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Medicine Term One > Nitrogen > Flashcards

Nitrogen Flashcards

1
Q

How do nitrogen fixing bacteria live

A

anerobically

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2
Q

what inactivates nitrogen fixing bacteria

A

oxygen

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3
Q

what do root nodules on legumes contain

A

Rhizobium bacteria

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4
Q

example of nitrogen fixing bacteria

A

cyanobacteria

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5
Q

Why are leguminous plants important for nitrogenous activity

A

legheamoglobin combines to oxygen making conditions aerobic therefore nitrogenase can work

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6
Q

Nitrogen fixing requires

A

nitrogenase enzyme and a lot of ATP

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7
Q

cyanobacteria forms what to prevent oxygen entry

A

heterocysts

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8
Q

example of symbiotic relationship

A

Leguminous plants and nitrogenase

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9
Q

what usable form of nitrogen is taken up by plants

A

Nitrate

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10
Q

Flow of N from NH4+ to other biomolecules occurs through

A

glutamate

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11
Q

Glutamate formed by

A

ketoglutarate and ammonia

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12
Q

what 4 amino acids are held in much higher concentrations

A

Alanine, glutamine, glutamate and aspartate

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13
Q

organisms can fix N2 therefore conserve nitrogen by

A

Transaminations

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14
Q

Whats is transamination

A

transfer of amino groups between different molecules

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15
Q

Taking an amino acid of creates a

A

ketoacid

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16
Q

In transamination one of the two substrates always has to be

A

glutamate

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17
Q

the synthesis and degradation of amnio acids is

A

reversible

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18
Q

what typically accepts amino groups

A

α-ketoglutarate

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19
Q

The enzyme catalysing transamination is

A

aminotransferases

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20
Q

aminotransferases depends on cofactor

A

pyridoxal phosphate

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21
Q

what acts as temporary storage for nitrogen

A

L glutamine

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22
Q

pyridoxal phosphate derive from

A

vitamin b6

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23
Q

If aminotransferase present in plasma indicates

A

cell damage i.e. liver disease

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24
Q

structure of amino acid

A

NH3 group attached to a carbon which is attached to a COOH

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25
Q

structure of a ketoacid

A

a C double bond O attached to the COOH group

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26
Q

amino acid biosynthesis

A

addition of amino groups to the carbon skeletons of a-keto acids

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27
Q

example of a ketoacid

A

pyruvate

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28
Q

Amino acids undergo oxidative catabolism under three circumstances

A

Left over proteins, degraded
Dietary proteins exceed protein synthesis
Starvation, proteins broken down

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29
Q

Whats happens to dietary proteins

A

enzymatically hydrolysed

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30
Q

What enzymes breaks down proteins in the stomach

A

pepsin

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31
Q

trypsin and chymotrypsin cut proteins into further peptides in the

A

small intestine

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32
Q

what does amniopeptidase do to proteins crossing over into in intestine

A

degrade proteins into amnio acids

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33
Q

What can also be targeted for destruction and has same endpoint as dietary proteins

A

cellualr proteins

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34
Q

what pathway is used to digest dietary proteins to amino acids

A

anabolic (storage energy)

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35
Q

What happens to proteins that are ingested exceeding body’s needs

A

Have to be catabolised as no storage facility

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36
Q

what does glycolysis yield

A

pyruvate

37
Q

what it it pyruvate transformed into for transport

A

alanine

38
Q

What is gout

A

build up uric acid crystallising in the joints

39
Q

causes of gout

A

high protein diet

40
Q

where is excess glutaine transported

A

intestines, kidneys and liver

41
Q

Glutamnine is transformed into alanine for transport of amino group as

A

alanine has 0 charge so can diffuse across membrane easily compared to glutamines -ve charge

42
Q

what does glutamine add on to alanine

A

amino group

43
Q

what two reactions happen in Glutamate Dehydrogenase Reaction

A

Two-electron oxidation of glutamate followed by hydrolysis

44
Q

where does glutamate dehydrogenase occur

A

mitochondria

45
Q

what is the electron acceptor in glutamate dehydrogenase

A

NAD

46
Q

Glutamate is broken down into

A

NH4 and ketoglutarate

47
Q

NH4 is synthesised into what

A

Carbamoyl Phosphate

48
Q

Carbamoyl Phosphate sythetase enzyme requires

A

Bicarbonate

ATP

49
Q

Ammonia is recaptured by carbamoyl phosphate in the

A

mitochondria

50
Q

The carbon skeleton of glutamate is

A

ketoglutarate

51
Q

what is the first nitrogen to enter urea cycle

A

carbonyl phosphate

52
Q

Where do products of glutamate dehydrogenase go

A

Urea cycle

53
Q

what is ketoglurate amino group transferred to

A

asparate

54
Q

what is the second nitrogen to enter urea cycle

A

asparate

55
Q

where does urea cycle occur

A

cytosol

56
Q

what happens to cytoskeleton after removal of amino group

A

converted to glucose or oxidised as part of the citric acid cycle

57
Q

Carbon atoms of degraded amino acids become

A

metabolic intermediates

58
Q

Name the 6 metabolic intermediates

A 
acetly coA
pyruvate 
oxoacetate 
ketoglutarate 
Fumarate 
succinyl-CoA
59
Q

where is fumarate produced

A

from urea cycle

60
Q

Metabolic intermediates are

A

glucogenic or ketogenic

61
Q

metabolic intermediates are found in which cycle

A

citric

62
Q

what amino acids are with either ketogenic or glycogenic

A

isoleucine, tyrosine and phenylalanine

63
Q

what metabolic intermediates are not glycogenic

A

acetyl coA and acetoacetate

64
Q

glucogenesis

A

glucose produced from non carbohydrate substates

65
Q

why can’t acetyl coA go through glucogenesis

A

as acetyl coA can not be reconverted to pyruvate therefore can produced glucose

66
Q

what is produced in ketogeneisis

A

ketone bodies

67
Q

where are ketone bodies produced

A

Liver

68
Q

What doesn’t use ketone bodies

A

liver

69
Q

where are ketone bodies transported

A

liver to tissue

70
Q

How do ketone bodies fuel the body

A

reconverted to acetly coA and go through citric cycle

71
Q

Properties of ketone bodies

A

small, and water soluble

72
Q

what can L glutamine do

A

synthesize new amino acids, or it can dispose of excess nitrogen as ammonia

73
Q

what catches toxic ammonia

A

carbonyl phospahte

74
Q

Carbon skeletons of amnio acids are

A

broken down to give energy

75
Q

what is inherited metabolic disorders usually due to

A

single gene defect

76
Q

inherited metabolic diseases usually result in abnormal synthesis of

A

Proteins
Amino acids
Carbohydrate
Lipids

77
Q

effects of enzyme defects

A

Decreased formation of the product
Accumulation of the substrate
Increased formation of other metabolites

78
Q

Heterozygotes of inherited metabolic disorders are usually

A

phenotypically normal

79
Q

disorder of urea cycle usually occurs on what enzyme

A

transcarbamoylase

80
Q

Failure of transcarbamoylase in urea cycle results in

A

elevated ammonia levels (hyperammonaemia)

81
Q

transcarbamoylase synthesises

A

carbamyl phosphate into citrulline

82
Q

Treatments of transcarbamoylase defect to reduce ammonia levels

A

introduction of aginine, Sodium phenylbutyrate, and Sodium benzoate, allows urea to be produced

83
Q

Amino acids disorder results in

A

Decreased product
Increased precursors
Alternative metabolic products

84
Q

example of amino acid disorder

A

Phenylketonuria (PKU)

85
Q

what causes PKU

A

absence of Phenylalanine hydroxylase enzyme, therefore increased levels of Phenylalanine

86
Q

PKU causes

A

impaired brain development

87
Q

What disorder is PKU

A

autosomal recessive

88
Q

Diagnosis of PKU

A

decreased levels of tyrosine

89
Q

Treatment of PKU

A

low protein diet i.e. with supplement

Medicine Term One (59 decks)

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