Dai 1

Question 0

Nonpolar amino acids. List.

Answer 0

On an Isolated Tryp to Alabama, Valerie and Lucy Met michael Phelps. glycine proline.

Question 1

Charged polar amino acids. List.

Answer 1

His Asp Lys in Glu, Arg!

Question 2

Uncharged polar amino acids.

Answer 2

Ser Thr Tyr Asn Gln Cys

Question 3

Nonessential amino acids, from glucose.

Answer 3

Alanine, Aspartate, Asparagine, Arginine
Glycine Glutamate, Glutamine,
Serine Proline (sugary prose-r)

Question 4

Essential aa in diet.

Answer 4

PVT TIM HALL

Question 5

Nonessential aa, from essential.

Answer 5

Tyr (from Phe)

Cys (from Met)

Question 6

What has a biological value of 100?

Answer 6

Egg, as all essential aa.

Question 7

90% of N excreted in _____ form.

Answer 7

Urea.

Question 8

T or F. Like carbs and lipids, Nitrogen is stored in our bodies.

Answer 8

F. AA meets our biosynthetic needs, rest metabolized.

Question 9

T or F. Positive N balance is needed for growth, lactation, recovery from emaciating illness.

Answer 9

True.

Question 10

What is kwashiorkor?

Answer 10

normal calories but inadequate protein uptake. defective growth and muscle wasting. labs show low plasma protein

Question 11

What is oncotic pressure?

Answer 11

osmotic pressure that proteins have in blood plasma, puts water in circulatory system.

Question 12

Digestion of protein is divided into 3 stages. Name the stages, and some enzymes found in each stage.

Answer 12

Gastric: pepsin and HCL (stomach acid)
Pancreatic: trypsin, chymotrypsin, elastase
Intestinal: aminopeptidases.

Question 13

Pepsin have specific cleavage activity for the ____ and _____ amino acids.

Answer 13

aromatic and acidic.

Question 14

Trypsin cleaves the ____ amino acids.

Answer 14

basic.

Question 15

Chyotrypsin cleaves the _____ and _____ amino acids.

Answer 15

aromatic, and hydrophobic.

Question 16

Elastase cleaves the _____ aa.

Answer 16

small. ala, gly, ser

Question 17

What are zymogens?

Answer 17

inactive enzyme precursors.

Question 18

T or F. Since concentration of aa in lumen is low, aa enters epithelial cells via active transport and NA-aa symport activity.

Answer 18

True.

Question 19

T or F. The basolateral membrane is impermeable to large polar amino acids and can’t passively diffuse.

Answer 19

F, basolateral leaky.

Question 20

What is cystinuria.

Answer 20

defective aa transporter. failure to reabsorb cystine into kidney, leads to kidney, urinary tract, and bladder stones,

Question 21

What is Hartnup disease?

Answer 21

Failure of aa transporter in renal, intestine. results in excretion of neutral aa like trypto into urine. leads to rash headache psych probs. treated by trypto diets. niacin.

Question 22

-uria means

Answer 22

elevated in urine

Question 23

-emia means

Answer 23

elevated in blood

Question 24

In N disposal, alpha amino groups are collected in glutamate via _________, released as NH4 via __________ and converted to urea by ________.

Answer 24

transamination of a ketoglutarate. oxidative deamination by NAD Urea cycle.

Question 25

The following amino acids can lose amino group via transamination. What do each become after transamination? alanine aspartate glutamate

Answer 25

alanine to pyruvate aspartate to OAA glutamate to a ketoglutarate

Question 26

What is the cofactor of aminotransferases?

Answer 26

PLP, pyridoxal phosphate, derivative of vit B6

Question 27

Alanine aminotransferase (ALT) and Asp aminotransferases (AST) levels in plasma is a monitor for ____

Answer 27

liver damage.

Question 28

oxidative deamination of glutamate is by what enzyme?

Answer 28

Glutamate dehydrogenase.

Question 29

How is oxidative deamination regulated?

Answer 29

High NAD activates glutamate dehydrogenase (energy deficiency) GTP allosteric inhibts glu dehydrogenase ADP allosteric activate glu dehdyrogenase.

Question 30

Why is high ammonia toxic?

Answer 30

high NH4, reverses oxidative deamination, lose ATP, energy, depletes a ketoglutarate. CNS defects (glutamate neurotransmitter)

Question 31

What are the urea cycle steps in mitochondria

Answer 31

NH3-CO2 to carbomoyl phosphate via carbamoyl phosphate synthetase (requires 2 ATP) L ornithine to L citrulline via ornitihine transcarbamoylase (requires carbamoy phosphate).

Question 32

Citrulline + aspartate --> arginosuccinate via

Answer 32

arginosuccinate synthetase (requires ATP).

Question 33

Arginosuccinate --> Arginine and fumarate --> L ornithine + Urea

Answer 33

arginosuccinate lyase. | arginase

Question 34

What are the 2 sources of N in the Urea cycle.

Answer 34

ammonia, aspartate.

Question 35

What is the rate limiting step in urea cycle?

Answer 35

CPS1 carbamoyl phosphate production

Question 36

what is a mandatory allosteric cofactor of cps1

Answer 36

Nag n acetyl glu

Question 37

Deficiency in urea cycle is usually a deficiency in enzyme ______ but can sometimes be deficiency in enzyme_______.

Answer 37

OTC. | CPS1/NAGsynthase.

Question 38

OTC deficiency leads to builup of _____, which can feed into CPS2 to become ______

Answer 38

Carbamoyl P, orotic acid/uracil