Test 1 Flashcards
1
Q
What are substrate binding sites called?
A
Active sites
2
Q
How well the substrate interacts with the binding site depends on what?
A
Affinity
3
Q
What are most enzymes made of?
A
Proteins
4
Q
Depends on precisely defined arrangement of atoms in a binding site
A
Specificity
5
Q
What shape is the active site?
A
3D
6
Q
How do enzymes affect a reaction?
A
Accelerate the reaction but don’t change the equilibrium
7
Q
When do enzymes bind in a reaction?
A
In the transition state
8
Q
What else do enzymes require for a reaction to occur?
A
Cofactors
9
Q
Deficiency of the enzyme phenylalanine hydroxylase
A
Phenylketonuria
10
Q
S/S phenylketonuria
A
Traits of albinism, musty odor, eczema
11
Q
Treatment for phenylketonuria
A
Diet low/absent in phenylalanine
12
Q
What does phenylalanine hydroxylase do?
A
Converts phenylalanine into tyrosine
13
Q
What are the two effects of enzyme regulations?
A
Increase (activate)
Decrease (inhibit)
14
Q
What decreases the rate of a reaction
A
Competitive inhibitor
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
16
Q
Involves the binding of an effector molecule to facilitate the additional binding of substrate or inhibition of substrate
A
Allosteric regulation
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
18
Q
What are an exception to the michaelis-menten enzyme model?
A
Allosteric enzymes
19
Q
The basics for most single substance enzyme kinetics, no intermediate or product inhibition
A
Michaelis menten enzyme
20
Q
Example of allosteric binding
A
O2 in hemoglobin
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
22
Q
Proteins that bind to and regulate other proteins
A
Regulatory proteins
23
Q
Reversible attachment of phosphoryl groups
A
Covalent modification
24
Q
Catalyze the attachment of phosphoryl groups
A
Kinases
25
Catalyze the removal of phosphoryl groups
Phosphatases
26
Effect of proenzymes
Break down proteins
27
Two or more enzymes in the same individual that differ in amino acid sequence but which catalyze the exact same chemical
Isozymes
28
Enzyme found in all human cells and is able to bind glucose
Hexokinase
29
Enzyme found only in pancreas, liver, small intestine, and brain and binds glucose but requires higher concentration
Glucokinase
30
Two major families of nitrogenous bases
Purines and pyrimidines
31
Purines are
Adenosine and quanine
32
Pyrimidines
Cytisine
Thymidine
Uracil
33
Nitrogenous base and a ribose sugar
Nucleoside
34
Nitrogenous base, ribose sugar, and a phosphate group
Nucleotide
35
Differene between DNA and RNA
DNA double helix with deoxyribose
Vs
RNA single strand with ribose
36
Three amino acids involved in the synthesis of purines
Aspartate
Glycine
Glutamine
37
Structure of purines
Double ring structure
38
What stems from inosine monophosphate (IMP)?
```
Adenosine monophosphate (AMP)
Guanosine monophosphate (GMP)
```
39
Required coenzyme for nucleoside/nucleotide synthesis and repair of DNA
Vitamin B9 folic acid (folate)
40
Structure of pyrimidine
Single ring
41
Difference between pyrimidines in RNA
RNA has uracil instead of thymidine
42
What nitro bases bond?
A-T(U in RNA)
| G-C
43
How many hydrogen bonds are between Cytosine and Guanine?
Three
44
2 Hydrogen bonds
Adenosine to Thymidine
45
Pyrimidine analogue that blocks production of dTDP
FdUMP
46
What is FdUMP used in?
Chemotherapy
47
How is fluorocytosine used?
As an antibiotic because it is converted into an active nucloside or nucleotide only in bacteria
48
Characterized by accessive uric acid
Gout
49
What kind of bond is formed in RNA and DNA?
Phosphodiester
50
What Carbons are involved in phosphodiester bonds?
3' and 5'
51
Is RNA or DNA more stable?
DNA
52
MRNA shape
Squiggles
53
TRNA shape
Cross or T
54
Function of mRNA
Carries genetic code from DNA
55
Function of tRNA
Carries individual amino acids and matches them with mRNA during protein synthesis
56
Purpose of regulatory RNA
Regulates DNA expression, posttransriptional mRNA processing and the activity of mRNA
57
Structure of DNA strand
Double helix
| Major and minor groove (where molecules can selectively bind)
58
Semi-conservative?
Two strands from one. Maintains one strand of parent strand in each new strand
59
What is ADA?
Adenosine deaminase deficiency
60
What does adenosine deaminase do?
Breaks down adenosine from food for the turnover of nucleic acids
61
S/S ADA
```
Severe combined immunodeficiency
Pneumonia
Chronic diarrhea
Skin rashes
Slow (retarded)
```
62
Potential treatment for ADA
Gene therapy
63
Melting points of saturated fatty acids
Longer the higher the melting point. More bonds to break
64
Fats that only contain single c-c bonds
Saturated fats
65
Compare the melting points of saturated and unsaturated fatty acids
Unsaturated have lower melting point because the uneven layering of C bonds
66
What happens as the number of c=c bonds increases?
Melting point decreases
67
What is the backbone of a sphingolipid?
Ceramide
68
Ceramide backbone with a phosphorylcholine
Sphingomyelin
69
Four glycosphingolipids
Cerebrosides
Sulfatides
Globosides
Gangliosides
70
Ceramide plus single glucose or galactose
Cerebroside
71
Ceramide plus one or more attached sialic acid molecules, most often NANA
Ganglioside
72
Sulfatides
Ceramide plus SO4 modified galactose
73
Ceramide plus N-acetyl
Globoside
74
Important glycosphingolipid in the nerve cell myelin membranes
Cerebrosides
75
Glycosphingolipid plays a role as an adhesion molecule in the recruitment of immune cells
Sulfatides
76
Where are sulfatides found
Mainly in the brain, CNS, and PNS
77
Glycosphingolipid works as a cell receptor
Globosides
78
Where are globosides found
RBC
Serum
Liver
Spleen
79
Glycoshingolipid involved in binding, recognition, and signaling between cells
Gangliosides
80
Where are gangliosides?
Nervous system
81
Basic glycosphingolipid involved in ABO blood types
Hh-substance
82
Four major groups of eicosanoids
Prostaglandins
Prostacyclins
Thromoxanes
Leukotrienes
83
What inhibits the cyclooxygenase in the eicosanoid synthetic pathway
Aspirin (irreversible)
| Motrin and indomethacin (competitive inhibitor)
84
What inhibitis the ablity of phospholipase A2 to convert into arachidonic acid?
Prednisolone (steroid)
85
What two pathways are in the eicosanoid synthetic pathway?
Conversion of arachidonic acid into cyclooxygenase or 5-lipooxygenase
86
Wher are prostaglandins produced?
Throughout the body and target cells in the immediate vicinity of their secretion
87
In CNS, mast cells, and adipose affecting sleep and lowering body temp (opposit effect of PGE2, contraction of bronchi, inhibited platelet aggregation
PGD2
88
Dilate blood vessels, patent ductus arteriosus, prevent gastric ulcers
PGE1
89
Causes fever, inflammation, sensitivity to pain, wakening, renal arteriolar dilation, smooth muscle activity, softening of cervix for labor, increase bone reabsorption
PGE2
90
Used medically to induce labor/abortion
PGF2a
91
Inhibits platelet activation, vasodilator, bronchodilator, and decreased stomach acid secretion
PGI2 or prostacycline
92
Facilitates platelat aggregation, vasoconstrictor
Thromboxanes
93
Eicosanoid synthesized by lipoxygenase in leukocytes, promotes inflammation in lungs
Leukotrienes
94
Purpose of cholesterol
Modulates fluidity critical to cell signaling, binding, wound healing, immune response
95
Dietary triacylglycerols (90%) and cholesterol
Chylomicrons
96
Endogenous triacylglycerols and cholesterol
VLDL
97
Triacylglycerols and cholesterol
IDL
98
Cholesterol
LDL
99
Phospholipid and protein
HDL
100
Two amino acids that make bile salts
Glycine and taurine
101
Purpose of bile acid
Solubilize dietary fats in the mainly watery environment of the small intestine
102
Where and from what are bile salts made
Liver, cholesterol
103
Regulates the mineral sodium and is made in the adrenal cortex
Mineralcorticosteroids
104
What is the primary mineralcorticoid in humans
Aldosterone (produced in adrenal cortex)
105
Controls the release of glucose from the liver and is made in the adrenal cortex
Glucocorticoid
106
When is glucocorticoid released?
During starvation and other stress related conditions
107
What does glucocorticoid do?
Promotes release of glucose from liver storage
108
What vitamin is required for calcium metabolism?
Vitmain D
109
How is vitamin D produced
Conversion of cholesterol
110
What's required to convert cholesterol into vitamin D
UV light to break open the second and third rings
111
What is the active form of vitamin D
Calcitrol
112
Where does vitamin D get another OH?
From the kidneys
113
Formula for a carbohydrate
CH2O
114
What makes up lactose
galactose to glucose b 1-4
115
Glucose to glucose a 1-1
Trehalose
116
Bonds of maltose
Glucose to glucose a 1-4
117
Glucose and fructose
Sucrose a1-2
118
What sugar is in milk
Lactose
119
Trehalose is found in
Sunflower seeds shrimp and mushrooms
120
Barley contains
Maltose
121
Table sugar is
Sucrose
122
Glycogen structure
Glucose to glucose a 1-4 bonds branching on a 1-6 approximately every 10 glucose residues
123
Cellulose structure
Chains of glucose to glucose b 1-4 bonds
124
What type of bond forms between sugars
Glycoside linkage
125
What gene turns off lactase production?
MCM6
126
What is lactase
Enzyme breaks down lactose
127
What is lactose intolerance?
A lactase deficiency caused by MCM6
128
Contain repeating disaccharide chains of a modified glucose and or galactose and compose a large portion of the extracellular matrix
Glycosaminoglycans (GAGS)
129
Mainly polysaccharides with a small percentage <10% protein
Proteoglycan
130
Mainly small proteins with a smmall percentage of carbohydrate
Glycoprotein
131
Essential amino acids
```
Threonine
Valine
Leucine
Isoleucine
Methionine
Phenylalanine
Tryptophan
Histidine
Lysine
```
132
Essential amino acids for childhood
Cysteine
Tyrosine
Argenine
133
Amino acids that prefer to be inside a folded protein
Hydrophobic
134
Amino acids that interact with surrounding water molecules
Hydrophillic
135
Amino acids that prefer to be at the surface of a folded protein or in contact with other charged atoms/molecules
Charged
136
Why is proline speciial
B turns
137
What does cysteine become and why
Cystine, di sulfide bonds
138
Histidine's special properties
4 places to lose a H+
139
Two amino acids that can make b-turns
Cysteine and glycine
140
Four pHs that histidine falls into
Below 1.3
1.3-6.0
6.0-9.3
Greater than 9.4
141
How do proteins bond?
Peptide bonds
They bind between the carboxyl group and the amine group
142
Primary structure
Sequence of amino acids
143
Shapes of the secondary structure
A-helix
B-sheets
DNA does not form an A-helix (Double helix)
144
2' structures fold and interact to form
Tertiary structure
145
Quaternary structure
Multiple protein subunits (monomers)
146
Two structural proteins
Actin and tubulin
147
Tubulin forms a
Dimer
148
Four categories of proteins
Enzymes
Structural proteins
Motor proteins
Transport/channel proteins
149
What optomizes the structure of collagen
Having Glycine as every third amino acid
150
Three typical amino acids in collagen
Glycine, proline, hydroxyproline
151
Genetic disease that affects collagen containing tissues
Osteogenesis imperfecta
152
What causes osteogenesis imperfecta?
Point mutations that destabilize or alter triple helix structure
153
What causes collagen to have a helical structure
Glycine as every third amino acid
154
Cause of scurvy
Vitamin c deficiency
155
S/S scurvy
Abnormal bleeding
Skin diiscoloration
Gum deterioration
Weakening of bones
156
Name one motor protein
Myosin
157
What transports O2?
Myoglobin and hemoglobin
