Exam 3

Question 1

Exogenous Glycation * Previously thought to be important solely to those suffering with type II diabetes * However, exogenous glycation reactions and their endproducts have been found to be important to all people as they contribute
to

Answer 1

a variety of diseases:– Retinal dysfunction– Cardiovascular diseases– Type II diabetes– Other age-related diseases Exogenous Glycation * Food producers have added AGEs to everyday foods to improve appearance and taste. * “Foods with significant browning, caramelization, or with directly added AGEs can be exceptionally high in these proinflammatory and disease initiating compounds.” * Watch out for these types of foods:– Donuts– BBQ meats – Cake– Dark colored soda a variety of diseases:– Retinal dysfunction– Cardiovascular diseases– Type II diabetes– Other age-related diseases Exogenous Glycation * Food producers have added AGEs to everyday foods to improve appearance and taste. * “Foods with significant browning, caramelization, or with directly added AGEs can be exceptionally high in these proinflammatory and disease initiating compounds.” * Watch out for these types of foods:– Donuts– BBQ meats – Cake– Dark colored soda

Question 2

• Exogenous glycations are normally created when

Answer 2

sugars are cooked with proteins or fats.

Question 3

Glucose in its linear form is

Answer 3

Toxic! STOP EATING PROCESSED FOODS AND DRINKING SUGARY DRINKS!

Question 4

What’s the difference between uncompetitive and noncompetitive inhibition?

Answer 4

*In uncompetitive inhibition, inhibitor only binds ES and not E alone

Question 5

Uncompetitive LWB-

Answer 5

Same angle, Different X intercept

Question 6

Uncompetitive inhibition principle-

Answer 6

Enzyme binds to allosteric site

Question 7

Exogenous Glycation

Answer 7

• Dietary or “pre-formed” glycation

Question 8

Why is Km lowered with uncompetitive inhibition?

Answer 8

-Km is lowered because formation of ESI increases concentration of ES via Le Chatelier/s Principl

Question 9

Effects of Mixed (Noncompetitive) Inhibitor on Enzyme Kinetics

Answer 9

-These inhibitors affect kcat only

Question 10

Non enzymatic glycosylation is a fast/slow process*

Answer 10

Slow process

Question 10

Why is non enzymatic glycosylation bad?

Answer 10

chaotic process that damages the function of biomolecules

Question 11

Non-Enzymatic Glycosylation deep mechanism-

Answer 11

Sugars combine with free amino group of proteins, then rearrange and dehydrate which results in the formation of pigment and cross-linked proteins.

Question 12

Non-Enzymatic Glycosylation is “the result of”-

Answer 12

a sugar molecule (fructose or glucose) bonding to a protein or lipid molecule without the action of an enzyme”
0 days

Question 13

Non-Enzymatic Glycosylation is aka-

Answer 13

also called glycation

Question 14

How does glucose change shape? (291)-

Answer 14

Free monosaccharides are hemiacetals that can undergo a reversible “anomerization” reaction

Question 15

What shapes can glucose take?-

Answer 15

Straight chain, Haworth, projection chair

Question 16

Mixed/noncompetitive inhibitor-

Answer 16

Binds to site other than active, with or without substrate

Question 17

Irreversible inhibition

Answer 17

(inactivators that irreversibly associate with enzyme, activity of enzyme does not recover with dilution, usually covalent interaction

Question 17

Competitive inhibitor on LWB-

Answer 17

different X intercept and angle

Question 18

Competitive inhibition-

Answer 18

Enzyme for K1 (Turning EI into ES + I) is usually a substrate analog.

Question 19

Types of reversible inhibition-

Answer 19

Competitive– Mixed (noncompetitive)– Uncompetitive

Question 20

Reversible inhibition

Answer 20

(inhibitors that can reversibly bind and dissociate from enzyme, activity of enzyme recovers when inhibitor diluted out, usually non-covalent interaction

Question 21

Noncompetitive inhibition effect on variables-

Answer 21

Decreases Vmax, can increase or decrease Km

Question 22

Competitive inhibition effect on variables-

Answer 22

Increases Km

Question 23

Uncompetitive inhibition effect on variables-

Answer 23

Decreases Km and Vmax

Question 24

Vmax can sometimes be difficult to

Answer 24

measure (e.g., difficult to reach experimentally), and so the Michaelis-Menton can be written in a reciprocal form that, when plotted, allows the user to calculate Vmax (and Km too

Question 25

When [S]<

Answer 25

ES, and so E = E

Question 26

It’s also worth mentioning that kcat/Km is also the

Answer 26

second order rate constant of the over-all enzymatic reaction when [S]<

Question 27

KM =

Answer 27

catalytic efficiency, e.g., rate over affinity of E for S

Question 28

kcat = KM = catalytic efficiency, e.g., rate over affinity of E for S It’s also worth mentioning that kcat/Km is also the second order rate constant of the over-all enzymatic reaction when [S]<

Question 29

Vmax =

Answer 29

k2 [E]T (when enzyme is saturated, i.e., [ES] = [E]T so kcat = k2 when enzyme is saturated kcat

Biochemistry

flashcards

Decks in class (18)

# Cards

• Codes- 1 letter
  20
• 3 letter codes
  21
• Pka values of side chain groups
  5
• Amino Acid R groups
  19
• Chromatographies and SDS
  13
• Alphas and betas (lmao)
  20
• 216 prep
  25
• 218
  14
• Starred notes
  11
• Practice questions I got wrong (and everything else that seems important)
  28
• Last prep!!!
  5
• Exam 2 initial review
  28
• Videos
  57
• Videos part 2
  37
• Last prep
  51
• Last last prep lmao
  14
• Exam study guide
  17
• Exam 3
  31