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MCAT > Biochemistry 1 > Flashcards

Biochemistry 1 Flashcards

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MCAT flashcards
1
Q

Glycine

A

Gly, G

non-polar

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2
Q

Alanine

A

Ala, A

non-polar

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3
Q

Valine

A

Val, V

non-polar

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4
Q

Leucine

A

Leu, L

non-polar

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5
Q

Isoleucine

A

Ile, I

non-polar

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6
Q

Methionine

A

Met, M

non-polar

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7
Q

Phenylalanine

A

Phe, F

non-polar

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8
Q

Tryptophan

A

Trp, W

non-polar

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9
Q

Proline

A

Pro, P

non-polar

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10
Q

Arginine

A

Arg, R

positive

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11
Q

Histidine

A

His, H

positive

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12
Q

Lysine

A

Lys, K

positive

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13
Q

Aspartic Acid

A

Asp, D

negative

(aspartate)

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14
Q

Glutamic Acid

A

Glu, E

negative

(glutamate)

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15
Q

Serine

A

Ser, S

polar

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16
Q

Threonine

A

Thr, T

polar

17
Q

Asparagine

A

Asn, N

polar

18
Q

Glutamine

A

Gln, Q

polar

19
Q

Cysteine

A

Cys, C

polar
pKa = 10.28

20
Q

Tyrosine

A

Tyr, T

non-polar

21
Q

isoelectric point

A

pI neutral = average of pKa amine and pKa carboxyl

pI acidic = average of pKa R group and pKa carboxyl

pI basic = average of pKa R group and pKa amine

22
Q

amino acid pKa

A

carboxyl group = 2

acidic R group = 4

histidine group = 6

amine group = 9

basic R group = 11-12

23
Q

trypsin

A

arginine, lysine

24
Q

chymotrypsin

A

phenylalanine, tryptophan, tyrosine

25
Q

Strecker Synthesis

A

nucleophilic addition → nucleophilic acyl substitution

26
Q

Gabriel Synthesis

A
27
Q

transferase

A

transfer functional groups → kinase

28
Q

hydrolase

A

hydrolysis

29
Q

isomerase

A

rearranges bonds within a molecule to form an isomer (epimerase)

30
Q

lyase

A

AB ⟷ A + B

cleavage / synthesis

31
Q

ligase

A

addition / synthesis of large molecules

usually ATP dependent

32
Q

Km

A

measure of an enzyme’s affinity for its substrate

↑ Km = ↓ affinity

↓ Km = ↑ affinity

Km = [S] @ 1/2 Vmax

33
Q

Michaelis-Menten Equation

A
34
Q

Lineweaver-Burk Plot

A

y-intercept = 1/Vmax

x-intercept = 1/Km

35
Q

competitive inhibitor

A

inhibitor binds to active site

Vmax → no change

Km → increases

36
Q

uncompetitive inhibitor

A

inhibitor binds to E-S complex

Vmax → decreases

Km → decreases

37
Q

non-competitive inhibitor

A

inhibitor binds away from active site → shape of enzyme changes

has equal affinity for enzyme and E-S complex

Vmax → decreases

Km → no change

38
Q

mixed inhibitor

A

inhibitor has unequal affinity for enzyme and E-S → favors one over the other

Vmax → decreases

↑ affinity for enzyme → Km = increases
↑ affinity for E-S → Km = decreases

MCAT (15 decks)

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