unit 8 protein metbolism HW

Carbs are natures favorite

circulating fuel

lipids are natures favorite

storage fuel

protein are natures favorite

building blocks

circulation for carbs

easy b/c they’re very hydrophilic

circulation for lipids means

complex w/ proteons (very hydrophilic)

protein circulation means

hydrophilic, 1st pass after eating

carbohydrate reserves

glycogen (liver/SM) ~12 hrs

lipid reserves

adipose (limitless)

protein reserves

unintentional reserves (in kidney/liver)

proteins are consumed for

10 essential amino acids

3 instances where substrate cycle between amino acid anabolism and protein catabolism can serve a useful purpose

1. elimination of malfunctioninf proteins

2. metabolic regulation of enzymes via AVAILABILITY

3. reserve when needed (fasting)

KFERQ tag

selective trafficking to lysozome (liver/kidney atrophy; uterine regression)

PEST protein

S/T phosphate sites more likely to get ubiquitin tag

ubiquitin tag

Lys residues are tagged w/ ubiquitin “death tag” protein; trafficked to proteasome for protease degradation

regulatory protein functions

turns on/off (present/absent) in response to cellular needs

housekeeping functions of proteins

basic functions that are always there (standards for exponential methods since these levels don’t tend to change w/ environment)

OAA aa counterpart

Asp

alpha keto glutarate aa counterpart

Glu

how to create alpha keto acids from aa

transamination

ammonia is in

fish

uric acid is in

birds/reptiles

urea is in

mammals

recipe for urea

HCO3- + H2N (from Asp in urea cycle) + H2N (from Glu via oxidative deamination)

what is 5 mM essential for

RBCs, Brain

what is SAMe

Alanine w/ methionine attached

SAMe function

biological methyl dimer (adds -CH3 to 40 rxns)

methionine cycle

methionine → SAMe → S-adenoxyl homocysteine → homocysteine → methionine

two things needed for 5’ methyl folate?

Vitamin B9 and functioning MTHFR

metabolic disorder PKU

lacks PAH, can’t convert phenylalanine into tyrosine

PAH stands for

phenylalaninehydroxylase

tyrosine affects

melanine (low Y = hypopigmentation) & dopamine and epinephrine levels

what does LNAA do to the blood brain barrier

saturates blood brain barrier, low LNAA = decreased neurotransmitters

essential aas

body cannot make them, must consume in diets

non-essential aas

we can make these aas ourselves

recipe for making amino non-essential acids

alpha keto acid skeleton → aa (via transamination, where glu becomes a-kg)

umami

taste for glu

recipe for heme

C (from succinyl-Coa [TCA]) & N (from glycine)

where is heme synthesized

RBC (Hb for O2 transport), liver (cytochromes P450 for detox), others (cytochrome c for ETC)

heme degradation pathway

heme (red) → biliverdin (green) → bilirubin (yellow) → excrete in urine/feces

NO and its biochemical and physiological functions

has a free radical (produced from Arg)

1. rasodilator

2. CNS component (cell signaling)

3. potent cytotoxin

nitrogen cycle

N2 → NH3 → NO- → NO3-

N2 fixing enzyme

nitrogenase