Biochem Exam 1: Set 2 (Acid-Base, Enzymes and Catalysis) Flashcards

1
Q

Name a prevalent amphipathic biological molecule

A

phosopholipid

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2
Q

What is normal blood pH?

A

7.35-7.45

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3
Q

What is the Henderson-Hasselbalch equation, and what is it used for?

A

pH= pKa + log([A-]/[HA])

Used to relate the concentration of buffer species, the pKa of the buffer, and the solution pH

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4
Q

What are the three biological buffer systems?

A

Biocarbonate, phosphate, and protein systems

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5
Q

How is Hb affinity for oxygen effected if pH is lowered

A

lower oxygen affinity

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6
Q

The pKr of which amino acid is close to biological pH?

A

Histidine

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7
Q

What are normal serum bicarbonate levels?

A

24-28 mmol/L

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8
Q

What indicates metabolic acidosis, and what causes it?

A

decreased pH, low HCO3-

caused by increased acid production (which causes an increased anion gap) or loss of HCO3- (e.g. diarrhea)

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9
Q

What indicates respiratory acidosis?

A

decreased pH, high pCO2

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10
Q

What is Kussmaul’s respiration?

A

rapid deep breaths usually associated with diabetic ketoacidosis

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11
Q

How do catalysts effect the reaction rate and equilibrium?

A

increases rate, equilibrium is constant

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12
Q

How would you test for liver damage?

A

ALT assay- ALT is a liver enzyme that is released into the blood after liver damage

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13
Q

What is the general function of oxidoreductase enzymes?

A

transfer of electrons

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14
Q

What is the general function of hydrolase enzymes?

A

addition of water

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15
Q

What is the general function of isomerase enzymes?

A

interconvert between isomers

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16
Q

What is the general function of transferase enzymes?

A

transfer a functional group

17
Q

What is the general function of lyase enzymes?

A

form or remove double bonds

18
Q

What is the general function of ligase enzymes?

A

condensation of two molecules to form bond

19
Q

How to enzymes effect the change in free energy of a reaction?

A

lower the change in free energy

20
Q

Why are transition state analogs a target for drug development?

A

enzymes favor binding transition state, and transition state analogs are stable as opposed to unstable transition state of natural substrates, which makes the drugs bind more tightly than the substrate

21
Q

How do enzymes increase the effective concentration of a substrate?

A

Brings substrates closer together and undergoes a conformational change: Proximity and Orientation

22
Q

How does acid-base catalysis function?

A

residues in active site donate/accept protons

23
Q

How does covalent catalysis function?

A

covalent intermediate is formed between substrate and enzyme

24
Q

What is a zymogen?

A

an inactive form of an enzyme (typically digestive proteases)

25
Q

What is the Michaelis-Menton equation?

A

V0=Vmax[S]/(Km+[S])

26
Q

What is kcat a measure of?

A

kcat= turnover number; measures molecules catalyzed per time

27
Q

Given the in vivo [S] for an enzyme, how could you approximate the Km of the enzyme?

A

Km ~ typical in vivo [S]

28
Q

How would you obtain a Lineweaver-Burk plot

A

reciprocal of M-M equation

29
Q

In a Lineweaver-Burk plot was is the slope of the line?

A

Km/Vmax

30
Q

Where does a competitive inhibitor bind and how does it effect Km and Vmax?

A

binds active site

Raises Km, Vmax is unchanged

31
Q

Statins act as what type of inhibitor of HMG-CoA reductase?

A

competitive

32
Q

Where does a noncompetitive inhibitor bind and how does it effect Km and Vmax?

A

binds to allosteric site

Km is unchanged, Vmax is decreased

33
Q

How do uncompetitive inhibitors function?

A

binds the enzyme-substrate complex

34
Q

Give an example of isozymes

A

Hexokinase and Glucokinase

35
Q

Phosphorylation and dephosphorylation occur on what amino acids?

A

Ser, Thr, Tyr

36
Q

What are some characteristics of rate-limiting steps in a reaction?

A

Thermodynamically unfavorable
Kinetically slow
Subject to regulatory mechanisms
Often inhibited by final product of reactions