studystack 1 Flashcards
Enzymes, Carbohydrates, Proteins, Amino acids (172 cards)
1
Q
Two major metabolic amino acids from muscle protein degradation?
A
Alanine
Glutamine
2
Q
Which hormone stimulates adipose stores to mobilize?
A
Glucagon
3
Q
Which tissues metabolize glutamine?
A
GUT
Kidney
4
Q
Besides protons, what else can decrease the affinity of HbA for O2?
A
2,3-bisphosphoglycerate (BPG or DPG)
5
Q
At normal pH, amino groups have what charge?
A
Positive
6
Q
Branched chain amino acids.
A
Valine (V)
Leucine (L)
Isoleucine (I)
7
Q
The n-side chain is a common site for what?
A
Glycosylation
8
Q
Positively charged basic molecules
A
Arginine (R)
Lysine (K)
Histidine (H)
9
Q
Bonds that held Cystine.
A
Disulfide bonds
10
Q
Amino acid that causes kinks in the peptide chain.
A
Proline
11
Q
Primary hemoglobin in adults.
A
HbA
12
Q
If the body wants to release oxygen, which form of hemoglobin will it use? If it wants to uptake oxygen?
A
Taut; Relaxed
13
Q
Hexokinase and Glucokinase are what kind of molecules?
A
Isozyme
14
Q
The only site that can reverse or dephosphorylate glucose-6-phosphate and export glucose?
A
Liver
15
Q
Rate limiting enzyme of glycolysis.
A
Phosphofructokinase 1
PFK-1
16
Q
Products of aerobic glycolysis.
A
Pyruvate
17
Q
Products of anaerobic glycolysis.
A
Lactate
18
Q
Site of glycolysis.
A
Cytosol
19
Q
2 requirements for aerobic glycolysis.
A
Oxygen
Mitochondria
20
Q
ATPs produced when using malate aspartate shuttle.
A
5 ATP
21
Q
In hypoxia, what happens to 2,3-BPG in RBC’s?
A
Increases
22
Q
Enzyme that adds phosphate from ATP to a molecule’s hydroxyl group.
A
Kinase
23
Q
Aerobic NADH reoxidation to NAD+ occurs via what process?
A
Oxidative phosphorylation
24
Q
2,3-BPG is produced via?
A
Glycolysis
25
Inorganic component (minerals) essential to make the reaction work
Cofactor
26
Organic component (vitamins) essential to make the reaction work
Coenzyme
27
Complete enzyme: functional enzyme.
Holoenzyme
28
Enzyme missing cofactor or coenzyme.
Apoenzyme
29
Enzyme precursor: Must be converted to active form.
Zymogen
30
Adds water, CO2 or ammonia to doubble bond or removes them from double bond.
Lyase
31
When [s] = km, them Vo = ?
1/2 Vmax
32
When Vo = 1|2 Vmax then [s] = ?
Km
33
If the concentration of substrate [s] is smaller than Km, what is the reaction dependant on?
Substrate
Competitive inhibition
34
When the concentration of substrate is bigger than Km, what is the reaction dependant on?
Non competitive inhibition
35
In Phosphorylation of glycogen phosphorylase, ____ activity
Increases
36
In Phosphorylation of glycogen synthase, ____ activity
Decreases
37
Regulatory enzymes in a cascade (rate limiting). Activator or inmhibitor binds to an allosteric site on the enzyme. Feedback inhibition. Tells the enzyme to speed up or slow down. Act like a noncompetitive inhibitor.
Allosteric Enzymes
38
Two specialized products derived from Tryptophan?
Serotonin, Niacin (NAD, NADP)
39
GABA is derived from which amino acid?
Glutamine
40
One specialized product that uses the entire structure of glycine?
Heme
41
What enzyme combines succinyl-CoA and glycine to start the Heme pathway?
ALA (aminolevulinic acid) synthetase
42
The rate of the reaction at saturation substrate concentrations for a given amount of enzyme.
Vmax
43
The substrate concentration that results in 50% Vmax.
Km
44
Competitive inhibitors ____________ (increase / decrease) the apparent Km.
Increase
45
An inhibitor that binds to, and takes an enzyme out of commission is called a ____________ inhibitor.
Noncompetitive inhibitor
46
NAD is synthesized from what vitamin?
Niacin (B3)
47
FAD is synthesized from what vitamin?
Riboflavin (B2)
48
TPP is what vitamin?
Thiamine (B1)
49
What would competitive inhibition affect km or vmax?
Km
50
In noncompetitive inhibition, what is changed?
Vmax
51
Alzheimer's disease has what specific plaque formation?
Beta amyloid
52
How many CO2 released in TCA?
2
53
When alpha-keto acids enter the TCA cycle what are the final products?
CO2, H2O, ATP
54
Enzyme deficient in Maple Syrup Urine Disease.
Branched-chain Alpha-keto acid dehydrogenase
55
L-glucose and D-glucose are examples of.
Enantiomers
56
Most predominant carbohydrate enantiomer in humans.
D
57
Monosaccharides that have the same chemical formula and different structural formula.
Isomers
58
Monosaccharides that are Epimers at C4.
Glucose and Galactose
59
Monosaccharides that are Epimers at C2.
Glucose and Mannose
60
What is the linkage between a pentose sugar and purine/pyrimidine?
beta-glycosidic linkage
61
Galactose in the lens of children with untreated galactosemia get?
Galactitol formation
62
What kind of sugar is lactose?
reducing sugar
63
What should be avoided in diet in children with Aldolase B deficiency?
Fructose
64
Cellulose composition and linkages.
glucose linked by beta 1-4 glycosidic linkages
65
Describe Vmax and Km for glucokinase vs. hexokinase?
Glucokinase Vmax and Km is higher. than hexokinase
66
Which steps in glycolysis are irreversible?
1) hexokinase/glucokinase
2) PFK-1
3) Pyruvate kinase enzyme reactions
67
Blocks enolase from converting 2 phosphoglycerate into phosphoenol pyruvate in glycolysis.
Fluoride
68
What is the fate of pyruvate in aerobic conditions?
Converted to acetyl CoA by pyruvate dehydrogenase and enters TCA cycle
69
What is the fate of pyruvate in anaerobic conditions?
Converted to lactate by lactate dehydrogenase and goes to liver via Cori cycle
70
Enzyme converts Pyruvate to Lactate.
LDH
71
What happens to the NADH formed in glucose under aerobic conditions?
Each NADH is used in ETC to produce 3 ATP (in malate-aspartate) 2 ATP (in glycerol-phosphate shuttle).
72
What happens to the 2,3 BPG level in people from high altitudes?
Increased
To facilitate unloading of oxygen.
73
What is the second most common form of hemolytic anemia?
Pyruvate kinase deficiency in RBCs
74
What is the most common form of hemolytic anemia?
G6PD deficiency
75
What effect when tumor cells use glycolysis as the main source of ATP
Warburg effect
76
Makes a phosphodiester bond between adjacent nucleotides in DNA.
DNA Ligase
77
The biochemical function of cAMP is to activate _______________.
Protein kinase A
78
Has a high Km for glucose and is active after a big meal.
Glucokinase
79
The enzyme primarily responsible for metabolizing alcohol.
Alcohol dehydrogenase
80
Stimulates the activity of phosphofructokinase-1 (PFK-1).
Fructose 2,6-bisphosphate
81
Rate limiting enzyme in cholesterol biosynthesis.
HMGCoA reductase
82
Catalyzes the first step in glycolysiss that produces ATP by substrate-level phosphorylation.
Phosphoglycerate kinase
83
Synthesizes cAMP
Adenyl cyclase
84
Breaks down cAMP
Phosphodiesterase
85
Precursor of Tyrosine.
Phenylalanine
86
Where is arginine created?
Urea cycle
87
2 Hormones stimulate amino acid uptake into the liver.
Glucagon
| Cortisol
88
Spans the inner membrane, the proton channel
Fo domain
89
Extended out into the matrix, the catalytic subunit
F1 domain
90
Inhibits ATP synthase by binding to the F0 domain thus closing the proton channel, electron transport is halted.
Oligomycin
91
Deficiency in PKU.
Phenyalanine hydroxylase
92
Stimulated by diacylglycerol (DAG) and inositol trisphosphate 3 (IP3)
Protein Kinase C
93
Cleaves phosphodiester bonds
Nuclease
94
Rate-limiting step of the Pentose Phosphate Pathway
Glucose-6-P Dehydrogenase (GPDH)
95
Allow for interconversion of diasteromers
Epimerase
96
Transfers a 3-carbon fragment from one sugar to another
Transaldolase
97
Rate-limiting step of fatty acid synthesis (requires biotin)
Acetyl CoA carboxylase
98
Transfers an electron from NADPH to the heme Fe in P450, reducing the Fe(III) to Fe(II)
Cytochrome P450 reductase
99
Inhibited in Complex I of the ETC.
NADH dehydrogenase
100
Inhibited in Complex III of the ETC.
Cytochrome c reductase
101
Inhibited in Complex IV of the ETC.
Cytochrome oxidase
102
Prevents Phosphoglycerate kinase ATP production
Arsenate
103
Enzyme that overcomes the irreversible pyruvate kinase reaction in glycolysis.
Phosphoenolpyruvate carboxykinase
104
The toxic effects of cyanide are due to _________________.
inhibition of cytochrome oxidase (Complex IV)
105
Enzyme unique to the Pentose Phosphate Pathway
Transketolase
106
An enzyme that removes a phosphate from the substrate.
Phosphatase
107
Where are free amino acids absorbed?
Small intestine
108
How are fructose absorbed?
Facilitated diffusion
109
GLUT 2 can be found in?
Basement membrane
110
Transport found in Luminal membrane.
GLUT 5
111
How many ATP produced in ETC?
30 or 32 ATP
112
Cofactors required in conversion of propionyl CoA to Succinyl CoA. r
Biotin and vitamin B12
113
(+) delta H
Endothermic reaction
114
(-) delta H
Exothermic reaction
115
A molecule with two charges but no net charge.
Zwitterion
116
pH = pKa + (log[A-]/[HA])
Henderson Hasselbalch equation
117
Glucose + Galactose
Lactose
118
Glucose + Fructose
Sucrose
119
Glucose + Glucose
Maltose
120
Essential Fatty Acids
Linoleate and Linolenate
121
Amino acid with no side chain, functions as inhibitory neurotransmitter and inhibited by strychnine
Glycine
122
Infants are unable to utilize oxidized glucose (glucoronic acid) to conjugate the drug chloramphenicol(antibiotic) results in high levels and toxicity
Grey baby Syndrome
123
The spatial arrangement of an organic molecule that is conferred by the presence of either (1) double bonds, about which there is no freedom of rotation, or (2) chiral centers, around which substituent groups are arranged in a specific sequence.
Configuration
124
A spatial arrangement of substituent groups that are free to assume different positions in space, without breaking any bond, because of freedom of rotation
Conformation
125
Compounds that have the same composition and the same order of atomic connections but different molecular arrangements
Stereoisomer
126
Inhibitors that blocks NADH dehydrogenase/complex I.
AMYTAL
Rotenone
Piericidin
127
Inhibitors that blocks complex III by preventing the oxidation of ubiquinol.
Antimycin A
128
reversible inhibitor of cytochrom oxidase, binds to Fe3+ heme group.
Cyanide
129
Compound in rat poison that inhibit aconitase.
Fluoroacetate
130
Found in brain; Highly expressed in erythrocytes and high affinity for glucose
GLUT 1
131
low affinity transporter, liver
GLUT 2
132
high affinity transporter, brain
GLUT 3
133
insulin sensitive, adipose and muscle
GLUT 4
134
main type CT, bone, teeth, encapsulated organs resist force, tension and stretch
type I collagen
135
cartilage resists intermittent pressure
type II collagen
136
found in reticular fibers scaffolding for specialized cells
type III collagen
137
basement membrane and filtration
type IV collagen
138
skin, eye, etc connects basement membrane to ECM
type VII collagen
139
The linear sequence of amino acids.
Primary Structure
140
The association of two or more polypeptides into a multi-subunit complex.
Quaternary Structure
141
Localized organization of parts of a polypeptide chain (e.g., the alpha helix or beta-pleated sheet).
Secondary Structure
142
The overall, three-dimensional arrangement of the polypeptide chain.
Tertiary Structure
143
covalent bond between two cys joining the subunits together
Disulfide bond
144
The result of the misfold is an abnormal haemoglobin (HbS); the switch from Glu to Val causes the cell to want to stabilise (protect the hydrophobic regions) resulting polymerisation
Sickle cell disease
145
Protein that can fold in multiple, structurally distinct ways, at least one of which is transmissible to other prion proteins; found on the surface of cells
Prion
146
21st amino acid; non-coded amino acid; encoded by subset of STOP codons, contains Se instead of S; reduced pKa useful for enzymes in anti-oxidant activity
Selencysteine
147
Carbon attached to the original carbonyl group in cyclic form
Anomeric carbon
148
N-terminal of amino acid
Amino group
149
C-terminal of amino acid
Carboxyl group
150
The only form found in proteins
L-form amino acids
151
Activation energy
ΔG
152
Study of the rate of an enzyme catalysed reaction and how it varies.
Enzyme kinetics
153
Initial reaction velocity, measured as soon as a substrate is mixed; rate of formation of the product.
V0
154
Vo=(Vmax[S])/(Km+[S])
Michaelis-Menton equation
155
Rearranging the Michaelis-Menten equation to the form y=mx+c; 1/Vo = (Km/Vmax[S]) + 1(Vmax); adds graphical value to the constant; can be used to determine the Km and Vmax as well to determine the action of enzyme inhibitors
Lineweaver-Burke plot
156
One of the most common forms of regulation; good way of controlling enzyme activity; sigmoid curve (compared to hyperbolic curve of M-M kinetics); slow to start, but more rapid change that reaches Vmax quicker.
Allosteric regulation
157
Also acts as a positive allosteric regulator of phosphenyolpyruvate to pyruvate (a later step in glycolysis);
Fructose 1,6-bis phosphate
158
Large polymeric oligosaccharides, formed by the linkage of multiple monosaccharides are called
Polysaccharides
159
What is the simplest aldose sugar?
Glyceraldehyde
160
The interconversion of alpha and beta forms of a sugar (which occurs slowly in a solution) and leads to an equilibrium mixture of the two forms.
Mutarotation
161
Shape of the graph of the Michaels-Menten equation.
Hyperbolic
162
What is the relationship between the Michaels-Menten equation and the Lineweaver-Burk equation?
The LBE is a double reciprocal equation of the MME so as to give a linear graph to correctly identify the Km and Vmax.
163
Vmax is unaffected but Km is increased.
Competitive inhibition
164
Vmax is decreased but Km is decreased.
Uncompetitive inhibition
165
Km is unaffected but Vmax is decreased.
Non-competitive inhibition
166
Interactions are the most important in the folding of the peptide chain.
Hydrophobic
167
Independent folding region that allows 1 protein to have multiple functions. Each domain has a specific function.
Domain
168
Aid in protein folding during synthesis. They also prevent misfolding and protein aggregation
Chaperones
169
What is ATP cleaved to for liberating energy?
ADP and Pi
170
Final electron acceptor.
Oxygen
171
Where does oxidative phosphorylation occur?
Inner Mitochondria
172
The largest complex in the chain.
Complex I: NADH-Q Oxidoreductase.
