KIN 217 - AA degradation and urea cycle

protein turnover

the constant synthesis/degradation of protein, where you cannot store excess amino acids which gets degraded

aminotransferases / transaminases

_____________________ transfers amine groups from an amino acid to alpha-ketoglutarate making glutamate

oxaloacetate and glutamate

aspartate transaminase uses aspartate and alpha-ketoglutarate to make

pyruvate and glutamate

alanine transaminase uses alanine and alpha-ketoglutarate to make

NH4+

glutamate dehydrogenase ca oxidatively deaminate glutamine to release

dehydratase

some amino acids can be directly deaminated using a _____________

true

muscles can export nitrogen from branched chain amino acids for the liver to process

t or f

alanine

the amine group is transferred to pyruvate to make __________

glutamine

amine group transfers to glutamate to make ________

CAC intermediates

carbons of branched chain amino acid is used for energy in mucles forming

liver

alanine is transferred to the ________ by bloodstream

urea cycle

amine is moved from alanine to glutamate for the ________

liver damage

blood levels of aminotransferases serves a diagnostic function of

alanine and aspartate

what exactly is measured in aminotransferase in blood

terrestrial vertebrates

urea production is in ____________

urea

excess NH4+ is converted to ________

liver

urea production occurs in the _______ for humans

volatile, basic

ammonia is small and mobile, ______ and ______

NH4+

ammonia accepts proton to become ____ which increases pH impacting metabolism

true

urea is soluble in water neutral and non toxic

t or f

aspartate, ammonia

urea has 2 nitrogen atoms 1 from _____________ and 1 from _______________

mitochondria matrix

nitrogen atom from ammonia will make carbamoyl phosphate in the

bicarbonate

step 1 of the urea cycle is coupling ammonia with ___________

carbamoyl phosphate synthetase (CPS I)

the coupling of ammonia with bicarbonate is catalyzed by ________________________

2

carbamoyl phosphate synthetase (CPS I) requires ___ ATP

carbamoyl phosphate synthetase

what is the key regulatory enzyme to the urea cycle

N-acetylglutamate

_______________________ is an allosteric activator of carbamoyl phosphate synthetase (CPS I)

amino acids

N-acetylglutamate is formed from acetyl CoA and glutamate, which occurs when there are excess ____________

ornithine

step 2 of the urea cycle has the carbamoyl group transferred to ____________

citrulline

ornithine uses ornithine transcarbamolyase to make __________ in step 2 of urea cycle

ornithine

step 2 of urea cycle citrulline is transported out of the mito. into the cytoplasm in exchange for __________

cytoplasm

step 3 of the urea cycle occurs in the

aspartate

step 3 citrulline condenses with ________ to make the 2nd nitrogen of urea

argininosuccinate

the 3rds step of urea cycle _______________ is formed where ATP to AMP and PPI driving the rxn

argininosuccinate synthetase

the formation of argininosuccinate uses the enzyme ___________________

arginine, fumarate

step 4 of the urea cycle involves argininosuccinate cleaved by argininosuccinase to make _______________ and ______________

fumarate

in step 4, which molecule leave the urea cycle

arginase

step 5 of the urea cycle involves arginine cleaved by _____________

H2O

arginase uses ________ molecule to make urea and ornithine

carbamoyl phosphate

ornithine is transported into the mitochondria to restart the cycle after receiving _______________

fumarate

which molecule links CAC with the urea cycle

true

fumarate can turn to oxaloactetate for CAC

t or f

aspartate

oxaloacetate from CAC can be transaminated into______________ for the 2nd nitrogen of urea

ketogenic amino acids

these amino acids are metabolized to acetyl Coa and acetoacetyl and can form fats only, no glucose

lysine, leucine

what amino acids are purely ketogenic

gluconeogenic amino acids

these amino acids degrade into pyruvate or CAC intermediates for glucose production

threonine

this amino acid have carbon structures that can be metabolized by either route

tryptophan, phenylalanine, tyrosine

these amino acids have large carbon structures that provides parts to both routes

alanine

this amino acid turn to pyruvate after transamination

aspartate

this amino acid turns to oxaloacetate after transamination

glutamate

this amino acid turns to alpha-ketoglutarate after transamination

3, 3

additional steps are needed to process other amino acids to carbon skeletal entry points, pyruvate needs ____ carbon amino acids and ___ carbon pieces

4

additional steps are needed to process other amino acids to carbon skeletal entry points, oxaloacetate needs ___ carbon amino acids

5, 5

additional steps are needed to process other amino acids to carbon skeletal entry points, alpha-ketoglutarate needs ___ carbon amino acids and ____ carbon pieces

non-polar amino acids

additional steps are needed to process other amino acids to carbon skeletal entry points, succinyl CoA needs ____________

branched chains AA, aromatic AA pieces

additional steps are needed to process other amino acids to carbon skeletal entry points, acetyl CoA and acetoacetate needs _______________, and ________________

aspartate (from urea cycle), phenylalanine/tyrosine pieces

additional steps are needed to process other amino acids to carbon skeletal entry points, fumarate needs _________ and ____________________

PKU / phenyketonuria

one of the first links b/w genetic mutation, biochemical errors and pathology, involving a genetic mutation resulting in a non-functional phenylalanine hydroxylase

Phe

PKU causes ____ to be unable to degrade properly, buulding up in tissues and blood

true

Phe build up causing a disruption in brain growth and metabolism

t or f

phenylpyruvate

______________ would be excreted in urine if Phe builds up to help metabolize by removing amine group

genetic screening for low Phe diet

how do we treat PKU