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Biochemistry I > Chapter 31: Amino Acid Biosynthesis > Flashcards

Chapter 31: Amino Acid Biosynthesis Flashcards

1
Q

Essential amino acids

A

-

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2
Q

Non-essential amino acids

A

-

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3
Q

Root nodule of the pea plant protects

A
  • The nitrogenase enzyme form degradation by oxygen
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4
Q

There is an obligate requirement for nitrogen to

A
  • Synthesize mino acids
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5
Q

Nitrogen, nitrites, and nitrates are used by bacteria and plants, then

A
  • We assimilate them into our diet
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6
Q

The liver is the major organ responsible for

A
  • Nitrogen metabolism

- Amino acid biosynthesis

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7
Q

Amino acids synthesized in the liver

A
  • Glutamate
  • Glutamine
  • Alanine
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8
Q

The most significant reactions in the pathways of amino acids are

A
  • Glutamate dehydrogenase (reversible)
  • Transamination reactions
  • One-carbon transfers
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9
Q

Glutamate dehydrogenase

A
  • Mitochondrial enzyme

- NH3 donated to alpha-ketoglutarate (forms AA glutamate at high livels of NH3)

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10
Q

One-carbon transfers are mediated by either

A
  • Tetrahydrofolate

- S-adenosylmethionine

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11
Q

One 10 of the amino acids required are synthesized

A
  • de novo (non-essential amino acids)
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12
Q

Non-essential amino acids are made

A
  • By the body
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13
Q

Biosynthesis achieved by

A
  • Simple reaction sequences
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14
Q

Essential amino acids must be provided

A
  • In the diet
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15
Q

In infants (+ve N balance) with high urea cycle activity,

A
  • Arginine becomes essential in the diet
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16
Q

Tyrosine is really misclassified since its made from

A
  • The essential amino acid phenylalanine
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17
Q

Although mammals synthesize arginine,

A
  • They cleave most of it to form urea
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18
Q

Phenylalanine hydroxase

A
  • Allows us to convert tyrosine to phenylalanine
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19
Q

Amino acids can also be made with a wide range of

A
  • Synthetic pathways

- 6 basic groups

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20
Q

Oxaloacetate (also in CAC and gluconeogenesis) can be used to make

A
  • Aspartate

- Aspartate can then make arginine, methionine, threonine (then isoleucine), lysine

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21
Q

Pyruvate can be used to make

A
  • Alanine
  • Valine
  • Leucine
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22
Q

Riobse-5-phopshate can by synthetically converted to

A
  • Histidine
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23
Q

3-phosphoglycerate can be used to make

A
  • Serine (AA)

- Serine can then make cysteine and glycine

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24
Q

Pyruvate (also in …) can be used to make

A
  • Alanine
  • Valine
  • Leucine
25
Riobse-5-phopshate (also in ...) can by synthetically converted to
- Histidine
26
3-phosphoglycerate (also in ...) can be used to make
- Serine (AA) | - Serine can then make cysteine and glycine
27
Alpha-ketoglutarate (also in ...) can be used to make
- Glutamate | - Glutamate can then make glutamine, proline, arginine
28
Phosphoenolpyruvate (also in ...) + Erythrose-4-phosphate (also in ...) can be used to make
- Phenylalanine (then tyrosine) - Tyrosine - Tryptophan
29
Cysteine is formed from
- Carbons from serine | - Sulfur from methionene
30
Glysine is formed from
- Serine by a serine hydroxymethyl transferase
31
Reversible transfer of the side chain carbon atom of serine to tetrahydrofolate forms
-glycine | Glycine is a pyridoxical phpsphate
32
Alanine is formed by
- Transamination of pyruvate | - Made from pyruvate in a single step
33
Alanine is the 2nd most abundant
- Amino acid in circulation | - (Number 1 is glutamine)
34
Alanine is important in the glucose-alanine cycle because it links
- Carbohydrate and amino acid metabolism
35
Alanine transaminase (ALT) serum levels are measured to
- Evaluate liver function
36
Alanine is a common substrate for gluconeogenesis by
- Reversal of this alanine formation via transamination of pyruvate reaction
37
Alanine transaminase (ALT) requires
- Pyridoxical cofactor
38
Alanine transaminase (ALT) requires
- Pyridoxical cofactor
39
Aspartate transaminas (AST) catalyzes
- Transamination of oxaloacetate to form aspartate | - Requires pyridoxical phopshate as a cofactor
40
Glutamate (alpha-ketoglutarate) participates in the aspartate transaminase reaction as the
- Amino group donor
41
Serum levels of AST are also utilized in
- Clinical evaluation of liver function
42
The amidation of aspartate is catalyzed by
- Asparagine synthetase | - Requires ATP
43
Nitrogen donor of aspartate amidation reaction
- Glutamine in eukaryotes | - Ammonium in bacteria
44
Glutamate dehydrogenase forms
- Glutamate from alpha ketoglutarate - Reductive amination - Reversible reaction
45
Hydroxyproline is formed from
- Proline catalyzed by a hydroxylase - Requires molecular O2 and vitamin C - Can be post-translationally modified - Involved with collagen
46
Tyrosine (nonessential) is produced by
- Hydroxylation of phenylalanine (essential - from diet)
47
Tyrosine is not usually considered to be an essential amino acid when
- Phenylalanine is present in diet
48
Synthesized form ingested phenylalanine that is converted to tyrosine by
- Phenylalaine hydroxylase
49
Impossible to synthesize phenylalanine
- In the reverse direction
50
In PKU, a deficiency of the enzyme leads to
- Elevated phenylalanine levels in the blood | - Accumulation of
51
In the case of PKU, infants can be placed on
- Special diet - Infants can alter diet again at 3-4 years of age and live a regular life - Diagnosis must be made early
52
Phenylalanine is found in
- Aspartame | - Found in many artificial sweeteners
53
Interconversion of C1 units carried by
- Tetrahydrofolate in amino acid metabolism
54
Methyl-derivative is used to make
- Methionine (methionine synthase) is the most reduced
55
With vitamin B12 deficiency,
- Most THF is trapped in the methyl-derivative/form | - Manifests in pernicious anemia
56
Formyl derivative of THF is the most
- Oxidized form
57
When trapped in the methyl-form, there is a requirement for
- Vitamin B12 | - Absorbtion requires intrinsic factor that is coming from parietal cells
58
In the absence of vitamin B12
- Methyl-form of THF cannot be removed or reused | - Causes circulation problems

Biochemistry I (34 decks)

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