Biochem part 1 Flashcards

1
Q

All 20 amino acids are in the L-form except for _____

A

Glycine

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2
Q

All 20 amino acids contain a chiral carbon except for ____

A

Glycine

-NOT in L-form

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3
Q

2 purely ketogenic Amino Acids

A

Leucine
Lysine
(lindsay lohan- NOT used for gluconeogenesis)

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4
Q

3 Aromatic AA’s

-How many of these are essential?

A

Phenylalanine - essential
Tyrosine
Tryptophan - essential

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5
Q

4 sulfur containing AA’s

A

Cysteine
Cystine
Methionine - essential
Taurine

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6
Q

branched chain AA’s

A

Leucine
Isoleucine
Valine

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7
Q

Disease in which one cannot break down BCAA’s

A

Maple syrup urine disease

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8
Q

2 Acidic AA’s

A
Aspartic acid (aspartate)
Glutamic acid (glutamate)
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9
Q

3 Basic AA’s

A

Histidine
Lysine
Arginine

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10
Q

AA’s which have the greatest positive net charge at normal pH of blood are considered (acidic/basic)

A

Basic

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11
Q

Wheat and rice’s limiting AA

A

neither contain Lysine

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12
Q

Pulses/Lentils limiting AA

A

Methionine

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13
Q

Corn’s limiting AA

A

Lysine and Tryptophan

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14
Q

Tyrosine is derived from which AA

A

Phenylalanine

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15
Q

Catecholamines (Epi and NE) are derived from which AA

A

Tyrosine —>L-dopa —-> dopamine—NE and Epi

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16
Q

T3 and T4 are derived from which AA

17
Q

Melatonin and Nicotinamide are derived from which AA

A

Tryptophan

18
Q

what is a Zwitter ion

A

when an AA is at its isoelectric point (no net electrical charge)

19
Q

Cofactor for glutathione peroxidase

20
Q

Tripeptide of Glycine + Glutamate + Cysteine = ______

A

Glutathione

21
Q

2 DNA strands together by hydrogen bonds is an example of (1,2,3, or 4) protein structure

A

Secondary

alpha helices and beta pleated sheets

22
Q

Classic example of a Tertiary protein structure

A

Myoglobin

-disulfide bonds

23
Q

Tertiary protein structures contain which type of bonds

A

Disulfide bonds

-myoglobin

24
Q

Classic example of Quaternary protein structure

A

Hemoglobin

  • hydrogen and disulfide bonds
  • Insulin, Antibodies
25
Bond type found in Quaternary protein structures
Hydrogen AND Disulfide bonds
26
A low Km will equal a (high or low) enzyme affinity
High affinity | -Inverse relationship
27
Enzymes increase the rate of the reaction by lowering the _________
activation energy
28
3 major factors that affect the reaction velocity of an enzyme
Substrate concentration Temp. pH
29
what is the Km
amount of substrate required to reach 1/2 Vmax
30
Noncompetitive inhibitors will have what effect on the Km
No change in Km
31
Competitive inhibitors will have what effect on the Km
Increase the Km
32
(Competitive or Noncompetitive) inhibitors will decrease the Vmax
Noncompetitive
33
a + Gibbs free energy means that a reaction is (favorable, equilibrium, or unfavorable)
Unfavorable -non spontaneous -requires energy/heat (<1 Keq)