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MCBM Exam 1 > 4 - Amino Acids > Flashcards

4 - Amino Acids Flashcards

1
Q

What amino acid is not chiral

A

Glycine

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2
Q

What are the 3 major purposes of Amino Acids

A

(1) Generation of Energy (2) Protein Synthesis (3) Synthesis of Heme, Purines, Melanin, Pyrimidines

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3
Q

α amino acids means

A

the amino and carboxyl group is
attached to the same carbon
atom (called the α carbon)

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4
Q

β amino acids means

A

theamino group is attached to the
second carbon away from the
carboxyl group (called the β
carbon)

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5
Q

What Amino acid does not have a Beta

A

Glycine

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6
Q

Only what isomer and what form is used in natural proteins

A

L isomer and α Form

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7
Q

D-Amino acids govern

A

stationary phase cell wall remodeling in bacteria

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8
Q

D amino acids also appear to do what

A

Appear to modulate synthesis of

peptidoglycan

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9
Q

D-Met and D-Leu

A

Vibrio cholerae

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10
Q

D-Tyr and D-Phe

A

Bacillus subtilis

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11
Q

What form of the peptide bond is favored

A

Trans

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12
Q

The peptide bond is metastable and
hydrolyzes in an aqueous environment
only in the presence

A

of a catalyst

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13
Q

What determines how a protein will fold

A

Side chains

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14
Q

The 3 characteristics of Branched Chain AA

A 
• Very nonpolar
(hydrophobic) R
groups
• Contribute greatly to
the hydrophobic
effect which drives
protein folding
• Found in the interior
of proteins
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15
Q

What are the 3 branched chain AA

A

Isoleucine, Leucine, Valine

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16
Q

What are the hydroxyl AA

A

Serine and Threonine

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17
Q

R groups contribute heavily to the formation of

A

hydrogen bonds

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18
Q

Hydroxyl AA also form bonds with

A

– Carbohydrates in
glycoproteins
– Phosphate in
phosphoproteins

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19
Q

What are the sulfur containing AA

A

Cysteine and Methionine

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20
Q

Disulfide bonds are very

important in

A

3D Structure

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21
Q

Insulin is made up of

A

2 peptide chains joined

together by 3 disulfide bonds

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22
Q

Sulfur containing AA are very hydrophobic or hydrophilic

A

Hydrophobic

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23
Q

Sulfur containing AA are participate as

A

Free Radical Scavenger

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24
Q

What is the precursor of
the methyl group donor S -
adenosylmethionine (SAM)

A

Methionine

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25
Q

What are the aromatic AA

A

Phenylalanine, Tyrosine, Tryptophan

26
Q

Aromatic amino acids are

usually sequestered in the what

A

Interior of protein

27
Q

hydrophobic effect is quite substantial in stabilizing the 3-D structure by

A

by lowering the free energy involved in folding

28
Q

What 2 Aromatic AA can form hydrogen bonds

A

Tyrosine and tryptophan

29
Q

Both tryptophan and tyrosine absorb

A

UV Light

30
Q

Acidic Amino Acids 4 functions

A
  • Serve as proton donors
  • Help make proteins more hydrophilic
  • Can also make hydrogen bonds
  • Help maintain the pH in active sites
31
Q

What are the acidic amino acids

A

Aspartate, Asparagine, Glutamate, Glutamine

32
Q

What are the basic amino acids

A

Lysine, Arginine, Histidine

33
Q

Basic amino acid functions

A 
• Serve as proton
acceptors
• Contribute
somewhat to the
pH
• Can help
activate
substrates for
enzymes by
abstracting a
proton
34
Q

What does proline do to chain

A

Introduces kinks into protein chain due to its bent structure

35
Q

Isoelectric point is

A

point at which there is no net charge (pI)

36
Q

Amino acid modifications can be used to tag proteins for

A

degradation

37
Q

What are the types of amino acid modifications

A
  • Glycosylation
  • Fatty Acylation or Prenylation
  • Regulatory modifications
38
Q

Essential AA means that

A

Cannot be synthesized by human body, must get from diet

39
Q

What are the essential AA

A
  • Valine
  • Threonine
  • Leucine
  • Methionine
  • Isoleucine
  • Lysine
  • Phenylalanine
  • Histidine
  • Tryptophan
40
Q

All amino acids except what two are at least partially glucogenic

A

Lysine and Leucine

41
Q

What are the only amino acids that are solely ketogenic

A

Lysine and Leucine

42
Q

What doe Lysine and Leucine give rise to

A

acetylCoA or acetoacetylCoA

43
Q

What amino acids give rise to both glucose and fatty acid precursors and are thus glucogenic and
ketogenic

A

isoleucine, phenylalanine, threonine, tryptophan, and tyrosine

44
Q

Tyrosine is the precursor to

A

(1) Dopamine (2) Epinephrine (3) Tyrosine

45
Q

Tryptophan is the precursor to

A

Serotonin

46
Q

Phenylalanine is the precursor to

A

Dopamine

47
Q

Glycine Degradation is carried out by

A

Glycine cleaving enzyme

48
Q

Deficiency in Glycine cleaving enzyme can cause

A

Nonketotic hyperglycinemia

49
Q

Nonketotic hyperglycinemia causes

A

death infancy or profound mental retardation in

survivors

50
Q

Glycine can also be converted into

A

Oxalate (which is found in most kidney stones)

51
Q

Deficiency in cystathionine synthase will lead to

A

Leads to accumulation of homocysteine and

methionine

52
Q

How is def in cystathionine synthase treated

A

restricting dietary methionine and adding folic

acid supplements

53
Q

Maple Syrup Urine Disease is a disorder with a deficiency in what

A

branched chain α keto acid dehydrogenase

54
Q

Complete deficiency of branched chain α keto acid dehydrogenase leads to

A

– Severe mental retardation
– Acidosis
– Sweet odor to urine
– Early death

55
Q

What supplement is sometimes useful for treating Maple Syrup Urine Disease

A

Thiamine

56
Q

Phenylketonuria is caused by

A

complete lack of phenylalanine hydroxylase

57
Q

With phenylketonuria, why are there no abnormalities at birth

A

because phenylalanine and
metabolites are transferable
across placenta

58
Q

Why do pts with PKU have a lighter complexion

A

Phenylalanine cannot be converted to Tyrosine which is a precursor to melanin

59
Q

PKU can be treated by

A

severely restricting dietaryphenylalanine

60
Q

In PKU what is also hazardous to the pt

A

Aspartame

61
Q

Why can the special diet in PKU be tapered off in adolescents

A

Only developing brain is vulnerable to

PKU

MCBM Exam 1 (6 decks)

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