amino acid biosynthesis Flashcards
how many amino acids can we produce (non-essential)
10
list the 10 non-essential amino acids
alanine, glutamate, glutamine, proline, arginine, serine, glycine, cysteine, aspartate, asparagine
list 3 ways in which amino acids are derived
glycolysis intermediates, CAC intermediates, PPP intermediates
describe how amino acids can be derived from the PPP
Glucose-6-P can be converted to metabolites by donating electrons to NADP+, producing lots of NADPH
what do aminotransferases do
move amino groups from one molecule to another
what is the name of the leftover molecule when an aminotransferase removes it’s amino group
carbon skeleton
which amino group was removed to create a carbon skeleton: backbone or R group
backbone (because not every a.a has an R group amine)
what is another name (the chemical name) for an amino acid minus its R group
a-keto acid
last class we saw that a-KG can make glutamate which can then make glutamine. List the other two derivatives of glutamate (aka a-KG derivatives)
proline and arginine
describe how proline is made from glutamate
glutamate is reduced by dehydrogenase and NADPH, The resulting molecule is spontaneously (non-enzymatically) cyclized. A final NADPH reduction = proline
to make proline: what enzyme is used
glutamate dehydrogenase
to make proline: ATP cost?
1 ATP
to make proline: NADPH cost?
uses 2 NADPH
describe how you make arginine from glutamate
reduce glutamate with NADPH. Aminotransferase introduces a second amino group, leaving glutamate as a-KG. Resulting molecule = ornithine, which enters the urea cycle to form arginine
to make arginine: enzymes used?
aminotransferase
to make arginine: ATP cost?
2 ATP
to make arginine: NADPH cost?
1 NADPH used
to make arginine: what intermediate is produced
ornithine
to make arginine: what happens to ornithine during the pathway
it enters the urea cycle to eventually form arginine
how many amino groups does arginine have
4
how many amino groups does urea have
2
what amino acid is produced from 3-phosphoglycerate? what amino acids does that produce?
serine, which makes glycine and cysteine
describe how we make serine from 3-phosphoglycerate
3-PG is oxidized by NAD+. Aminotransferase adds an amino group. Phosphatase removes the phosphate
to make serine: enzymes used?
aminotransferase and phosphatase
to make serine: ATP cost?
none
to make serine: byproducts? (ie are the electron carriers oxidized or reduced)
NAD+ is used, NADH is produced
describe how glycine is produced from serine
hydroxymethyltransferase removed OH and methyl group from serine
to make glycine: enzymes used?
hydroxymethyltransferase
to make glycine: ATP cost?
none
to make glycine: and electron carriers?
none
describe how to make cysteine from serine
plants uptake sulfates (SO4 2-) from the soil which are reduced by NADPH to sulfide (S2-). The sulfide is exchanged for the serine OH
to make cysteine: enzymes used?
none that are mentioned (S is replaced with OH)
to make cysteine: ATP cost?
none
to make cysteine: electron carriers?
NADPH used
which amino acid does OAA make
aspartate
which amino acid does aspartate make (that we can synthesize)
asparagine
which amino acid does pyruvate make (that we can synthesize)
alanine
describe how alanine is made from pyruvate
pyruvate is transaminated via aminotransferase