3.4 proyein catabolism

Question 1

what happens to excess amino acids?

Answer 1

they serve as metabolic fuels because they can be converted to glucose acetyl-CoA and ketone bodies

Question 2

trypsin

Answer 2

found in bovine pancreas
highly specific
polar charged residues like arginine and lysine but not proline

Question 3

chymotrypsin

Answer 3

deals with more bulky hydrophobic groups like phen, trp, tyr, BUT NOT PRO
slowly works for asparginine, his, met, leu

Question 4

elastase

Answer 4

small neutral residues like ala, gly, ser, val BUT NOT PRO

Question 5

turn over

Answer 5

proteins have half lives so when they are no longer needed they are degraded into amino acids

ex: transcription has high turnover

Question 6

indogenous

Answer 6

you already had these kind of proteins already inside of you

Question 7

exogenous

Answer 7

you have to digest these proteins which come from food and they are digestive proteins

they are first line when needing to get amino acids

Question 8

absorbable

Answer 8

means when u uptake it, it will break down

Question 9

unabsorbable

Answer 9

means that when you ingest these types, it will not be digested such as fiber, sugar, and bacteria are not absorbed through blood and goes through waste for the most part…

Question 10

glucogenic amino acids

Answer 10

amino acids broken down into glucose precursors like pyruvate , alpha keto glutarate, succinal coA, fumarate, cell respire etc.

13 amino acids are glucogenic

Question 11

Ketogenic

Answer 11

KL amino acids (lysine and leucine)

ketogenic precursor amino acids such as acetyl-coA and acetoacetate

Question 12

what are the five amino acids that are both ketogenic and glucogenic

Answer 12

WIFTY

tryp
isoleucine
phenal
threonine
tyro

Question 13

what are the two mechanisms for amino acid degradation?

Answer 13

transamination (occurs in all cells)
deamination (occurs mostly in liver)

ammonium is used more than ammonia and bc it has to be protonated because the basic nh3 is higher than the normal blood ph of 7.4

Question 14

transamination process

Answer 14

NH2 group of an amino acid (the donor) is transferred to an alpha-keto acid (the acceptor)—the most common alpha-keto acid acceptor is alpha-ketoglutarate

occurs in the cytoplasm

Question 15

how to generate alpha keto glutarate when you have glutarate

Answer 15

aspartate aminotransferase, producing aspartate as a by-product (particularly in liver cells)—or the reaction may proceed in the reverse direction producing oxaloacetate (usually enters gluconeogenesis)

Question 16

alanine aminotransferase

Answer 16

Catalyzed by alanine aminotransferase, the transfer of –NH2 group of glutamate to pyruvate generates α-ketoglutarate and alanine (transporter) for nitrogen carrier btwn peripheral tissues and liver

reversible

Question 17

glutamate to glutamine

Answer 17

glutamate—the end-product resulting from the transamination of most amino acids—can also be converted to glutamine through condensation with NH4+ by glutamine synthetase,

glutamine is nitrogen carrier
pseudo transamination bc it delivers the glutamine (itself) directly

Question 18

what kind of acid is in peripheral tissues??

Answer 18

glutamate as products

if as reactant, than going to liver

Question 19

what does it means if amino acid during deaminase is direct?

Answer 19

does not to be converted to glutarate

Question 20

ex of direct amino acids

Answer 20

serine, threonine, glutamine,