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BMSC 200 > post midterm ch. 6-10 > Flashcards

post midterm ch. 6-10 Flashcards

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1
Q

what is vitalism?

A

the belief that living things are fundamentally different from non living things

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2
Q

what is an apoenzyme?

A

inactive protein portion

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3
Q

what is a cofactor/conenzyme?

A

active non protein portion

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4
Q

what is a holoenzyme?

A

active whole enzyme

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5
Q

what do catalysts do?

A

lower the amount of energy required for a reaction to proceed, speed up attainment of equilibrium, unchanged by the reaction and recycled to participate in another reaction

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6
Q

what is an active site?

A

3D cleft formed from different parts of the polypeptide chain, where substrates are bound to enzymes by multiple weak interactions

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7
Q

when is a reaction spontaneous (exergonic)?

A

only if delta G is negative

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8
Q

what does the delta G of a reaction depend on?

A

the free energy of the product minus the free energy of the reactants

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9
Q

what is the relationship between the rate of a reaction and the activation energy?

A

inverse and exponential

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10
Q

when enzymes provide a lower energy pathway between the substrate and the product what happens?

A

activation energy of the transition state decreases which increases the rate of the reaction

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11
Q

what are the forces that lower the activation energy?

A
  • binding effects (substrate binding and transition state stabilization)
  • chemical effects (acid/base catalysis and covalent catalysis)
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12
Q

binding of substrate in the active site provides what?

A

specificity and catalytic power

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13
Q

how does substrate binding promote reactions?

A
  • reduces entropy
  • alignment of reactive functional groups of enzyme with the substrate
  • desolation of the substrate (removal of H2O molecules) to expose reactive groups
  • distortion of substances
  • induced fit of the enzyme in response to substrate binding
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14
Q

Thrombin cleaves which bonds?

A

Arg-Gly bonds

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15
Q

Trypsin cleaves by ?

A

cuts beside positively charged residues, cleaves by Lys and Arg

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16
Q

Chymotrypsin cleaves by ?

A

cuts beside aromatics, cleaves by Phe, Tyr, or Met

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17
Q

Elastase cleaves by ?

A

cuts beside small hydrophobics, cleaves by Gly and Ala

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18
Q

what is Histidines role in the catalytic mechanism?

A

acts to accept and donate a proton at each of the 2 stages of the reaction mechanism (acid base catalysis)

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19
Q

what is Aspartates role in the catalytic mechanism ?

A

stabilizes the positively charged Histidine to facilitate serine ionization

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20
Q

what is Serine’s role in the catalytic mechanism?

A

attacks the carbonyl group of the peptide bond to be cleaved (covalent catalysis)

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21
Q

what is involved in regulation of enzyme availability? (long term)

A

location, rate of synthesis, and degradation

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22
Q

what is involved in regulation of enzyme activity?

A
  • covalent modification (phosphorylation, methylation, glyosylation etc.)
  • non-covalent modification (allosteric regulation)
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23
Q

enzymatic pathways are often controlled through what?

A

negative feedback inhibition by the final product of the pathway to inhibit the enzyme catalyzing the first unique and committed step of the branch

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24
Q

the carbon that becomes chiral as a result of cyclization is ?

A

the anomeric carbon

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25
what is mutarotation?
- the alpha and beta configurations inter convert - occurs through a linear intermediate - represents a change in configuration
26
in solution, glucose is how much beta- glucopyranose and how much alpha-glucopyranse?
2/3 b-glucopyranose 1/3 a-glucopyranose
27
where is b-fructopyranose found?
in honey, is extremely sweet
28
what happens when you heat b-fructopyranose?
converts to b-fructofuranose, less sweet
29
corn syrup has a high concentration of what and is used to sweeten what?
high concentration of b-fructopyranose, used to sweeten cold drinks (not hot)
30
myrosinase acts on glucosinolate to produce what?
glucose and isothiocyanate (sharp bitter taste)
31
when do myrosinase and glucosinolate come together?
upon tissue damage
32
linear forms of monosaccharides are oxidized by what and allows for what?
- oxidized by mild oxidizing agents like iron and copper - allows for quantifications of sugars present in blood or urine
33
the end of the chain with a free anomeric carbon is called what?
the reducing end
34
what is a glycosidic bond?
primary structural linkage in all polymers of monosaccharides
35
where do O-glycosidic bonds occur?
through oxygen
36
where do N-glycosidic bonds occur?
through nitrogen
37
higher order carb structures are generated through the action of what?
glycotransferases
38
lactose intolerant people have insufficient levels of what?
insufficient levels of lactase that catalyses the hydrolysis of lactose into glucose and galactose
39
what are homopolysaccharides?
polymers containing a single type of monosaccharide
40
what are heteropolysaccharides?
polymers containing more than one type of monosaccharide
41
where and what form is glucose stored in animals?
stored as glycogen in the liver and skeletal muscle of animals
42
what form is glucose stored in plants?
stored as starch, mix of amylose (unbranched) and amylopectin (branched)
43
what is amylose?
a linear polymer of glucose residues through a(1-4) bonds
44
what is amylopectin?
consists of a(1-4) linked glucose residues with a(1-6) branch points every 24-30 residues
45
how many reducing ends do amylose and amylopectin have?
one
46
how many non-reducing ends do amylose and amylopectin have?
amylose has one amylopectin has multiple
47
what is cellulose?
- the primary component of plant cell walls (fibre) - a linear, homopolysaccharide of glucose residues - linear arrangement of b(1-4) glycosidic residues
48
what is chitin?
- the main component of exoskeletons (insects, lobsters etc.) - a linear homopolysaccharide of N-acetylglucosamine residues
49
what is the chemical difference between cellulose and chitin?
the replacement of hydroxyl group at C2 with acetylated amino group
50
what are glycoproteins?
proteins with covalently attached sugars, mostly protein, and serve a variety of biological roles
51
what are proteoglycans?
protein component linked to a carb called glycosaminoglycan, mostly carb, and serve structural and lubricating functions
52
in glycoproteins what are the sugars attached to?
the amide nitrogen of the side chain of asparagnine OR the hydroxyl oxygen of the side chain of serine or threonine
53
what does erythropoietin do?
- stimulates red blood cell productions, highly affective in the treatment of anemia - exploited by endurance athletes to increase oxygen carrying capacities
54
what is the extracellular matrix (ground substance) made of and what does it do?
- made of a mesh work of fibrous proteins and heteropolysaccharides (glycosaminoglycans) - holds cell together, provides a porous pathway for diffusion of nutrients/waste products and serves a cushioning function
55
what are fatty acids?
hydrocarbon with carboxylic head, usually an even number of carbons (12-24)
56
what does a saturated fatty acid look like?
no double bonds
57
more carbons means what for the melting point?
higher melting point
58
fatty acids required for energy are stored as what?
triacylglycerols
59
what is a low oxidation state?
less oxygenated fuels burn more efficiently; triacylglycerols have lower oxygenation state than carbs
60
what is a low hydration state?
lipids are hydrophobic with limited interaction with water providing a more compact, dehydrated energy storage form
61
what is saponification?
making soap from fat- treatment of fat with a string vase breaks the water linkages to release free fatty acids
62
how do fatty acids function as detergents and soaps ?
through formation of micelles that capture hydrophobic molecules
63
what are waxes?
non-polar esters of long chain fatty acids and long chain mono hydroxyl is alcohols
64
what are glycercophospholipids?
most abundant lipids in membranes, glycerol backbone with a phosphate at the C3 position
65
archaebacteria (extremophiles) membrane lipids contain what?
- ether linkages - branch points within the hydrocarbon tails - membrane spanning hydrocarbon tails composed from a single molecule
66
what is the structure of steroids (sterols) and what do they do?
four fused ring steroid nucleus (3 six carbon rings and a 5 carbon D ring) - serve as precursors for many biologically active products ex. testosterone
67
what does cholesterol do?
serves a number of critical biological functions like mediating membrane fluidity also serves as a precursor of steroid hormones and bile salts
68
what are the active roles of lipids?
intracellular signaling molecules, hormones, enzyme cofactors, pigments, vitamins
69
what are eicosanoids?
paracrine hormones, derivatives of C20 PUFAs (prostaglandins, thromboxanes, leukotrienes)
70
what are prostaglandins involved in?
construction of blood vessels
71
what are thromboxanes involved in?
blood clot formation
72
what are leukotrienes involved in?
smooth muscle contraction
73
below the phase transition temp the membrane is?
too solid
74
above the phase transition temp the membrane is?
too fluid
75
how do peripheral membrane proteins associate with the membrane?
through electrostatic or H-bonding interactions
76
the bulk of the peripheral membrane proteins is where?
in the cytosol or extracellular space
77
what does a hydropathy index look at?
the hydrophobic characteristics of a protein to predict transmembrane regions

BMSC 200 (2 decks)

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