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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
structure of a ketoacid
a C double bond O attached to the COOH group
26
amino acid biosynthesis
addition of amino groups to the carbon skeletons of a-keto acids
27
example of a ketoacid
pyruvate
28
Amino acids undergo oxidative catabolism under three circumstances
Left over proteins, degraded Dietary proteins exceed protein synthesis Starvation, proteins broken down
29
Whats happens to dietary proteins
enzymatically hydrolysed
30
What enzymes breaks down proteins in the stomach
pepsin
31
trypsin and chymotrypsin cut proteins into further peptides in the
small intestine
32
what does amniopeptidase do to proteins crossing over into in intestine
degrade proteins into amnio acids
33
What can also be targeted for destruction and has same endpoint as dietary proteins
cellualr proteins
34
what pathway is used to digest dietary proteins to amino acids
anabolic (storage energy)
35
What happens to proteins that are ingested exceeding body's needs
Have to be catabolised as no storage facility
36
what does glycolysis yield
pyruvate
37
what it it pyruvate transformed into for transport
alanine
38
What is gout
build up uric acid crystallising in the joints
39
causes of gout
high protein diet
40
where is excess glutaine transported
intestines, kidneys and liver
41
Glutamnine is transformed into alanine for transport of amino group as
alanine has 0 charge so can diffuse across membrane easily compared to glutamines -ve charge
42
what does glutamine add on to alanine
amino group
43
what two reactions happen in Glutamate Dehydrogenase Reaction
Two-electron oxidation of glutamate followed by hydrolysis
44
where does glutamate dehydrogenase occur
mitochondria
45
what is the electron acceptor in glutamate dehydrogenase
NAD
46
Glutamate is broken down into
NH4 and ketoglutarate
47
NH4 is synthesised into what
Carbamoyl Phosphate
48
Carbamoyl Phosphate sythetase enzyme requires
Bicarbonate | ATP
49
Ammonia is recaptured by carbamoyl phosphate in the
mitochondria
50
The carbon skeleton of glutamate is
ketoglutarate
51
what is the first nitrogen to enter urea cycle
carbonyl phosphate
52
Where do products of glutamate dehydrogenase go
Urea cycle
53
what is ketoglurate amino group transferred to
asparate
54
what is the second nitrogen to enter urea cycle
asparate
55
where does urea cycle occur
cytosol
56
what happens to cytoskeleton after removal of amino group
converted to glucose or oxidised as part of the citric acid cycle
57
Carbon atoms of degraded amino acids become
metabolic intermediates
58
Name the 6 metabolic intermediates
``` acetly coA pyruvate oxoacetate ketoglutarate Fumarate succinyl-CoA ```
59
where is fumarate produced
from urea cycle
60
Metabolic intermediates are
glucogenic or ketogenic
61
metabolic intermediates are found in which cycle
citric
62
what amino acids are with either ketogenic or glycogenic
isoleucine, tyrosine and phenylalanine
63
what metabolic intermediates are not glycogenic
acetyl coA and acetoacetate
64
glucogenesis
glucose produced from non carbohydrate substates
65
why can't acetyl coA go through glucogenesis
as acetyl coA can not be reconverted to pyruvate therefore can produced glucose
66
what is produced in ketogeneisis
ketone bodies
67
where are ketone bodies produced
Liver
68
What doesn't use ketone bodies
liver
69
where are ketone bodies transported
liver to tissue
70
How do ketone bodies fuel the body
reconverted to acetly coA and go through citric cycle
71
Properties of ketone bodies
small, and water soluble
72
what can L glutamine do
synthesize new amino acids, or it can dispose of excess nitrogen as ammonia
73
what catches toxic ammonia
carbonyl phospahte
74
Carbon skeletons of amnio acids are
broken down to give energy
75
what is inherited metabolic disorders usually due to
single gene defect
76
inherited metabolic diseases usually result in abnormal synthesis of
Proteins Amino acids Carbohydrate Lipids
77
effects of enzyme defects
Decreased formation of the product Accumulation of the substrate Increased formation of other metabolites
78
Heterozygotes of inherited metabolic disorders are usually
phenotypically normal
79
disorder of urea cycle usually occurs on what enzyme
transcarbamoylase
80
Failure of transcarbamoylase in urea cycle results in
elevated ammonia levels (hyperammonaemia)
81
transcarbamoylase synthesises
carbamyl phosphate into citrulline
82
Treatments of transcarbamoylase defect to reduce ammonia levels
introduction of aginine, Sodium phenylbutyrate, and Sodium benzoate, allows urea to be produced
83
Amino acids disorder results in
Decreased product Increased precursors Alternative metabolic products
84
example of amino acid disorder
Phenylketonuria (PKU)
85
what causes PKU
absence of Phenylalanine hydroxylase enzyme, therefore increased levels of Phenylalanine
86
PKU causes
impaired brain development
87
What disorder is PKU
autosomal recessive
88
Diagnosis of PKU
decreased levels of tyrosine
89
Treatment of PKU
low protein diet i.e. with supplement

Medicine Term One (59 decks)

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