module 12- amino acid synthesis Flashcards

1
Q

what is the endpoint of nitrogen fixation

A

ammonium

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2
Q

glutamate dehydrogenase

A

a-ketoglutarate -> glutamate

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3
Q

glutamine synthetase

A

glutamate -> glutamine

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4
Q

glutamate synthase

A

a-ketoglutarate -> 2 glutamate

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5
Q

what is the regulatory enzyme of nitrogen metabolism

A

glutamine synthetase

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6
Q

T or F: glutamine synthetase is present in all organisms

A

T

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7
Q

ubiquitous enzyme

A

present in all organisms

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8
Q

how is glutamine synthetase regulated (2)

A

covalent modification & allosterically

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9
Q

how many allosteric inhibitors? how many come from glutamine and how many from amino acids

A

8 total, 6 from glutamine & 2 from amino acids

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10
Q

concerted inhibition

A

effects are more than additive

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11
Q

allosteric inhibitors are ( ) inhibition

A

concerted

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12
Q

covalent modification of glutamine synthetase

A

adenylylation

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13
Q

adenylylation

A

linking AM to tryosine

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14
Q

glutamine synthetase is a ( ) structure

A

quaternary & has multiple subunits which each have an active site

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15
Q

consequence of adenylylation

A

insensitive to allosteric inhibitors, need combination of covalent & allosteric to control activity

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16
Q

SAM

A

adds methyl groups

17
Q

why is SAM used over methione?

A

methionine is not very reactive

18
Q

methyl groups are almost always transferred to a ( ) or ( ) atom

A

nitrogen or oxygen

19
Q

N-methyltransferase

A

SAM transfers nitrogen to norepinephrine

20
Q

what is tetrahydrofolate derived from

A

vitamin B9 (folate)

21
Q

what does N5 & N10 indicate?

A

indicate specific atoms in tetrahydrofolate to which carbons are attached

22
Q

source of one-carbon units

A

serine or formate, oxygen, nitrogen

23
Q

T or F: tetrahydrofolate is a carrier of very diverse types of one-carbon units

A
24
Q

aspargaine synthetase

A

aspartate -> asparagine

25
Q

T or F: both glutamine & glutamate act as amino group donors at different steps of the synthetic pathway for histidine in plants

A

T

26
Q

what 3 metabolic pathways supply the intermediates that amino acids are synthesized from?

A

glycolysis, pentose phosphate, CAC

27
Q

conditionally essential amino acids

A

essential only during specific points

28
Q

what are the 5 non-essential amino acids

A

alanine, asparagine, aspartate, glutamate & serine

29
Q

what amino acids can be derived from oxaloacetate

A

aspartate, asparagine, methionine, lysine, & threonine

30
Q

what amino acids can be derived from pyruvate

A

alanine, valine, leucine & isoleucine

31
Q

what is used as an amino group donor in lysine pathway

A

glutamate

32
Q

product inhibition

A

end product acts as allosteric inhibitor of 1st step

  • prevents unnecessary production of F when levels are sufficient
33
Q

sequential inhibition

A

branched into 2 end points, F & G inhibit 1st committed step

F & G inhibit the conversion of C to D and E, and C acts back on A to B

34
Q

concerted inhibition

A

F & G inhibit A to B

35
Q

enzyme multiplicity

A

2 isoenzymes are inhibited by F or G

allows fine tuning

36
Q

what 2 molecules provide entry points for the assimilation of ammonium into biomolecules

A

glutamine & glutamate

37
Q

what process does glutamate donates its amino groups for the synthesis of other amino acids?

A

transamination

38
Q

what 2 molecules provide 1 carbon units for the synthesis of biomolecules

A

tetrahydrofolate derivatives & SAM

39
Q

oxaloacetate is a direct precursor for which animo acid?

A

aspartate