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IPAP Biochem Martin > Test 1 > Flashcards

Test 1 Flashcards

1
Q

What are substrate binding sites called?

A

Active sites

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2
Q

How well the substrate interacts with the binding site depends on what?

A

Affinity

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3
Q

What are most enzymes made of?

A

Proteins

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4
Q

Depends on precisely defined arrangement of atoms in a binding site

A

Specificity

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5
Q

What shape is the active site?

A

3D

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6
Q

How do enzymes affect a reaction?

A

Accelerate the reaction but don’t change the equilibrium

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7
Q

When do enzymes bind in a reaction?

A

In the transition state

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8
Q

What else do enzymes require for a reaction to occur?

A

Cofactors

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9
Q

Deficiency of the enzyme phenylalanine hydroxylase

A

Phenylketonuria

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10
Q

S/S phenylketonuria

A

Traits of albinism, musty odor, eczema

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11
Q

Treatment for phenylketonuria

A

Diet low/absent in phenylalanine

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12
Q

What does phenylalanine hydroxylase do?

A

Converts phenylalanine into tyrosine

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13
Q

What are the two effects of enzyme regulations?

A

Increase (activate)

Decrease (inhibit)

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14
Q

What decreases the rate of a reaction

A

Competitive inhibitor

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15
Q

How do B-lactam antibiotics work?

A

Mimic the end amino acid sequence of unlinked peptidoglycans and IRREVERSIBLY BIND TO THE ACTIVE SITE TO COMPETITIVELY BLOCK FINAL CROSS-LINKING REACTION

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16
Q

Involves the binding of an effector molecule to facilitate the additional binding of substrate or inhibition of substrate

A

Allosteric regulation

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17
Q

Enzyme reaction RATE is increased or decreased by the binding of a second molecule at a site other than the first active site

A

Allostery

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18
Q

What are an exception to the michaelis-menten enzyme model?

A

Allosteric enzymes

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19
Q

The basics for most single substance enzyme kinetics, no intermediate or product inhibition

A

Michaelis menten enzyme

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20
Q

Example of allosteric binding

A

O2 in hemoglobin

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21
Q

Particular type of simple regulation in which the product of a single or a series of enzyme reactions can bind to inhibit or activate itself or the 1st enzyme in the reaction series

A

Feedback regulation

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22
Q

Proteins that bind to and regulate other proteins

A

Regulatory proteins

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23
Q

Reversible attachment of phosphoryl groups

A

Covalent modification

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24
Q

Catalyze the attachment of phosphoryl groups

A

Kinases

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25
Q

Catalyze the removal of phosphoryl groups

A

Phosphatases

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26
Q

Effect of proenzymes

A

Break down proteins

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27
Q

Two or more enzymes in the same individual that differ in amino acid sequence but which catalyze the exact same chemical

A

Isozymes

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28
Q

Enzyme found in all human cells and is able to bind glucose

A

Hexokinase

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29
Q

Enzyme found only in pancreas, liver, small intestine, and brain and binds glucose but requires higher concentration

A

Glucokinase

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30
Q

Two major families of nitrogenous bases

A

Purines and pyrimidines

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31
Q

Purines are

A

Adenosine and quanine

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32
Q

Pyrimidines

A

Cytisine
Thymidine
Uracil

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33
Q

Nitrogenous base and a ribose sugar

A

Nucleoside

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34
Q

Nitrogenous base, ribose sugar, and a phosphate group

A

Nucleotide

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35
Q

Differene between DNA and RNA

A

DNA double helix with deoxyribose

Vs

RNA single strand with ribose

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36
Q

Three amino acids involved in the synthesis of purines

A

Aspartate
Glycine
Glutamine

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37
Q

Structure of purines

A

Double ring structure

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38
Q

What stems from inosine monophosphate (IMP)?

A 
Adenosine monophosphate (AMP)
Guanosine monophosphate (GMP)
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39
Q

Required coenzyme for nucleoside/nucleotide synthesis and repair of DNA

A

Vitamin B9 folic acid (folate)

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40
Q

Structure of pyrimidine

A

Single ring

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41
Q

Difference between pyrimidines in RNA

A

RNA has uracil instead of thymidine

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42
Q

What nitro bases bond?

A

A-T(U in RNA)

G-C

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43
Q

How many hydrogen bonds are between Cytosine and Guanine?

A

Three

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44
Q

2 Hydrogen bonds

A

Adenosine to Thymidine

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45
Q

Pyrimidine analogue that blocks production of dTDP

A

FdUMP

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46
Q

What is FdUMP used in?

A

Chemotherapy

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47
Q

How is fluorocytosine used?

A

As an antibiotic because it is converted into an active nucloside or nucleotide only in bacteria

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48
Q

Characterized by accessive uric acid

A

Gout

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49
Q

What kind of bond is formed in RNA and DNA?

A

Phosphodiester

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50
Q

What Carbons are involved in phosphodiester bonds?

A

3’ and 5’

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51
Q

Is RNA or DNA more stable?

A

DNA

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52
Q

MRNA shape

A

Squiggles

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53
Q

TRNA shape

A

Cross or T

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54
Q

Function of mRNA

A

Carries genetic code from DNA

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55
Q

Function of tRNA

A

Carries individual amino acids and matches them with mRNA during protein synthesis

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56
Q

Purpose of regulatory RNA

A

Regulates DNA expression, posttransriptional mRNA processing and the activity of mRNA

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57
Q

Structure of DNA strand

A

Double helix

Major and minor groove (where molecules can selectively bind)

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58
Q

Semi-conservative?

A

Two strands from one. Maintains one strand of parent strand in each new strand

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59
Q

What is ADA?

A

Adenosine deaminase deficiency

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60
Q

What does adenosine deaminase do?

A

Breaks down adenosine from food for the turnover of nucleic acids

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61
Q

S/S ADA

A 
Severe combined immunodeficiency
Pneumonia
Chronic diarrhea
Skin rashes
Slow (retarded)
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62
Q

Potential treatment for ADA

A

Gene therapy

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63
Q

Melting points of saturated fatty acids

A

Longer the higher the melting point. More bonds to break

64
Q

Fats that only contain single c-c bonds

A

Saturated fats

65
Q

Compare the melting points of saturated and unsaturated fatty acids

A

Unsaturated have lower melting point because the uneven layering of C bonds

66
Q

What happens as the number of c=c bonds increases?

A

Melting point decreases

67
Q

What is the backbone of a sphingolipid?

A

Ceramide

68
Q

Ceramide backbone with a phosphorylcholine

A

Sphingomyelin

69
Q

Four glycosphingolipids

A

Cerebrosides
Sulfatides
Globosides
Gangliosides

70
Q

Ceramide plus single glucose or galactose

A

Cerebroside

71
Q

Ceramide plus one or more attached sialic acid molecules, most often NANA

A

Ganglioside

72
Q

Sulfatides

A

Ceramide plus SO4 modified galactose

73
Q

Ceramide plus N-acetyl

A

Globoside

74
Q

Important glycosphingolipid in the nerve cell myelin membranes

A

Cerebrosides

75
Q

Glycosphingolipid plays a role as an adhesion molecule in the recruitment of immune cells

A

Sulfatides

76
Q

Where are sulfatides found

A

Mainly in the brain, CNS, and PNS

77
Q

Glycosphingolipid works as a cell receptor

A

Globosides

78
Q

Where are globosides found

A

RBC
Serum
Liver
Spleen

79
Q

Glycoshingolipid involved in binding, recognition, and signaling between cells

A

Gangliosides

80
Q

Where are gangliosides?

A

Nervous system

81
Q

Basic glycosphingolipid involved in ABO blood types

A

Hh-substance

82
Q

Four major groups of eicosanoids

A

Prostaglandins
Prostacyclins
Thromoxanes
Leukotrienes

83
Q

What inhibits the cyclooxygenase in the eicosanoid synthetic pathway

A

Aspirin (irreversible)

Motrin and indomethacin (competitive inhibitor)

84
Q

What inhibitis the ablity of phospholipase A2 to convert into arachidonic acid?

A

Prednisolone (steroid)

85
Q

What two pathways are in the eicosanoid synthetic pathway?

A

Conversion of arachidonic acid into cyclooxygenase or 5-lipooxygenase

86
Q

Wher are prostaglandins produced?

A

Throughout the body and target cells in the immediate vicinity of their secretion

87
Q

In CNS, mast cells, and adipose affecting sleep and lowering body temp (opposit effect of PGE2, contraction of bronchi, inhibited platelet aggregation

A

PGD2

88
Q

Dilate blood vessels, patent ductus arteriosus, prevent gastric ulcers

A

PGE1

89
Q

Causes fever, inflammation, sensitivity to pain, wakening, renal arteriolar dilation, smooth muscle activity, softening of cervix for labor, increase bone reabsorption

A

PGE2

90
Q

Used medically to induce labor/abortion

A

PGF2a

91
Q

Inhibits platelet activation, vasodilator, bronchodilator, and decreased stomach acid secretion

A

PGI2 or prostacycline

92
Q

Facilitates platelat aggregation, vasoconstrictor

A

Thromboxanes

93
Q

Eicosanoid synthesized by lipoxygenase in leukocytes, promotes inflammation in lungs

A

Leukotrienes

94
Q

Purpose of cholesterol

A

Modulates fluidity critical to cell signaling, binding, wound healing, immune response

95
Q

Dietary triacylglycerols (90%) and cholesterol

A

Chylomicrons

96
Q

Endogenous triacylglycerols and cholesterol

A

VLDL

97
Q

Triacylglycerols and cholesterol

A

IDL

98
Q

Cholesterol

A

LDL

99
Q

Phospholipid and protein

A

HDL

100
Q

Two amino acids that make bile salts

A

Glycine and taurine

101
Q

Purpose of bile acid

A

Solubilize dietary fats in the mainly watery environment of the small intestine

102
Q

Where and from what are bile salts made

A

Liver, cholesterol

103
Q

Regulates the mineral sodium and is made in the adrenal cortex

A

Mineralcorticosteroids

104
Q

What is the primary mineralcorticoid in humans

A

Aldosterone (produced in adrenal cortex)

105
Q

Controls the release of glucose from the liver and is made in the adrenal cortex

A

Glucocorticoid

106
Q

When is glucocorticoid released?

A

During starvation and other stress related conditions

107
Q

What does glucocorticoid do?

A

Promotes release of glucose from liver storage

108
Q

What vitamin is required for calcium metabolism?

A

Vitmain D

109
Q

How is vitamin D produced

A

Conversion of cholesterol

110
Q

What’s required to convert cholesterol into vitamin D

A

UV light to break open the second and third rings

111
Q

What is the active form of vitamin D

A

Calcitrol

112
Q

Where does vitamin D get another OH?

A

From the kidneys

113
Q

Formula for a carbohydrate

A

CH2O

114
Q

What makes up lactose

A

galactose to glucose b 1-4

115
Q

Glucose to glucose a 1-1

A

Trehalose

116
Q

Bonds of maltose

A

Glucose to glucose a 1-4

117
Q

Glucose and fructose

A

Sucrose a1-2

118
Q

What sugar is in milk

A

Lactose

119
Q

Trehalose is found in

A

Sunflower seeds shrimp and mushrooms

120
Q

Barley contains

A

Maltose

121
Q

Table sugar is

A

Sucrose

122
Q

Glycogen structure

A

Glucose to glucose a 1-4 bonds branching on a 1-6 approximately every 10 glucose residues

123
Q

Cellulose structure

A

Chains of glucose to glucose b 1-4 bonds

124
Q

What type of bond forms between sugars

A

Glycoside linkage

125
Q

What gene turns off lactase production?

A

MCM6

126
Q

What is lactase

A

Enzyme breaks down lactose

127
Q

What is lactose intolerance?

A

A lactase deficiency caused by MCM6

128
Q

Contain repeating disaccharide chains of a modified glucose and or galactose and compose a large portion of the extracellular matrix

A

Glycosaminoglycans (GAGS)

129
Q

Mainly polysaccharides with a small percentage <10% protein

A

Proteoglycan

130
Q

Mainly small proteins with a smmall percentage of carbohydrate

A

Glycoprotein

131
Q

Essential amino acids

A 
Threonine
Valine
Leucine
Isoleucine
Methionine
Phenylalanine
Tryptophan
Histidine
Lysine
132
Q

Essential amino acids for childhood

A

Cysteine
Tyrosine
Argenine

133
Q

Amino acids that prefer to be inside a folded protein

A

Hydrophobic

134
Q

Amino acids that interact with surrounding water molecules

A

Hydrophillic

135
Q

Amino acids that prefer to be at the surface of a folded protein or in contact with other charged atoms/molecules

A

Charged

136
Q

Why is proline speciial

A

B turns

137
Q

What does cysteine become and why

A

Cystine, di sulfide bonds

138
Q

Histidine’s special properties

A

4 places to lose a H+

139
Q

Two amino acids that can make b-turns

A

Cysteine and glycine

140
Q

Four pHs that histidine falls into

A

Below 1.3
1.3-6.0
6.0-9.3
Greater than 9.4

141
Q

How do proteins bond?

A

Peptide bonds

They bind between the carboxyl group and the amine group

142
Q

Primary structure

A

Sequence of amino acids

143
Q

Shapes of the secondary structure

A

A-helix
B-sheets

DNA does not form an A-helix (Double helix)

144
Q

2’ structures fold and interact to form

A

Tertiary structure

145
Q

Quaternary structure

A

Multiple protein subunits (monomers)

146
Q

Two structural proteins

A

Actin and tubulin

147
Q

Tubulin forms a

A

Dimer

148
Q

Four categories of proteins

A

Enzymes
Structural proteins
Motor proteins
Transport/channel proteins

149
Q

What optomizes the structure of collagen

A

Having Glycine as every third amino acid

150
Q

Three typical amino acids in collagen

A

Glycine, proline, hydroxyproline

151
Q

Genetic disease that affects collagen containing tissues

A

Osteogenesis imperfecta

152
Q

What causes osteogenesis imperfecta?

A

Point mutations that destabilize or alter triple helix structure

153
Q

What causes collagen to have a helical structure

A

Glycine as every third amino acid

154
Q

Cause of scurvy

A

Vitamin c deficiency

155
Q

S/S scurvy

A

Abnormal bleeding
Skin diiscoloration
Gum deterioration
Weakening of bones

156
Q

Name one motor protein

A

Myosin

157
Q

What transports O2?

A

Myoglobin and hemoglobin

IPAP Biochem Martin (1 decks)

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