Amino acid synthesis and degradation and urea cycle :/ Flashcards

1
Q

How are amino acids obtained

A

diet
synthesised by body
produced from normal protein turnover (recycled)

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2
Q

what happens if aa are not required

A

degredated

can be used as a source of energy

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3
Q

can amino acids be stored or not

A

cannot be stored

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4
Q

List some essential aa from the diet

A
histidine
isoleucine
leucine
lysine
methaionaine
phenylalanine
threonine
typtophan
valine
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5
Q

non essential aa examples

A
alanine
aspargine
aspartate
glutamate
serine
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6
Q

conditionally essential aa examples

A
arginine
cysteine
glutamine
glycine
proline
tyrosine
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7
Q

what is cystinuria

A

defective carrier system
- leads to aa in urnine
crystals of cysteine form kidney stones

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8
Q

what happens when nitrogen is consumed in the diet

A

usually consumed in a form of protien
- hydrolysed to aa by proteolytic enzymes
aa AT into epithelial cells and enter blood

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9
Q

what are the proteolytic enzymes and where are they found

A

pepsin in stomach

trypsin in pancreas

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10
Q

what is required to make aa

A

carbon

nitrogen

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11
Q

what can aa be made from

A

glucose and nitrogen source) aa or ammonia)

can be made from intermediates of glycolysis and the TCA cyecle

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12
Q

what amino acids can be made from aa

A

non essential amino acids can be made from essential

- donate molecule

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13
Q

why would aa be needed to degradate

A

excess in diet

some no longer needed

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14
Q

types of aa

A

Glucogenic aa

ketogenic aa

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15
Q

degredation of glycogenic aa

A

carbons converted to glucose

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16
Q

degradation of ketogenic

A

converted to acetylene Ca or acetoacetate(ketone bodies)

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17
Q

what does the amino acid split into

A

carbon skeleton

amino acid nitrogen

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18
Q

how is nitrogen removed from aa

A

transamination

- amino group from one aa transferred to another

19
Q

removal of aa nitrogen as ammonia

A

glutamate can collect nitrogen from other aa
converted to ammonia by glutamate dehydrogenase in the liver
aa enters urea cycle

20
Q

what is removal aa nitrogen as ammonia alllostericaly alters by

A

allosteric regualtion by :

  • ATP and GTP (inhibits)
  • ADP and Gdp activates
21
Q

lysosome

A

protease filled vesicles

22
Q

ubituitin

A

small protiens that target proteins for degredation

23
Q

proteasome

A

protease complex
proitne is unfolded and degraded
- easier for the protein to be degredated by proteases

24
Q

what form of nitrogen is not usable in biological systems

A

NH2

25
Q

nitrogen that is usabel

A

NH3

26
Q

nitrogen that is toxic

A

NH4+

27
Q

nitrogen balance

A

nitrogen ingested (proteins)= nitrogen excreted

28
Q

children and preganen woman nitrogen balance

A

+

29
Q

disease / starvation nitrogen balance

A

-

30
Q

nitrogen cycle

A
5 main steps
1st 2 in mitochondrion
other 3 in cytosol
nitrogen enters as NH4+ and aspartate
ornithine initiates and is regenerated
31
Q

control of the urea cyle

A

feed forward regulation
allosteric activate of enzymes
high protein diet or fasting induces urea cycle ensymes

32
Q

feed forward urea control

A

high rate of ammonia production higher rate of urea

33
Q

what enzymes allosterically control the urea cycle

A

arginine stimulates carbonyl phosphate synthase§

34
Q

what is the glucose alanine cycle

A

cycling of nutrients between muscles and liver

35
Q

what does the glucose alanine cycle dependon

A

physiological state i.e. fed or fastine

36
Q

what occurs on fasting

A

muscle protein broken down to aa
transaminate to form alanine
transported to liver
nitrogen enters urea cycle and pyruvate used to make energy (glucose)

37
Q

what are Ketone bodies

A

combination of acetoacetate and beta hydroxybutyrate

38
Q

what happens to Ketone bodies when glucose is low

A

reconverted to acetylene coA

enter TCA cycle for entry

39
Q

what can acetoacetate break down to

A

acetone spontaneously

40
Q

what is a diagnostic tool for ketonic states

A

fruity breath

41
Q

Phenylketonuria

A

mutation in phenylalanine hydroxylate
leads to metal retardation
affects nervous tissue

42
Q

urea cycle disroder

A

accumulation of ammonia

toxic to NS

43
Q

inborn errors of aa metabolism

A

deficient enzymes in aa metabolism

leads to accumulation of harmful producs

44
Q

what are some inborn errors in aa metabolism examples

A

phenylketonura

urea cycle disorders