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In Gamma-glutamyl Cycle how many atp's a
Terms in this set (20)
What are proteins in the PEST sequence?
-proteins with short 1/2 lives
- Proline, Glutamate, Serine and Threonine
Proteins with 1/2 lives over 100 hours?
Where are Pentapeptide KFERQ selectively lost or otherwise kept in response to fasting?
Lost- Liver and Kidney
Kept- Brain and Testis
Reaction with Ubiquitin is retarded by amino terminal residues?
Reaction with Ubiquitin is accelerated by amino terminal residues?
Pancreatic proteases include...
What are endopeptidases?
They are? Which is most specific?
- cleave peptide bonds at various points within protein chain
-Trypsin, pepsin, chymotrpsin and elastase
-Trypsin- cleaves lysine or arginine
Elastase cleaves elastin, but also what other small side chains?
What are exopeptidases?
- Cleave one amino acid at a timefrom the end chain.
-Carboxypeptidase and aminopeptidase
3 ways in which amino acids are absorbed from the intestinal lumen?
-through secondary active Na+ dependent transport
-through facilitated diffusion
-through transport linked to the gamma-glutamyl cycle.
In Gamma-glutamyl Cycle how many atp's are used?
The extracellular amino acid reacts with.....
What enzyme can accept both NAD+ and NADP+ ?
What are the similarities and differences in non-oxidative deamination of the enzymes Amino acid dehydrase and Amino acid desulfhydrase?
both require pyroxidal PO4 as cofactor, while
dehydrase acts on hydroxy amino acids- serine, threonine and tyrosine
Desulfhydrase- acts on sulfur containing cysteine, homocysteine
Which aa can't undergo transamination reactions?
Lysine and threonine
Carrier or coenzyme during transamination?
Aminotransferases mostly except??
a-ketoglutarate (lesser extent oxaloacetate)
uses ammonia as its nitrogen donor, very dependent on N-AGA
uses glutamine, cytosolic in location, no n aga
Which process releases urea and regenerates ornithine?
Clevage of arginine by arginase
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