BCH4024 Exam 2 Questions And Answers
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Primary metabolites - Answer✔needed for normal operation of metabolic pathways and main
cellular functions
ex: aa's, nucleotides, RNA, DNA, B vitamins
Secondary metabolites - Answer✔organic compounds NOT needed for cell growth,
development, or reproduction
typically for pathogens and predaotrs
or prevent against osmotic damage
helpful for treating many illnesses
Alkaloids - Answer✔plant-derived nitrogen-containing secondary metabolites
Common alkaloids we should know: - Answer✔caffeine (stimulant)
morphine (analgesic)
taxol (anticancer)
LSD (psychedelic)
Fungal metabolites we should know: - Answer✔Penicillin (antibiotic)
Streptomycin (antibiotic)
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Cyclosporin (immunosuppressant for organ transplants)
Nutritionally essential amino acids: - Answer✔PVT TIM HiLL
Conditionally essential amino acids - Answer✔Ariginine: we make it, but need more for growth
during childhood and pregnancy
Tyrosine: becomes essential when Phe is inadequate
Cysteine: becomes essential, when Met is inadequate
Sources of amino acids: - Answer✔Intracellular proteolysis: removes misfolded, old, damaged
proteins to supply essential AAs, and controls cell cycle transitions and cell disjunction
Digestion of proteins in food
de novo AA synthesis: provides nutrionally nonessential aa's that are needed for protein
synthesis, helps adjust aa pools in different tissues, allows cells to adapt to metabolic stress,
controls concentrations of central pathway metabolites, needed to make nucleotides hemes
hormons and neurotransmitters
Three pathways for intracellular protein turnover: - Answer✔Lysosome pathway:
an acidic organelle where proteins are protonated, undergo partial unfolding due to repulsion,
susceptible to proteolysis
Proteasome pathway:
ubiquitin is an 8.6 kDA protein enzymatically connected to unfolded proteins, marking them for
breakdown. Only ubiq. proteins can enter PROTEASOMES, barrel-like macromolecular
structures that use on-board proteases to form small peptides and AAs
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Autophagic pathway:
uses ubiquitin system and lysosomes to remove old organelles that get engulfed in an
autophagic vacuole
Ubiquitination's three enzyme process: - Answer✔Ubiquitination-initiating enzyme (E1)
Ubiquitin-conjugating enzyme (E2)
Ubiquitin-protein ligase (E3)
Poly-ubiquitination - Answer✔additional ubiquitin molecules can be added to any of the 7 lysyl
residues OR the N-terminus on ubiquitin to form ubiquitin chains, causing it to be delivered to
the proteasome
Endocytic and phagocytic vesicles - Answer✔recycle membrane-assoc proteins as well as
extracellular proteins, pathogens, and particles
Digestion - Answer✔process of breaking down food both mechanically and enzymatically within
GI tract to form body-utilizable substances
Digestion is almost completely ________, - Answer✔hydrolytic, using water to cleave peptides,
carboxylic esters, phosphate esters, phosphodiesters, O and N glycosides
Internal digestion is highly efficient bc: - Answer✔Breakdown of products can be captured
internal chem environment can be efficiently controlled
Digestive enzymes are produced and stored in _______ and ________.
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Release is controlled ______ __________ - Answer✔pancrease and stomach
neuro-hormonally
Pepsin - Answer✔enzyme in stomach, pref to cleave after Phe, Leu and Glu linkages
Enzymes in small intestine: - Answer✔Chymotrypsin : carboxyl side of aromatic residues
Trypsin: carboxyl side of lysine and arginine
Carboxypeptidase: cleaves C-terminal aa's
Elastase:
cleaves cross-links in ELASTIN, a flexible protein found in connective tissue
Zymogens - Answer✔inactive form of the enzyme, becomes active AFTER proteolytic cleavage
inactive enzymes are safer to store
zymogens prevent autophagy and apoptosis
The 4 major digestive proteases: - Answer✔Pepsin
Chymotrypsin
Trypsin
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