Protein META Flashcards

1
Q

The amount of nitogen excreted in a day is = amount consumed daily as dietary proteins
TRUE OR FALSE?

A

True

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2
Q

During tissue growth, growing children, or after surgery
Nitrogen balance is =

A

Intake is greater than output
Since there’s nitrogen retention for building new tissues

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3
Q

In fever, starvation or cachexia nitrogen balance is -very
True or false

A

True
Intake is less than loss

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4
Q

During lactation and pregnancy the nitrogen balance is?

A

Positive

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5
Q

The amount of protein synthesized and broken down in a day is?

A

300-400g/day
350-400g/day

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6
Q

The amount of amino acids poll in the body is?

A

100gm

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7
Q

All amino acids are transaminated except?

A

Lysine, threonine, proline
They follow a degredative pathway

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8
Q

Transanimation takes place in ____ part of the cell

A

Cytoplasm

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9
Q

Oxidative deamination takes place in ____ part of the cell?

A

Mitochondria

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10
Q

Metabolism of amino acids can lead to the production of?

A

ATP, Non essential amino acids, glucose( gluconeogenesis), formation of lipids

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11
Q

What amino acid reacts with alpha krto glutamate to form Oxaloacet and glutamate?

A

Asparate and asparagine

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12
Q

What amino acid reacts with alpha krto glutamate to form fumarate and glutamate?

A

Phenylalanine and tryosine

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13
Q

What amino acid reacts with alpha krto glutamate to form pyruvate and glutamate?

A

Alanine, Glysine, Serine,Cysteine, Tryptophan and Threorine

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14
Q

What amino acid reacts with alpha krto glutamate to form alpha keto glutamate and glutamate?

A

Glutamate—–Arginine, Glutamine,Histidine, Proline

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15
Q

What amino acid reacts with alpha krto glutamate to form Acetyl CoAand glutamate?

A

Leucine, Tryptophan, Threonine, Isoleucine

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16
Q

The coenzyme of Transamination is?

A

Pyridoxal Phosphate ( Amino Tranferase)

17
Q

What’s deamination?

A

The removal of nitrogen from amino acids as NH4

18
Q

Oxidative deamination is catalyzed by?

A

Glutamate dehydrogenase or Amino acid oxidase

19
Q

Non Oxidative deamination is catalyzed by?

A

Amino acid dehydratase
And AA disulphydeatase

20
Q

What’s the function of oxidative deamination by glutamate dehydrogenase Catabolically and Anabolically?

A

Cata— channels N from glutamate to ammonia
Ana– catalyzes amination of alpha keto glutamate to glutamate

21
Q

What amino acid undergo non- oxidative deamination?

A

AA dehydrogenase
Serine, homoserine and threonine
AA disulfhydrase
Cysteine and homo cysteine

22
Q

Histidine undergoes what type of deamination?
And is deaminated to ______

A

Non oxidative
Urocanate

23
Q

The ammonia produced in the brain and the muscles are trapped by ____ and _____ to form _____ and ______ before sending it to the liver?

A

Glutamic acid and asparic acid
Glutamine and asparagine
The glutamine is reversed back to glutamic acid in the liver by glutaminase

24
Q

Urea cycle is connected to the kreb cycle by_____ at ____ step?

A

Fumarate
@ step4

25
Q

______ ATP is consumed to form 1 molecule of urea?
And how many is produced?

A

4 ATP
2.5 ATP @ malate—oxaloacetate
NET = -1. 5 ATP

26
Q

What are the significance of urea cycle?

A

Detoxification of NH3
Disposal of waste products nh3 and biocarbonate
Regulation of pH
Bio synthesis of argenine

27
Q

What’s the difference between CPS1 AND CPS2?

A

Cps1– mitochondria, requires cofactor NAG, urea synthesis, no inhibitor, Ammonia-N- donor

Cps2– cytosol, doesn’t require cofactor, pyrimidine synthesis, CTP inhibitor, Glutamate-N-donor