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Biomolecules Of Life > W8 vitamins > Flashcards

W8 vitamins Flashcards

1
Q

what are vitamins for

A

metabolic functions

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2
Q

what are accessory nutrients

A

supply no energy
form no structures

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3
Q

what are vitamin precursors called

A

pro-vitamins

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4
Q

what are the classes of vitamins

A

A-E
K

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5
Q

what type of class B vitamins are there (nums)

A

1,2,3,5,6,7,9,12

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6
Q

what is vitamin B8 known as

A

AMP

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7
Q

what is vitamin H

A

biotin

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8
Q

which vitamins are water soluble

A

vitamin C and H
all of vitamin B types

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9
Q

what happens to vitamin soluble vitamins

A

not stored in tissue
excess removed w urine

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10
Q

which 4 vitamins are lipid soluble

A

vitamin A D E K

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11
Q

what happens to lipid soluble vitamins

A

stored in liver and adipose
cannot be removed only used

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12
Q

where are ingested vitamins from (apart from B12)

A

plants - photosynthesis

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13
Q

which 2 vitamins origins is from pro-vitamins synthesis

A

vitamin A and D

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14
Q

what is the pro-vitamin for retinol (vitamin A)

A

Beta carotene

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15
Q

What is the co-enzyme most vitamins are converted to

A

B12

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16
Q

which 2 vitamins act as hormones sometimes

A

A and D

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17
Q

which 2 vitamins are antioxidants

A

C and E

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18
Q

What do co-enzymes do

A

Makes active site for reactive for substrates

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19
Q

What are the 4 oxidative coenzymes

A

NAD{
NADP+
FAD
lipoic acid

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20
Q

What can vitamin cofactors do

A

Act as donor or acceptors

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21
Q

What is antioxidant known as as a

A

Reducing agent

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22
Q

How is ascorbic acid vitamin C synthesised

A

Hydorxlyation of collagen

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23
Q

Which type of vitamin acts as energy carriers

A

B vitamins

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24
Q

Where is riboflavin (B2) found

A

Eggs dairy veg

25
What is coenzyme A derived from
B5
26
Which vitamin is a steroid hormone
D3
27
What does vitamin D3 do
Regulate calcium and phosphorous
28
What is proteolysis
Process where specific peptide bonds are hydrolysed by proteases
29
what is the enzyme that speeds up peptide bonds breakage
peptidases
30
what is chymotrypsin
digestive enzyme found in gut
31
what family of proteins is chymotrypsin apart of
serine protease
32
what are the 3 polypeptide chains of chymotrypsin cleaved by
trypsin
33
what are the 3 chains of chymotrypsin is bonded by
hydrogen bonding
34
what does chymotrypsin cleave
peptide bond on COOH side of aromatic AA
35
what is the mechanism of chymotrypsin called
double displacement reaction
36
How does a double displacement work
Acylation then deacylation
37
What are the 2 phases of chymotyrpsin mech
Burst and steady-state
38
what is the mechanism of chymotrypsin
covalent catalysis nucleophile attacks carbonyl C nucleophile is from serine of active site
39
how is the chymotrypsin nucleophile made
histidine polarises OH in serine and substrate H57 to make alkoxide ion
40
what is the tetrahedral intermediate of chymotrypsin mech stabilised by
oxyanion hole
41
what are the steps to chymotrypsin mechanism
subrate A binds nucleophile attacks to make tetrahedral intermediate tetrahedral intermediate collapse amine is released]water binds nucleophile attacks in acyl enzyme collapse again release of carboxylic acid
42
what is the hydrophobic pocket in chymotrypsin
S1 pocket
43
what are the other 3 possible nucleophiles
cysteine protease apartyl protease metalloprotease
44
what is haemoglobin structure
2 alpha and 2 beta subunits
45
what group binds to O2
haem group
46
where does the Fe2+ lie in haemoglobin
outside tetrapyrrole ring
47
what helps the binding of O2 to haem
histidine residue
48
what makes O2 binding easier
cooperative binding
49
what does binding of O2 to haemoglobin do
changes angle of a1b1 by 15 degree
50
what are the 2 states of haemoglobin
tesne = deoxygenated relaxed = oxygenated
51
in the concerted model of cooperative binding what does it look like
r state have O2 in circles t state have O2 in boxes more O2 binding equilibrium shifts to R state
52
53
in the sequential model of cooperative binding what does it look like
binding of O2 causes shift to R form allows other subunits ti bind O2 at a higher affinity
54
which can stabilise the T state
2,3 BPG
55
what are the 2 allosteric regulators of O2 binding
Co2 and H+
56
what does decreased Ph do for T state
stability to allow salt bridges to form
57
how does Co2 decrease pH
carbonic anhydrase
58
what is formed for salt bridges due to CO2
carbamate

Biomolecules Of Life (11 decks)

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