Chapter 8 ( Amino Acids , Proteins And Enzymes ) Flashcards

1
Q

Hydrophobic amino acids ?

A
Phenylalanine 
Tyrosine 
Tryptophan
Alanine 
Valine
Leucine
Isoleucine 
Proline
Methionine
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2
Q

Hydrophilic amino acids ?

A
Aspartic acid
Glutamic acid 
Lysine
Arginine
Histidine 
Serine
Threonine 
Asparagine 
Cysteine
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3
Q

Sulfur containing amino acids ?

A

Cysteine

Methionine

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4
Q

Branched chain Amino acids that their metabolism are abnormal in maple syrup urine disease ?

A

Valine
Leucine
Isoleucine

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5
Q

Protein break down cellular sites ?

A

Lysosomes by lysosomal proteases which digest endocytosed proteins
Proteasomes ( large cytoplasmic complexes ) which digest older or abnormal proteins that covalently tagged with Ubiquitin for destruction

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6
Q

Essential amino acids ?

A
PVT TIM HALL
Phenylalanine
Valine
Threonine 
Tryptophan 
Isoleucine 
Methionine 
Histidine 
Arginine ( only during positive nitrogen balance )
Leucine 
Lysine
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7
Q

Diet for PKU patient ?

A

Diet with restricted Phenylalanine and rich in Tyrosine

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8
Q

Negative nitrogen balance examples ?

A
Protein malnutrition 
Dietary deficiency of even 1 amino acid 
Starvation 
Uncontrolled diabetes 
Infection
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9
Q

Positive nitrogen balance examples ?

A

Growth
Pregnancy
Convalescence
Recovery from condition associated with negative nitrogen balance

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10
Q

Why Arginine is an essential amino acid during positive nitrogen balance conditions ?

A

As the urea cycle can’t make enough arginine needed for histone synthesis which in turn is needed for DNA synthesis

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11
Q

First order kinetics ?

A

The more substrate proportionally the more product is going to be made

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12
Q

0 order kinetics ?

A

Whatever increase in the substrate, the product is still the same as we reached the enzyme limiting capacity (Vmax)

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13
Q

Michaelis- Menten Equation ?

A

Describes how the rate of the reaction depends on the concentration of both the enzyme and the substrate which forma the product

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14
Q

Lineweaver-Burk equation ?

A

A reciprocal form of the Michaelis-Menten equation

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15
Q

Examples for competitive inhibitors ?

A

1- the Statin drugs ( lovastatin, simvastatin ) competitively inhibit HMG CoA reductase in cholesterol biosynthesis to control blood cholesterol
2- Methotrexate competitively inhibits dihydrofolate reductase depriving the cell of active folate needed for purine and deoxythymidine synthesis thus interfering with DNA replication during S phase
3- Oseltamivir which competitively inhibits influenza neuraminidase

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16
Q

Examples for noncompetitive inhibitors ?

A

1- Allopurinol which noncompetitvely inhibits xanthine oxidase
2- Aspirin which noncompetitvely inhibits cyclooxygenase

17
Q

Example for enzyme showing cooperative kinetics ( Allosteric kinetics ) ?

A

Phosphofructokinase-1 (PFK-1) in glycolysis

18
Q

Examples for inhibitors and activators of enzymes that show Allosteric kinetics ?

A

AMP
ATP
Citrate
Fructose-2,6-bisphosphate (F2,6-BP)