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biochem > lecture 10 > Flashcards

lecture 10 Flashcards

1
Q

what is nitrogen

A

critical part of amino acids and nucleotides

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2
Q

nitrification by soil bacteria

A

oxidative process

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3
Q

denitrification

A

anaerobic process

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4
Q

nitrogen fixation by some bacteria

A

reduction of atmos N2

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5
Q

N2 + 10H+ +8e- +16 ATP

A

2NH4+ + 16 ADP +H2

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6
Q

per e

A

2 ATP peer cycle

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7
Q

2 ATP binding

A

shifts reduction potential

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8
Q

clusters of

A

Fe-S

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9
Q

iron Molybdenum

A

cofactor for nitrogenase

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10
Q

8 electrons

A

6 for N2, 2 for H2

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11
Q

nitrogenase

A

perfoms nitrogen fixation

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12
Q

plant derived leghemoglobin

A

Oxygen toxicity to bacterial nitrogenase

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13
Q

glutamine synthetase

A

Catalyzes assimilation of NH4+ into glutamate to yield glutamine

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14
Q

how many subunits does glutamine synthetase have

A

12 identical subunit active sites

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15
Q

how does regulation of nitrogen metabolism occur

A

allosteric regulation
covalent modification

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16
Q

allosteric regulation

A

Ala, Gly, etc. are allosteric inhibitors of enzyme. All 8 molecules needed to effectively block enzyme activity. .

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17
Q

what do adjustments of glutamine react to

A

immediate metabolic requirements

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18
Q

covalent modification

A

adenylation of enzyme tyrosine residue (Tyr397)

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19
Q

adenylation

A

covalent, inhibitory

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20
Q

AT

A

Adenylyltransferase

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21
Q

Uridylyation of Tyr(PII-UMP)

A

stimulates deadenylation

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22
Q

amino acid carbon skeletons are derived from

A

glycolysis
TCA
pentose phosphate pathway

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23
Q

for pathways

A

know key precursors &
intermediates that give rise to specific
AA synthesized

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24
Q

alpha-ketogluterate

A

glutamate
glutamine
proline
arginine

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25
Q

pyruvate

A

alanine
valine
leucine
isoleucine

26
Q

3-phosphoglycerate

A

serine
glycine
cysteine

27
Q

phosphoenolpyruvate/erythrose 4-phosphate

A

tryptophan
phenylalanine
tyrosine

28
Q

oxaloacetate

A

aspartate
asparagine
methionine
threonine
lysine

29
Q

ribose 5-phosphate

A

histidine

30
Q

allosteric regulation of isoleucine

A

feedback inhibition

31
Q

threonine dehydratase

A

inhibited by end product by isoleucine

32
Q

coordinated regulatory mechanisms in eColi

A

have aspartate as precursor

33
Q

isozymes

A

can have or not have allosteric regulation

34
Q

fates of amino group and carbon skeleton

A

take separate but interconnected paths

35
Q

fate of amino group nitrogen

A

removed from AA by aminotransferases to yield ammonia (nitrogen not used in energy-producing pathways)

36
Q

fate of rest of carbon skeleton of AA

A

enter metabolic pathways as precursors of glucose or Krebs cycle intermediates.

37
Q

In many aminotransferase reactions

A

a-ketoglutarate is the amino group acceptor

38
Q

all aminotransferases have

A

pyridoxal phosphate as a cofactor

39
Q

fate of ammonium ions

A

Some used in synthesis of nitrogen compounds (amino acids, nucleotides)

40
Q

excess ammonium ions converted into

A

ammonia, urea, or uric acid (depends on organism) and then excreted

41
Q

what do we derive a small amount of from catabolism of amino acids

A

oxidative energy

42
Q

what are amino acids derived from

A

breakdown of cellular proteins, ingested proteins, & body proteins (when other forms of fuel aren’t available)

43
Q

what do proteins degrade

A

ingested proteins in stomach & small intestine

44
Q

early step in catabolism

A

separation of amino group from carbon skeleton

45
Q

amino group transferred to a-ketoglutarate

A

to form glutamate (REquires PLP)

46
Q

Ammonia from other tissues transported to liver as

A

1) amide nitrogen of glutamine 2) amino group of alanine (from skeletal muscle)

47
Q

pyruvate can be produced by

A

deamination of alanine (liver)

48
Q

pyruvate produced by deamination of alanine

A

is converted to glucose ( transported back to muscle)

49
Q

glucose-alanine cycle

A
50
Q

amino group catabolism

A

depends on the organism NH4 is excreted in different forms

51
Q

urea cycle

A

Arginine to ornithine to citruline to arginosuccinate

carbomoyl phosphate enters right before citruline

aspartate enters right before arginosuccinate

numerate exits after argininosuccinate

urea is produces when water enters after arginine

52
Q

aspartate- argininosuccinate shunt

A

links urea to krebs

53
Q

fumerate from urea cycle

A

becomes malate which enters the Krebs

54
Q

what does alanine serve as

A

a carrier of ammonia & a carbon skeleton of pyruvate from skeletal muscle to the liver

55
Q

pyruvate produced by deamination of alanine

A

is converted to glucose

56
Q

ammonia

A

is excreted

57
Q

phenylketonuria

A

defective process- conversion of phenylalanine to tyrosine

58
Q

phenylalanine hydroxylase

A

error in this enzyme cause phenylketonuria

59
Q

Ammonia

A

most aquatic vertebrates, such as bony fishes and the larvae of amphibia

60
Q

urea

A

many terrestrial vertebrates, also sharks

61
Q

uric acid

A

birds, reptiles

biochem (9 decks)

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