1404 Renal Biochem

Question 1

What is anabolism?

Answer 1

Making of large molecules,requires energy

Question 2

What is catabolism?

Answer 2

Break down of large molecules,releases energy

Question 3

What is metabolism

Answer 3

Anabolism and catabolism

Question 4

What is de novo/ endogenous?

Answer 4

Can make in house,so not essential

Question 5

What are the non essential amino acids?

Answer 5

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Alanine
Asparagine
Glutamate
Glutamine
Cysteine
Asparate
Glycine
Tyrosine
Proline
Serine

Question 6

Which amino acids are nonessential (produced by the body) but are still classified as essential

Answer 6

Arginine
Methionine
Phenylalanine

Question 7

Why is Arginine like this?

Answer 7

Arginine is synthesized by mammalian tissue but the rate is not sufficient to meet the required amount during growth

Question 8

Why is methionine like this?

Answer 8

Methionine is required in large amounts to produce cysteine

Question 9

Why is phenylalanine like this

Answer 9

Phenylalanine is needed in larger amnts to form tyrosine

Question 10

Where are amino acid precursors present?

Answer 10

Amino acid precursors are intermediates in glycolysis, TCA,Kreisler Cycle,Citric Acid Cycle and PPP

Question 11

What is transamination?

Answer 11

Transamination is the transfer of NH2 group between amino acid and a keto acid via a transaminase
Eg. Pyridoxal Phosphate

Question 12

What is amination?

Answer 12

Transfer of NH2 groups between AAs using ATP and synthesizing enzymes

Question 13

Why is arginine only essential to infants

Answer 13

Arginine is only essential to infants because of higher growth requirements

Question 14

How do adults synthesize arginine

Answer 14

Adults synthesize arginine from glutamate

Question 15

What is glutamate used to produced

Answer 15

Glutamate is used to produce proline

Question 16

What is glutamate used to produce

Answer 16

Glutamate is used to produce arginine and prolime

Question 17

How is serine produced?

Answer 17

3-physphoglycerate is oxidized to a ketoacid intermediate
Glutamate donates an amine group to form serine precursor
Phosphate removed from serine precursor to produce serine

Question 18

How is glycine produced?

Answer 18

Glycine is produced by removing an R group from serine
Serine - R Group —> Glycine

Question 19

How is cysteine produced?

Answer 19

Cysteine is synthesized by bacteria without the need for methionine

Question 20

How is cysteine also produced?

Answer 20

Methionine converted to homocysteine
Homocysteine then converted to cysteine

Question 21

How is tyrosine formed?

Answer 21

Tyrosine is formed by hydroxylating phenylalanine.Phe Catabolism

Tyrosine important for production of enzymes,hormones,melanin,E,NE,dopa.

Question 22

What is Garrods Hypothesis

Answer 22

Errors of amino acids are genetic disorders
Formed by mutations in gene coding enzyme
Symptoms results from too little AA production,toxic accumulation of intermediates or formation of alternative metabolites.

Question 23

What are the inborn errors associated with non essential amino acids

Answer 23

Alkaptonuria- Tyrosine

Question 24

What inborn errors are associated with essential amino acids?

Answer 24

Phenylketouria
Histindinemia(Histidine)

Question 25

What enzyme is mutuated in PKU

Answer 25

The enzyme phenylalanine hydroxylase is mutated in PKU

Question 26

What happens to excess Phe?

Answer 26

Excess Phe is shafted to other pathways where it is converted to other metabolites

Question 27

What are the symptoms of PKU

Answer 27

Reduced synthesis of neurotransmitters Sever neural degradation Mental retardation Albinism Musty odor in breath urine and skin

Question 28

What is albinism caused by?

Answer 28

Albinism is caused by a tyrosine deficiency

Question 29

How is tyrosine formed

Answer 29

Tyrosine is formed from phenylalanine via the enzyme phenylalanine hydroxlase Phenylalanine—>Tyrosine

Question 30

What are the treatments for PKU?

Answer 30

Tyrosine Supplements Limited Restriction of Phe Gene Theraphy Screening- pregnant women

Question 31

What enzyme is mutated in the disease Alkaptonuria?

Answer 31

Homogentisate oxidase is mutated in alkaptonuria

Question 32

What is the role of homogentisate oxidase?

Answer 32

This enzyme is involved in the Phe/Tyr catabolic pathway

Question 33

What is the effect of this mutation of homogentisate oxidase in Alkaptonuria?

Answer 33

Phe/Tyr not properly broken down and metabolites accumulate to toxic levels Homogentisate/homogentisic acid accumulates in blood and tissues causing damage to heart valves Accumulation in joints cause osteoarthritis

Question 34

What is ochronosis?

Answer 34

Excess homogentisate is converted to benzoquinone acid which is similar to melanin,giving tissues a dark colour

Question 35

Is homogentisate excreted ?

Answer 35

Homogentisate and its oxidized form alkapton are excreted in urine Urine becomes dark in color Even though excreted, levels of homogentisate in the body remain high

Question 36

What are the treatments for alkaptonuria?

Answer 36

Nitisinone Anti inflammatory Physical therapy Manage Phe and Tyr intake

Question 37

How does nitisinone treat alkaptonuria?

Answer 37

Nitsinone reduces the level of homogentisic acid in the body

Question 38

What causes hyperthyroidism

Answer 38

Hyperthyroidism is caused by an accumulation of tyrosine Increased metabolism and HR

Question 39

What is the cause of hypothyroidism?

Answer 39

Hypothyroidism is caused by a tyrosine deficiency Slow metabolism and weight gain

Question 40

`what is the importance of histidine and histamine?

Answer 40

Hisitidine and histamine is important for rodents and human infants

Question 41

What is the role of THF

Answer 41

THF is an important cofactor for proper functioning of FTCD enzyme Folic acid deficiency can lead to Histidinemia THF needed for purine and Pyrimidines synthesis

Question 42

What are the treatments for Histidinemia?

Answer 42

Genetic screening Low Histidine diet Enzyme replacement therapy