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XIO > Chem test 3 > Flashcards

Chem test 3 Flashcards

1
Q

if a zwitter ion is in a basic solution…

A

(ph 12) it will lose an H from NH3 to become NH2

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2
Q

if a zwitter ion is in an acidic solution…

A

pH 1, it will gain an H, to become NH3 - OH

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3
Q

peptide bond is just…(amino acid)

A

the C and the NH joining - the OH and the other H from the N form a + H20

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4
Q

ex. of primary structure

A

Asp-Arg-Val-Tyr

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5
Q

secondary structure is also the…(second loop-d-loop)

A

loops and coils

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6
Q

Tertiary structure held together by…

A

noncovalent bonds - primarily amino acid side chains, sometimes disulfide bonds between thiol groups

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7
Q

Quaternary structure - held together by what bonds?

A

held together by noncovalent interactions

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8
Q

how to tell if it’s quaternary? (quarterback has more than one leg)

A

if there is more than one polypeptide chain

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9
Q

if there are bends, twists, or a compact structure, it’s (tt twist)

A

tertierary

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10
Q

5 interactions in tertiary and quatranery structures (SHHHD the tert and quat)

A

hydrophilic and hydrophobic interactions, salt bridges, hydrogen bonds, and disulfide bonds

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11
Q

motifs of secondary structures - this is just what secondary structures are

A

alpha, beta, loops and coils

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12
Q

Polypeptides are primarily held together by

A

noncovalent forces, but covalent bonds and non–amino acid portions may also be incorporated

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13
Q

Cofactors can be…(co can be uptight or loose)

A

tightly held or loosely bound, so that they can enter and leave the active site

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14
Q

coenzyme is an…

A

organic molecule that acts as an enzyme cofactor

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15
Q

By combining with cofactors, enzymes acquire…

A

chemically reactive groups not available in side chains, ie metal ions and trace minerals

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16
Q

are enzymes soluble or not?

A

most are soluble, globular, with a few exceptions

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17
Q

The catalytic activity of an enzyme is measured by…

A

its turnover number

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18
Q

enzymes - Because oxidation and reduction must occur together, these enzymes…(always need a co)

A

require coenzymes that are reduced or oxidized as the substrate is oxidized or reduced

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19
Q

Oxidoreductases Subclasses - this is an enzyme subclass (just dehydrate the oxi, but keep the ases)

A

Oxidoses
Reductases
Dehydrogenases

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20
Q

Oxidoses (oxidize me)

A

catalyze oxidation by addition of O2 to a substrate

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21
Q

Reductases (reduct the oxygen)

A

removing oxygen

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22
Q

Dehydrogenases (not what you think)

A

catalyze the removal or addition of 2 H atoms and require a coenzyme

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23
Q

enzyme classification (enzymes, TO HILL! all ase ending - they’re enzymes)

A

Oxidoreductases, Transferases, Hydrolases, Isomerases, Lyases, Ligases

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24
Q

Transferases catalyzes…

A

transfer of a group from one molecule to another.

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25
Q

types of Transferases (kin is transferring to tran)

A

Transaminases and Kinases

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26
Q

Transaminases

A

transfer an amino group between substrates

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27
Q

Kinases

A

transfer a phosphate group from adenosine triphosphate (ATP) to produce adenosine diphosphate (ADP) and a phosphorylated product.

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28
Q

Hydrolases

A

catalyze the hydrolysis of substrates, the breaking of bonds with addition of water. These enzymes are particularly important during digestion, and provide amino acids for protein synthesis and glucose for use in energy- generating pathways.

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29
Q

Hydrolases Subclasses (PLAN to split the water) think digestion

A

lipases, proteases, amylases, nucleases

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30
Q

Lipases (fatty lips) type of hydrolases

A 
break glycerides (fats) into glycerol and
fatty acids
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31
Q

Proteases (tease protein into amino acids) type of hydrolases

A

break proteins into peptides and amino acids

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32
Q

Nucleases - type of hydrolases (nuclear DNA)

A

break deoxyribonucleic acid (DNA) and RNA into nucleic acids

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33
Q

Lyases (type of hydrolases) (liase-on makes a double bond - client and boss)

A

catalyze the addition of a molecule such as H2O, CO2, or NH3 to a double bond or the reverse reaction in which a molecule is eliminated to create a double bond

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34
Q

Lyases Subclasses (as a liase-on I hid - HDDD) think De - removal

A

Decarboxylases
Deaminases
Dehydratases
Hydratases

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35
Q

Decarboxylases

A

catalyze the removal of CO2

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36
Q

Deaminases

A

catalyze the removal of NH3

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37
Q

Ligases (2 substrates need a lig up for ATP and DNA)

A

catalyze the bonding together of two substrate molecules. Because such reactions are generally not favorable, they require the simultaneous release of energy by a hydrolysis reaction, usually by the conversion of ATP to ADP. Ligases are involved in synthesis of biological polymers, such as proteins and DNA

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38
Q

Ligases Subclasses (lig up in SoCal)

A

Synthetases and Carboxylases

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39
Q

Synthetases (synthetic ATP)

A

catalyze the formation between two

substrates using ATP energy

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40
Q

Carboxylases

A

catalyze the formation of a bond between CO2 and a substrate using ATP energy

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41
Q

Enzymes act as catalysts because of their ability to: (COPE)

A

proximity, orientation, catalytic, and energy effect

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42
Q

Enzymes denature when

A

Enzymes denature when noncovalent attractions between protein side chains are disrupted, destroying the active site

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43
Q

Water-soluble vitamins contain

A

Water-soluble vitamins contain –OH, –COOH, or other polar groups that impart water solubility

44
Q

types of vitamins

A

water soluble and fat soluble

45
Q

water soluble vitamins found in what foods? (BMMP)

A

milk, meat, bread, potatoes

46
Q

fat soluble vitamins (KADE is…)

A

A, D, E, and K

47
Q

no fat soluble vitamins are…(fat can’t be co)

A

coenzymes

48
Q

antioxidants - (not anti free radicals)

A

defuse free radicals - prevent oxidation by reacting w/ oxidizing agent

49
Q

mutarotation (mutate god position)

A

alpha and beta switch due to change in equalibrium

50
Q

As the open-chain aldehyde is oxidized,

A

the equalibrium is thrown off and it continues to reproduce as open chain

51
Q

Carbohydrates that react with mild oxidizing agents are…(mild sugar)

A

classified as reducing sugars

52
Q

tautomerism (the H taught the double bond to switch)

A

equilibrium that results from a shift in position of a hydrogen atom and a double bond

53
Q

can easily be converted to sugar alcohol

A

monosaccharides. This is done by exposing sugar to H2 in presence of catalyst Pt. Basically H-C=O becomes CH2OH

54
Q

hemiacetals plus alcohols makes..

A

acetals. Bi-product is H2O

55
Q

glycosides

A

glucose and other monosaccharides are cyclic hemiacetals, they also react with alcohols to form acetals called glycosides

56
Q

Glycosidic bond

A

A bond between the anomeric carbon atom of a monosaccharide and an –OR group

57
Q

the reverse of glycosidic bond formation

A

hydrolysis - takes place during digestion of all carbohydrates

58
Q

common monosaccharides (mono mi fgg)

A

fructose, galactose and glucose

59
Q

common disaccharides (SML disacchrides)

A

lactose, maltose, sucrose

60
Q

reducing sugar

A

Sugars that can freely interconvert between the cyclic structure and the straight chain form with an available aldehyde or ketone

61
Q

how to calculate the number of possible stereoisomers in sugars

A

it’s just 2 (n), n = number of chiral carbons, so if it’s 3, then it’s 2 x 2 x 2.

62
Q

cellulose structure (to get rid of it, start up! )

A

3 is up, 2 is down, O is up, 3 is down, 2 is up

63
Q

amylose, amylopectin and glycogen (the same) structure (amy start up, but then goes down in the middle)

A

up, down, down, up, down

64
Q

common use of fructose

A

to make high fructose corn syrup

65
Q

common use of maltose

A

in beer, used to sweeten foods

66
Q

common use of lactose

A

milk sugar

67
Q

common use of sucrose

A

table sugar, made from sugar beets

68
Q

common use of amylose (amy loves potatoes)

A

20% starch, beans, grains, potatoes

69
Q

amylopectin (amy hangs out with amy)

A

found in seeds, plants, 80% of starch

70
Q

glycogen

A

stored as glucose

71
Q

glyceraldehyde

A

only 3 carbons, and it’s an aldehyde of course

72
Q

Catalase (heme enzyme) is almost completely specific for one reaction:

A

the decomposition of hydrogen peroxide

73
Q

Thrombin

A

catalyzes hydrolysis of a peptide bond following an arginine, and primarily acts on fibrinogen, a protein essential to blood clotting.

74
Q

Carboxypeptidase A (A to C)

A

removes many different C-terminal amino acid residues from protein chains during digestion

75
Q

Papain

A

catalyzes the hydrolysis of peptide bonds in many locations

76
Q

in lyases subclasses, only Hydratases is..

A

addition, decarboxylases, Deaminases, and Dehydratases are all removal

77
Q

if a double bond is created or removed in a reaction, it’s (the bond is the liase -on)

A

lyases

78
Q

acids…

A

donate protons

79
Q

bases

A

accept

80
Q

The rate when the enzyme is saturated is determined by (PET rate)

A

the efficiency of the enzyme, the pH, and the temperature

81
Q

Rates of enzyme-catalyzed reactions do not increase…

A

continuously with rising temperature. They reach a plateau and then drop

82
Q

example of nonpolar and neutral amino acid AND it’s structure

A

glycine - no side chain, just an H

83
Q

example of polar and neutral amino acid AND it’s structure

A

cysteine - side chain is just CH2 with an SH hanging off it

84
Q

example of acidic amino acid AND it’s structure

A

asparatic acid, side chain is just one CH2 with a C-O- attached.
||
O

85
Q

example of basic amino acid AND it’s structure

A

lysine - 4 CH2s and the last one is NH3+

86
Q

ribose structure (down w/ ribs)

A

5 carbon circle - all OHs are down

87
Q

deoxyribose structure (missing one rib)

A

5 carbon sugar circle - only 2 OHs, both down - just 2 Hs in the middle

88
Q

all simple sugars, including all aldehyde and ketose (in basic solution) are…

A

reducing sugars - any sugar than can be turned into carboxylate

89
Q

to identify chiral carbons in cyclic molecules…

A

go in a circle clockwise and counterclockwise. In glucose circle, there are 5 chiral carbons. In straight chain, there are 4.

90
Q

galactose structure (galactose and glucose are in the same neighborhood)

A

galactose the same but 2 houses on the left

91
Q

dextrose is just…

A

glucose

92
Q

when 2 monosaccharides join, both hemiacetals, it forms…

A

disaccharides, they become acetals. The alcohol is from the OH on carbon 4 of the hemiacetal on the right

93
Q

maltose is made of (malt on gg bridge)

A

2 glucoses

94
Q

one polysaccharide humans can use is…

A

starch. Remember - polysaccharides are made only of glucose.

95
Q

which is soluble, amylose or amylospectine?

A

only amylose

96
Q

glycogen link is…(god needs glycogen)

A

alpha 1,4 (a few 1,6)

97
Q

if an amino acid has an OH in the side chain, it’s always going to be…

A

polar neutral

98
Q

dipolar ions are…

A

zwitter ions. They have one + charge and one - charge

99
Q

wool, hair and fingernails are alpha or beta?

A

ALPHA

100
Q

trace minerals join with enyzme by…

A

coordinate covalent bonds (just means one is providing 2 electrons) and they act as a lewis acids - BECAUSE they are positive ions and they need electrons - ie Mg2+

101
Q

important co-enzymes (B an important FAN of co-enzymes)

A

FAD, A, B12, NAD

102
Q

naming enzymes ex.

A

pyruvate carboxylate (this is ligase) adding a carboxyl group to pyruvate

103
Q

active site is…(the shape is active)

A

a pocket in an enzyme with the specific shape and chemical makeup necessary to bind a substrate

104
Q

Specificity of the enzyme is…(specificity is the STR of the show)

A

the limitation of the activity of an enzyme to a specific substrate, specific reaction, or specific type of reaction

105
Q

a co-enzyme is a type of…

A

cofactor

106
Q

what vitamins are water soluble?

A

all B and C and biotin AND they act as co-enyzmes

107
Q

vitamin B1 does what?

A

lowers blood pressure

XIO (372 decks)

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