Biochemistry 1 Flashcards by Schuyler Nissen

Glycine

Gly, G

non-polar

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Alanine

Ala, A

non-polar

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Valine

Val, V

non-polar

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Leucine

Leu, L

non-polar

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Isoleucine

Ile, I

non-polar

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Methionine

Met, M

non-polar

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Phenylalanine

Phe, F

non-polar

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Tryptophan

Trp, W

non-polar

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Proline

Pro, P

non-polar

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Arginine

Arg, R

positive

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Histidine

His, H

positive

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Lysine

Lys, K

positive

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Aspartic Acid

Asp, D

negative

(aspartate)

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Glutamic Acid

Glu, E

negative

(glutamate)

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Serine

Ser, S

polar

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Threonine

Thr, T

polar

Asparagine

Asn, N

polar

Glutamine

Gln, Q

polar

Cysteine

Cys, C

polar
pKa = 10.28

Tyrosine

Tyr, T

non-polar

isoelectric point

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

amino acid pKa

carboxyl group = 2

acidic R group = 4

histidine group = 6

amine group = 9

basic R group = 11-12

trypsin

arginine, lysine

chymotrypsin

phenylalanine, tryptophan, tyrosine

Strecker Synthesis

nucleophilic addition → nucleophilic acyl substitution

Gabriel Synthesis

transferase

transfer functional groups → kinase

hydrolase

hydrolysis

isomerase

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

lyase

AB ⟷ A + B cleavage / synthesis

ligase

addition / synthesis of large molecules usually ATP dependent

measure of an enzyme's affinity for its substrate ↑ Km = ↓ affinity ↓ Km = ↑ affinity Km = [S] @ 1/2 Vmax

Michaelis-Menten Equation

Lineweaver-Burk Plot

y-intercept = 1/Vmax x-intercept = 1/Km

competitive inhibitor

inhibitor binds to active site Vmax → no change Km → increases

uncompetitive inhibitor

inhibitor binds to E-S complex Vmax → decreases Km → decreases

non-competitive inhibitor

inhibitor binds away from active site → shape of enzyme changes has equal affinity for enzyme and E-S complex Vmax → decreases Km → no change

mixed inhibitor

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