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48 Cards in this Set
- Front
- Back
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proteins contain lots of _ |
nitrogen |
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Aa can be used for _ |
-protein synth -glucose synth -ketogen -synth of N containing stuff like nucleotides, neyroTs |
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Aa contain two thing |
alpha amino group (NH3) carbon skeleton |
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what happens to parts of Aa |
alpha amino grp gets extreted in urine as urea or NH4 C skeleton gets metabolized inot TCA cycle intermediate, or made into glucose |
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digestion of proetins happens where |
in stomach and small intestine |
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in stomach, theres __ which is protease that digest whole proteins into polypeps and invd Aa |
pepsin |
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complete digestion happens in _ of _ |
lumen of small intestine |
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trypsin is the master protease. it is synth as a __ known as __ which is inactive. once it comes into contact with __, then another protease known as __ cuts off portion converting it to trypsin. then trypsin cleaves __. |
zymogen known as trypsinogen. dietary proteins, enteropeptidase. trypsin cleaves series of other zymogens, activating them. |
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reason for this is |
want to keep them inactive until needed. |
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trypsin two main roles |
-cut peptide bond next to arginine and lysine, helps digest them -cleaves more small zymogens, activating them |
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so now they are all di-peps and tri-peps and indv __ |
Aa |
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now these can be __ into __ and released as __, where theyre carried to the __ by circulation |
absorbed into enterocytes, Aa into the bld stream. carried to liver. |
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c skeletons of Aa can be used to make (once nitrogen has been made into urea) |
glucose ketons or FA ATP (via TCA) |
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intracellular proteins are marked for degredations by __ |
ubiquitin proteasome system |
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first step is to attach sm protein called__ |
ubiquitin |
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ubiquinated proteins then sent to the _ for degradation |
proteasome |
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__complex binds to UB protein, __ them, threads a linear __ into the core of the complex |
-barrel-shaped -unfolds them -threads linear polypeptide thru proteolytic core |
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when leave proteasome, they are in form of __ |
small peptides |
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sm peptides degraded further into Aa by |
non specific proteases |
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this process is for __ proteins |
endogenous |
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proteasome pathway is active when ___ is low. bc Aa needed for _ |
when insulin is low bc Aa needed for gluconeogenesis |
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diets rich in protein stim enough __ to not degrade muscle |
stim enough insulin |
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Steps for Aa metabolism. Aa can come frmo __ or __ |
dietary proteins endogenous proteins |
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1) Removal of __ |
alpha amino grp (NH3) |
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can be done two ways: -transfer a amino grp to __ (catalyzed by __) -__ deamination (process where a amino grp directly cleaved off as NH3) |
-alpha keto acceptor (by aminotransferases) -oxidative deamination |
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after deamination, amino grp goes to __ and the C skeleton goes to __ for complete oxidation (fed state) or to __ (fasted state) |
-urea cycle for disposal. -TCA cycle, make glucose or make ketones |
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fate of Aa depends on |
whether in fasted or fed state. |
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Carbon skels of glucogenic Aa are used to make glucose during __. they enter cycle __ of __. |
gluceneogenesis. enter downstream of alpha ketoglutarate. |
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C skels of ketogenic Aa can ONLY be used to make ketones. its bc their C skels metabolize to __. in fasting state, most __ will be converted to ketones bc of lack of __ |
their C skels metabolize to acetyl-coA. acetyl coA gets turned into ketones in fasting state bc of lack of OAA. |
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in aminotransferase rn, the __ grp of one __ is transfered to __ of a __. makes new __ and new __. |
alpha amino grp of Aa transfered to alpha positino of an alpha-keto acid acceptor. makes new alpha keto acid, and new Aa. |
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enzyme used is |
aminotransferase |
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there are 12 dif __ in our bodies. each have dif. every Aa has corresponding __ |
aminotransferases. each has dif substrate. corresponding alpha-keto acid. |
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another word for carbon skeletons of Aa |
alpha-keto acids |
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all aminotransfer rns need __. all are __. |
need PLP (vit B6) are reversible. |
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after this, glutamate can get oxidatively deaminated by ___ to regenerate alpha-ketoglutarate and make __. This will enter urea cycle or be __. depends on what hepatocytes it happens in . |
glutamate dehydrogenase. makes NH4. goes to urea or incorp into glutamine, depends. |
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Glucose-Alanine cycle: way for __ |
muscles to makes glucose without brking down own proteins |
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muscle cells cant to __, rely on hepatocytes |
cant do gluconeogenesis |
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When needed, muscle proteins degreade to Aa. __grps transfered to __, makes glutamate. then __ tranfered to pyruvate to make __ (by ALT enz). |
alpha-amino grps transfer to alpha-ketoglutarate. then alpha-amino transfer to pyruvate. |
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alanine goes___ |
into blood to the liver |
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once in the liver, alpha-amino grp is ___ onto ___ makes pyrivate and glutamate (by ALT enz). Pyruvate gets __. the glutamate gets __, enters __. |
transfered back onto new molec of alpha-ketoglutarate. pyruvate to glucose thru normal gluceneogenesis. glutamate deaminated, NH4 does to urea cycle. |
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ALT enzyme is present in both __ cells. catalyzed opposite rns the cells types both during FASTING. |
muscle and liver. |
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its the __ and __ that are transported btwn muscle and liver. __ doesnt get transported, just exists in both tissues |
alanine and glucose. alpha keto glutarate doesnt get transported. |
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arginosuccinate to urea is catalyzed by |
arginine |
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2 sources of N in urea |
ammonia and aspartate (from AST rn) |
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stages where ATP used for urea cycle |
with carbamoyl synthetase 1 and when aspartate to arginosuccinate |
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where does ATP come from for urea cycle |
from FA oxidation )B ox) |
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aspartate from AST + ___ = ___ uses |
citrulline = arginosuccinate uses 1 ATP |
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if theres lots of E coming in , lots of acetyl coA, glutamate will accum. enzyme will link 2 together and make |
urea cycle go faster |
