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Biochem > Exam 2 Peng 3 > Flashcards

Exam 2 Peng 3 Flashcards

1
Q

what factors make side chains different?

A

1) charge
2) length
3) aromatic rings
4) branched chain

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2
Q

how do you deaminate aromatic rings?

A

strong enzymes and oxidation

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3
Q

the 20 AA are converted to ___ intermediates products?

A

7 intermediate products, chemical rxn may convert one intermediate product to another

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4
Q

intermediate products directly enter intermediary metabolism, resulting in either the synthesis of?

A

glucose of lipid or energy production

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5
Q

what are he ketogenic amino acids?

A

leucine and lysine

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6
Q

what are the glucogenic AND ketogenic AA?

A

isoleucine, tryptophan, phanylalanine, tyrosine

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7
Q

what are the glucogenic AA?

A

everything except: leucine, lysine, isoleucine, typtophan, phenylalanine, tyrosine

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8
Q

what is the entry point for 3 carbon AA? What are these AA?

A

pyruvate; alanine, cysteine, serine, glycine, threonine, tryptophan, asparate and asparagine

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9
Q

what is the entry point for 5 carbon AA? examples?

A

alpha-ketoglutarate; glutaine, proline, arginine, histodine

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10
Q

how are alanine, cysteine and serine converted to pyruvate?

A

by transamination, oxidative deamination and desulfuration

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11
Q

tryptophan is catabolized to form?

A

alanine

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12
Q

asparate and asparagine are converted to?

A

oxyloacetate (OAA)

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13
Q

proline (oxidized) and glutamine (hydrolyzed) to form?

A

glutamate

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14
Q

arginine is hydrolyzed to produce?

A

ornithine in the urea cycle and converted to glutamate

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15
Q

**histidine converted to?

A

FlGlu

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16
Q

what does FlGlu do?

A

denates formino group to tetragydrofolate (THF)

17
Q

THF is synthesized from?

A

folic acid

18
Q

folic acid deficiency? tested how?

A

increased excretion to FlGlu in urine, espesially after intake of histidine; test by checking urine for folic acid

19
Q

what all is converted to succinyl CoA?

A

methionine, valine, isoleucine, threonine

20
Q

how does methionine convert to succinyl CoA? what intermediate products?

A

through a complicated 9 step process, requires ATP

1) SAM
2) Homocysteine

21
Q

what is SAM? formed? activated methyl group in SAM transferred by?

A

S-adenosylmethionine

  • formed when methionine condenses with adenosine triphosphate
  • methyl transfered by methyltransferases to substrates
22
Q

the reaction to SAM to SAH is?

A

irreversible

23
Q

what is the importance of SAM?

A

MAJOR methyl donor

24
Q

what is homocystein?catalyzed by?

A

resynthesis of methionine

  • remethylated to form methione
  • catalyzed by methionine synthase
25
Q

homocystine reaction back to methionine is influenced by?

A

folic acid and B12

26
Q

where is the methyl group for homocysteine produced from?

A

5-methyl THF (tetrahydrofolate)

27
Q

what is THF? good carrier for what and why? carries where?

A

tetrahydrofolate is a good glycarbon carrier bc it has a pocket structurally to carry different types of carbons
*carries units to methionine, nucleotide synthesis, and alternative synthesis of glycine and serine

28
Q

SAM and THF are both? difference is?

A

Both methyl transfer systems

*SAM can only transfer methyl group, THF can transfer many IC groups (aka with different oxidative states)

29
Q

what is SAH? hydrolized to?

A

S-adenosylhomocysteine

*hydrolyzed to homocysteine and adenosine

30
Q

elevatedlevels of SAH in plasma promotes?

A

oxydative damage, inflammation,andothelial dysfunction

31
Q

what reduced the levels of homocysteine in plasma?

A

B6, B12, and folic acid

32
Q

elevated levels of homocysteine are a marker for what diseases?

A

heart and cardiovascular diseases bc elevated levels lead to oxidative damage

33
Q

homocystinuria and cystathionine are treated how?

A

by B6 and B12 to reduce the elevated levels of homocysteine and vascular disease

Biochem (16 decks)

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