Amino Acids Flashcards
(21 cards)
Gluconeogenic amino acid examples
Ala, Arg, Asn, Asp, Cys, Glu, Gln, Gly, His, Pro, Ser, Met, Val
Glucogenic/ketogenic aa examples
isoleucine, phenylalanine, tyrosine, tryptophan
Ketogenic aa examples
leucine, lysine
types of essential aa
glucogenic, ketogenic, glucogenic/ketogenic
acidic amino acids
aspartic acid, glutamic acid
- negatively charged at body pH
basic aa
arginine (most basic), lysine, histidine
- Histidine has no charge at body pH
which form of amino acids found in proteins
L-form
Sulfer-containing amino acids
methionine, cysteine
conditionally essential amino acids
can be made by body, but the capacity for their synthesis is limited and in high states of consumption (i.e. critical illness) deficiency may develop
amino acids with nitrogen side chain
Glutamine, asparagine, lysine, histidine, arginine
branched amino acids
Valine, isoleucine, leucine
aromatic amino acids
tryptophan, tyrosine, phenylalanine
glucogenic amino acids
used as substrates for gluconeogenesis
ketogenic aa
when broken down, these generate Acetyl CoA and can’t participate in gluconeogenesis but produce ATP through TCA or be used for ketone synthesis
Post-translationally modified amino acids
hydroxy-proline, hydroxy lysine, gamma carboxyglutamate, ornithine
Intracellular pathways for protein degradation
ubiquination, degradation in lysosomes
Ubiquination
targets proteins for degradation in the proteasome
transamination
- normally in liver (less in kidney, intestine, muscle), bidirectional
- NH2 removed from amino acid
- NH2 added to carbon skeleton
- NH2 transferred from nitrogen molecule to carbon skeleton or from amino acid to acceptor molecule
Transamination reaction
NH2 from amino acid to alpha-ketoglutarate –>alanine – go to liver –> glutamate –> urea
key regulated step in protein metabolism
NH3+CO2–> Carbamoyl phosphate via carbamoyl phosphate synthase; requires N-acetylglutamate as a cofactor
how does ammonia
?
