Lecture 10 Flashcards

1
Q

What is the cell’s workhorse?

A

proteins

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2
Q

What is one of the cell’s workhorses?

A

enzymes

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3
Q

What are enzymes?

A

proteins (or RNA)

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4
Q

What do enzymes do?

A

-CATALYSE the making and breaking of covalent bonds in the cell
-INCREASE REACTION RATES
-allow MILDER reaction conditions (i.e. near neutral pH and low temperatures)
-can DISPLAY VERY HIGH specificity (distinguish between optical isomers)
-REGULATE reactions and pathways

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5
Q

Who discovered enzymes, and how?

A

Anselme Payen

-discovered in a brewery
-discovered first enzyme diastase
-did NOT know amylase was a protein

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6
Q

Enzymes work by lowering what?

A

they lower the activation energy

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7
Q

What are the four catalysis mechanisms/key features to lower the activation energy?

A

Proximity
Orientation
Strain/ distortion
Acid-base catalysis

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8
Q

What is the proximity catalysis mechanism?

A
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9
Q

What is the orientation catalysis mechanism?

A
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10
Q

What is the strain/distortion catalysis mechanism?

A

if binding puts strain on bond making it easier for reaction to occur

enzymes encourage substrate distortion into its transition state conformation

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11
Q

What is the acid/base catalysis mechanism?

A

protons (H+) donated/accepted or hydroxyls (OH-) a great nucleophile is generated:

-enzymes overcome very low concentrations of these reactive molecules in the environment
-in the active site of enzymes concentration of OH- or H+ in vicinity of bond to be attacked can be effectively 1 M

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12
Q

Enzymes have remarkable specificity- what can explain this?

A

LOCK AND KEY: binding site has complementary shape to substrate
INDUCED FIT: contact between part of the binding site and the substrate induces a change in shape of the active site to bind to the substrate

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13
Q

What are enzymes?

a. They catalyze reactions
b. They increase reaction rates
c. They allow milder reaction conditions
d. They can display very high specificity
e. All of the above

A

e. All of the above

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14
Q

Explain Fischer’s Lock and Key

A

The substrate fits perfectly into it’s enzyme’s active site leading to an enzyme complex

-the enzyme and substrate fit together like a lock and a key
-substrate complements catalytic site geometry

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15
Q

Explain Induced Fit

A

The substrate and enzyme do not appear to be a perfect fit, but the substrate induces the enzyme to change shape of the binding site so they can fit

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16
Q

Enzyme active sites share what five common features?

A

1) The active site is a three-dimensional cleft or crevice created by amino acids from different parts of the primary structure.
2) The active site constitutes a small portion of the enzyme volume.
3) Active sites create unique MICRO ENVIRONMENTS.
4) The interaction of the enzyme and substrate at the active site involves MULTIPLE WEAK interactions.
5) Enzyme specificity depends on the molecular architecture at the active site.

17
Q

What is unique about lysozyme active site residues?

A

they are distributed among the sequence appearing to be scattered, but when folded they all come together to form the active site

18
Q

What are the four types of specificity?

A

1) Absolute
2) Bond
3) Group
4) Stereo

19
Q

What is absolute specificity?

A

substrate specific

-enzyme specific to only one substrate

20
Q

Urease?

21
Q

What is bond specificity?

A

bond type specific

-enzyme specific to certain types of bonds

22
Q

What is group specificity?

A

chemical group specific

-enzyme specific to certain types of chemical groups

23
Q

What is stereo specificity?

A

chirality specific (i.e. D/L isomers)

-enzyme specific to stereochemistry (chirality) of substrate

24
Q

The active site of an enzyme:

a) is a series of amino acids which bind the enzyme
b) is a linear sequence of amino acids that react with each other
c) binds covalently to the substrate
d) allows water to enter into the active site and thereby solvate the substrate
e) none of the above

A

e) none of the above

25
What are the six major enzyme groups?
1) oxidoreductases 2) transferases 3) hydrolases 4) lyases 5) isomerases 6) ligases
26
Explain oxidoreductases (dehydrogenases)/ what they are?
catalyze oxidation-reduction reactions OiL RiG = Oxidation Is LOSS of electrons, Reduction Is GAIN of electrons
27
What can oxidation be identified as? Oxidation = loss of an electron
Addition of oxygen Removal of hydrogen Increase in valences of metal ion Generally needs a cofactor (NADH)
28
What are transferases/ what is an example of one?
catalyze group transfer reactions Alanine aminotransferase
29
What do hydrolases do and what is an example?
catalyze hydrolysis reactions where water is the acceptor of the transferred group alpha amylase
30
What are lyases and what is an example of one?
catalyzes the lysis (breakdown) of a substrate (generating a double bond) by means other than hydrolysis or oxidation pyruvate decarboxylase (requires metal and cofactor)
31
What are isomerases and some examples?
catalyzes isomerization reaction Alanine racemase
32
Which coenzyme/cofactor is shown? a) Thiamine pyrophosphate b) NAD+/NADP+ c) PLP d) None of the above
b) NAD+/NADP+ NAD is a common cofactor for REDOX reactions carried out by ocidoreductases' since it can transfer two electrons
33