Stuff
Things
Whatever
Matters
Concerns
100
Run, Protein, Run!!! Once this covalently binds to you, your next stop is degradation by the proteasome.

What is ubiquitin?

100

You had one main job to do: excrete the toxic ammonia out of the body.

What is the main role of the urea cycle?

100

Dr. Veenstra, as far as livers go, yours looks great!!!! The test for this transaminase came back within range. I would still cut down on the apple fritters, though.

What is alanine aminotransferase (ALT)?

100

The 19S subunit of the proteasome works hard, but it won't do that.

What is digest ubiquitinated proteins into amino acid fragments?

100

Large double double coffee

What does Dr. Veenstra order at Tim Hortons?

200

I can't cut up protein yet, but wait until I am activated!!!!

What is a zymogen?

200

Get them in your diet or from the degradation of cellular proteins: those are your two main options of obtaining this class of biomolecules?

What are the two major sources of amino acids?

200

I made these two molecules by deaminating glutamate using the enzyme glutamate dehydrogenase.

What are alpha-ketoglutarate and NH4+? 

200

In most individuals it is equal.

How does the amount of endogenous protein that humans produce each day compare to the amount that humans consume in their diet?

200

This region of the proteasome is where proteins go to get chopped up into smaller peptides.

What is the 20S subunit?

300
This form of nitrogen removed from amino acids cannot be reabsorbed by the kidney tubules.

What is NH4+?

300

Need to make glutamate and oxaloacetate via a transamination reaction? I suggest starting with these two molecules.

What are aspartate and alpha-ketoglutarate?

300

These two molecules are on an exchange program in the urea cycle and meet as they pass each other crossing the mitochondrial membrane.

What are ornithine and citrulline?

300

Glutamate's nitrogen group can enter the urea cycle in either of these two forms.

What are attached to aspartic acid or as NH4+?

300

Here I am, anchored into the membrane of the brush border cells of the small intestine waiting to cut trypsinogen into trypsin.

Who is enterokinase?

400

The major driver that regulates the urea cycle.

What is the amount of ammonia present in the body?

400

If you are trying to convert amino acids and keto acids to other amino acids and keto acids in a transamination reaction, you better have plenty of this cofactor.

What is pyridoxal-5'-phosphate?

400

I am sorry if preparing for this exam is putting you in a state that is resulting in a negative nitrogen balance.

What is stress?

400

They get sent to the liver and are converted to glucose and triglycerides.

What happens to excess proteins that are not used for growth or enzymatic reactions in the body?

400

Energy levels are low and AMP levels are high in the cell. Looks like mTOR is inactive. It looks like this is going to be active, however.

What is autophagy?

500
Zymogens that are converted to their active forms by trypsin.

What are trypsinogen, chymotrypsinogen, proelastase, and procarboxypeptidase?

500

This X-linked condition, which results in hyperammonemia, generally results in more severe symptoms in males than females.

What is ornithine transcarbamylase (OTC) deficiency? 

500

The primary purpose of the Glucose-Alanine Cycle.

What is to send alanine to the liver so it can be converted to pyruvate (to produce glucose) and nitrogen (for the urea cycle)?

500

Wow, did someone just go to 5 Guys or needs to go to 5 Guys!!!!  Something is causing the transcription and synthesis of all 5 enzymes of the urea cycle to be increased. 

What is increased amino acid catabolism?  (Hint: it occurs after eating a meal high in protein or during fasting)

500

Need to move amino acids from the lumen of the small intestine into the enterocytes? I would use this method.

What is secondary active Na+-dependent transport?