opens up DNA
27
Ubiquitylation In cytoplasm targets proteins for destruction via the
proteaosome
28
In the nucleus this type of modificationcan alter properties of histones and other proteins involved in gene expression
ubiquitylation
29
which covalent Modification allows the clotting factors to chelate calcium and adhere to vessel wall near site of injury ?
carboxylation
30
Allows the subunits to move along the cytoplasmic face of membrane; speeds up their interaction with downstream effectors
lipidation
31
Gs(alpha) with adenylyl cyclase is seen in this type of covalent modification
lipidation
32
Attachment of carbohydrate groups, including modified sugars (GlcNAc) and oligosaccharide groups is seen in this type of covalent modification ?
glycosylation
33
Which residues (AA) does glycosylation attach to ?
Covalent attachment is to serine, threonine or asparagine residues
34
in glycosylation, modification is directed to (3 things ) ?
Modification is to extracellular domain of transmembrane proteins, or secreted proteins (e.g., EPO), or proteins destined for lysosome
35
chelate ?
compound containing a ligand bonded to a central metal atom at 2 more points? "grab and bond to "
36
phosphorylation and glycosyation are the only reversible reactions in Post-Translational Covalent Modification of Enzymes/ Proteins?
Falce : phosphoylation AND aceylation
37
ATP provides energy by simple hydrolysis. T/F?
False. ATP provides energy by group transfer.
38
what is used to lower ADP levels during periods of intense demand for ATP
Adenylate kinase
39
reasons why there is a large (-) delta G of hydrolysis of ATP?
1. More resonance forms 2. less bond strain (repulsion) in ADP 3. Greater degree of solvation (hydration) in products
40
Coupled reactions
refers to coupling unfavorable and favorable reactions to drive reaction forward
41
coupled reaction examples
1. Unactivated vs activated conformations of a motor protein 2. hydrolysis of ATP 3. ATPase
42
what compound has 2 phosphoanhydride bonds that, when hydrolyzed, yield a lot of free energy
ATP
43
Phoshpoanhydride bond?
links a ribose sugar and. three phosphate groups
44
High energy compound thar rapidly synthesizes ATP when low in the muscle
creatine phosphate
45
In exercise __ ttansfers phosphryl group to ADP to generate ATP
Creatine phosphate
46
In enol phosphates such as phosphoenolpyruvate what will give the product more stabiulty than reactant
the ability to tautomerize
47
tautomerism
isomers of a compound which differ only in the position of the protons and electrons. usually seen as a PROTON TRANSFER
48
ATP generating pathways are __ by high energy charge
inhibited : seen in catabolic
49
ATP utilizing pathways are __ by high energy charge
activated :seen in anabolic
50
activated carriers of electrons for fuel oxidation
NAD+, NADH and FAD
51
activated carriers of elctons for reductive biosynthesis
NADP+, NADPH .
52
[NADP+]/[NADPH] is kept low or high ?
low so hydride trasfer favors [NADPH]
53
[NAD+]/[NADH] is kept low or high ?
HIGH low so hydride trasfer favors [NAD+]
54
this type of covalent modification is seen in the alpha and beta/gamma subunits of heterotrimeric G-proteins
lipidation