2.10-AA Catabolism Flashcards Preview

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Flashcards in 2.10-AA Catabolism Deck (16):
1

In the MAIN reaction: what enzyme do we use to get the amino group from an AA to an Alpha-KetoGlutarate? Whats the COenyme?!

AminoTransferase...Coenzyme:Pyridoxal Phosphate

2

What receives our amino group in step 1?

Glutamate!

3

Which AminoTransferase is the RULE?

ALT-Alanine AminoTransferase

4

Which aminotransferase is the EXECPTION?

AST-Aspartate AminoTransferase

5

What is the result of step 2 to free our ammonia? What it is freed from? What molecules inhibit? Activate?

Glutamate gives up its amnio group. ATP/GTP inhibit, GDP/ADP activate (it produces NADPH!)

6

What is the KEY reaction of the Urea cycle? Where is it happening? HOW MUCH ATP used? ENZYME?

FORMATION of CARBAMOYL Phosphate IN the Mitochondira.2 ATP used. Carbamoyl Phosphate Synthase I (CPS 1)

7

What links the Urea cycle with GNG?

Fumarate

8

What is the enzyme made by bacteria that cleaves urea?

Urease

9

What molecule do we use to safely transport ammonia? Enzyme involved?

Glutamine. Catalyzed by Glutaminase

10

Which cycle is reminiscent of the core cycle that transports amino groups from muscle to liver?

Glucose-Alanine Cycle

11

What are the two main ammonia donors?

Glutamate or Aspartate

12

What is argininosuccinate cleaved into (2 products)?

Arginine and fumarate

13

What is arginine cleaved to make (2 products)?

Orn-thi-ne and Urea

14

What it the non toxic transporter of ammonia?

Glutamine (not glutamate) (glutamate gets converted TO glutamine for the ammonia transport)

15

How is alanine formed?

transamination of glutamate to pyruvate

16

Why is ammonia bad for you? MAIN POINT

depletes alpha-ketoglutarate