BIOCHEM Flashcards
1
Q
aliphatic means:
A
nonaromatic
2
Q
how many H bonds does C (cytosine) make with G (guanine)
A
3
3
Q
how many H bonds does T (thymine) make with A (adenine)
A
2
4
Q
adding more bonds to H
A
reduction
5
Q
adding more bonds to oxygen
A
oxidation
6
Q
a kinase is an example of what type of enzyme
A
transferase
7
Q
a polymerase is an example of what type of enzyme
A
transferase
8
Q
pepsin is an example of what type of enzyme
A
hydrolase
9
Q
enzyme that switches arrangement of atoms within a molecule
A
isomerase
10
Q
synthatase is an example of what type of enzyme
A
ligase
11
Q
enzyme that requires ATP to function
A
ligase
12
Q
cofactors/coenzymes present with enzyme
A
holoenzyme
13
Q
cofactors/coenzymes not present with enzyme
A
apoenzyme
14
Q
inorganic metal ions
A
cofactors
15
Q
organic (vitamins)
A
coenzymes
16
Q
inactive form of an enzyme
A
zymogen
17
Q
metabolic pathways that take place in the mitochondria:
A
TCA, beta oxidation, and ETC
18
Q
the site of synthesis of proteins and other molecules, such as lipids or hormones, that are destined for secretion by the cell
A
ER
19
Q
sorts and adds modifications to molecules created by the ER, but it does not participate in protein synthesis
A
Golgi apparatus
20
Q
bond that forms with polar head to fatty acid tails in phospholipids
A
phosphodiester bonds
21
Q
difference b/t phenylalanine and tyrosine
A
phenylalanine: benzene ring in side chain
tyrosine: benzene ring plus -OH making it a phenol in side chain
22
Q
non-functional tRNA would cause what
A
no proteins to be made
23
Q
the presence of more than one mtDNA type in an individual
A
heteroplasmy
24
Q
insert and remove themselves from a genome; when removed, gene function is restored
A
transposons
25
cleaves proteins
proteases
26
less protein in blood meaning a decrease in osmotic pressure
hypoalbuminemia
27
lactose is a mono or disaccharide
disaccharide
28
NADPH a reducer or an oxidizer
reducer; so less of this would mean more oxidation
29
is ATP hydrolysis coupled in glycolysis
absolutely
30
bonds that require stronger bonds than H bonds (disulfide)
irreversible bonds
31
enzyme involved in DNA replication and transcription that also helps with helicases function
topoisomerase
32
transcriptional regulatory sequences that function by enhancing the activity of RNA polymerase at a single promoter site
enhancers
33
what decreases transcription of genes
DNA methylation (think heterochromatin-very methylated)
34
an inducible system; inducer binds to repressor
lac operon
35
a repressible system; blocks transcription
trp operon
36
peptide bonds are also known as
amide linkages
37
located in nucleolus and synthesizes rRNA
RNA polymerase I
38
located in nucleus and synthesizes hnRNA and snRNA and is the main player in transcribing mRNA
RNA polymerase II
39
located in nucleus and synthesizes tRNA
RNA polymerase III
40
mRNA is derived from ____ via posttranscriptional modifications
hnRNA
41
rate limiting enzyme for glycolysis
PFK-1
42
3 irreversible steps in glycolysis:
1, 3, 10
43
3 enzymes involved in the irreversible steps of glycolysis:
step 1: hexokinase
step 3: PFK-1
step 10: pyruvate kinase
44
Net gain at end of glycolysis:
2 NADH
2 ATP
2 pyruvate
45
any step in TCA cycle that produces a NADH or FADH2 uses what kind of enzyme
dehydrogenase
46
rate limiting enzyme for TCA cycle:
isocitrate dehydrogenase
47
Net gain after TCA cycle:
6 NADH
2 FADH2
2 GTP
48
electron donors in ETC:
NADH and FADH2
49
electron acceptor in ETC:
oxygen
50
what complex along ETC does not pump protons to IMS
complex II
51
ATP synthase on ETC uses what to have a conformation shift to eventually make ATP
chemiosmotic coupling (flow of protons with conformational shift)
52
rate-limiting enzyme in glycogenolysis
glycogen phosphorylase
53
does glycogenolysis use branching or debranching enzyme
debranching
54
2 main things used in glycogenesis
glycogen synthase
| branching enzyme
55
irreversible enzymes used in gluconeogenesis
step 1: pyruvate carboxylase
step 3: fructose 1,6-bisphosphatase
step 10: glucose-6-phosphatase
56
rate limiting enzyme in gluconeogenesis
fructose 1,6-bisphosphatase
57
total amount of ATP produced after TCA cycle and ETC
30-32
58
Acetyl-CoA- malonyl CoA- palmitic acid (16 C)
fatty acid synthesis
59
rate limiting enzyme of fatty acid synthesis
acetyl-CoA carboxylase
60
reducing agent in fatty acid synthesis
NADPH
61
how many NADPH used to make 16 C palmitic acid
14
62
what gets fatty acids into matrix
carnitine
63
breakdown of fatty acids to Acetyl-CoA
beta-oxidation (in matrix)
64
how many acetyl CoAs for a 16 carbon fat that is broken down
8
65
point of TCA cycle
produce NADH and FADH2
66
point of beta-oxidation
reduce Acetyl-CoA to enter into TCA cycle
67
breakdown what to put glucose back in blood
glycogen
68
a way to move Acetyl-CoA in the blood
ketogenesis (ketone bodies from beta-oxidation)
69
what happens when you synthesize triacylglycerol?
you can store fatty acids
70
2 reactions not in mitochondria
gluconeogenesis
| glycolysis
71
how many ATP from 2 turns of TCA cycle
20
72
all amino acids have chiral alpha carbon except
glycine
73
2 amino acids have a chiral carbon in side chain:
threonine and isoleucine
74
AA with an ionizable side chain
histidine (imidazole ring- N atom that can be protonated)
75
Amino acids that are both ketogenic and glucogenic:
tryptophan, phenylalanine, tyrosine, isoleucine, threonine (FITTT)
76
ketogenic amino acids:
leucine and lysine
77
glucogenic amino acids:
13 remaining amino acids that aren't ketogenic and aren't both
78
amino acids that can be converted into ketone bodies are called
ketogenic
79
amino acids that can be converted into glucose are called
glucogenic
80
this gel disrupts disulfide bonds and would show 2 bands instead of 1 if molecule contains these bonds
reducing gel
81
this gel disrupts non-disulfide interactions, so when there is a smaller band produced with half the weight, it consists of a homodimer (2 identical subunits)
SDS page
82
phosphorylation occurs on these AA's due to their hydroxyl group on side chain
serine, threonine, and tyrosine
83
ending of enzymes involved in redox reactions:
-oxidase, -reductase, -dehydrogenase, -monooxygenase
84
why must FAD/FADH2 be bound to enzymes?
b/c it can exist as a semiquinone and if bound to enzymes it won't easily react with oxygen
85
molecule that contains an imine (C=NH) and a carboxyl group
imino acid
86
why can a reaction that is spontaneous under standard conditions also run in reverse
cell alters conc. of substrates (reactants)
87
amine to amide when amine group acts as a ___ in a rxn
nucleophile
88
amines vs. amides
amides have carbonyl group attached to N atom
89
only AA that does not have a beta carbon
glycine
90
polypeptides are named how?
N terminus to C terminus
91
a type of fat that contains double bonds and is therefore considered unsaturated
trans fat
92
which phosphates on ATP get transferred to other molecules by a kinase
gamma- phosphate
93
why G-C causes higher melting temp. of DNA rich in GC content
stronger pi stacking interactions than A-T
94
under anaerobic conditions, how many ATP are produced from 1 mole of glucose
2 ATP
95
originate from centrosomes
microtubules
96
4 fused rings indicative of...
steroid
97
Keq for DNA unfolding
Keq= unfolded/native
98
this muscle fiber type uses more mitochondria and is used for aerobic activity
slow twitch muscle fiber
99
under low oxygen conditions (hypoxia), glycolysis works but oxidative phosphorylation won't so how do you allow glycolysis to proceed?
NADH converted back to NAD+ through lactic acid fermentation
100
if an inhibitor is able to have an effect on an enzyme for 7 days, what kind of inhibition does it have?
irreversible
101
high Km means two things:
lower affinity and decreased reaction rate
102
cytochrome P450 acts as what
monooxygenase- it oxidizes substrates
103
function of a carboxylase
add a carboxyl (COO-) group to molecule
104
ATP consumption and production during glycolysis
2 ATP consumed; 4 ATP produced
105
least suitable for a vaccine
toxicity
106
large subunit of prokaryote ribosome
50S
107
intact prokaryotic ribosomes
70S
108
large subunit of eukaryotic ribosome
60S
109
intact eukaryotic ribosome
80S
110
D54 residue means what
aspartate residue (D)
111
K54 residue means what
lysine residue (K)
112
separates molecules based on electrophoretic mobility; relying on length, conformation change, charge
Native PAGE
113
separates proteins only on the basis of their size
Gel Filtration Chromatography
114
weight of amino acid
110 Da
115
cocaine (a stimulant) would have a physiological effect similar to what that would increase what metabolism
stress; increase glucose metabolism
116
important enzyme that produces NADH in glycolysis
glyceraldehyde-3-phosphate dehydrogenase (makes sense b/c ending in dehydrogenase means producing either FADH2 or NADH)
117
what enzymes perform substrate level phosphorylation during glycolysis
3-phosphoglycerate kinase and pyruvate kinase
118
main purpose of TCA cycle
oxidize acetyl-CoA to CO2 and produce GTP and NADH and FADH2 for ETC
119
rate limiting enzyme of Pentose Phosphate Pathway (PPP)
glucose-6-phosphate dehydrogenase
120
chylomicrons, VLDL, IDL, LDL, and HDL transport what
lipids
121
key enzyme in cholesterol biosynthesis
HMG-CoA reductase
122
the only fatty acid that humans can synthesize
palmitic acid
123
brain uses what metabolism normally? but if it's in prolonged starvation, it uses what
glucose; and then uses ketolysis (ketone bodies)
124
what is the shape of graph for normal MM kinetics with graph of Vo vs. substrate concentration [S]
hyperbolic
125
used to describe the rate-limiting step of catalysis under SATURATING conditions of substrate
kcat
126
what does Hill Coefficient do
tells us if something exhibits cooperativity or not
127
Hill coefficient greater than 1 means
it will exhibit cooperativity
128
these bind the enzyme and the enzyme-substrate complex with the same affinity; vmax decreases but Km remains unchanged
noncompetitive inhibitors
129
AA's that have amide group in their side chains
glutamine and asparagine
130
deamidation reaction releases what
NH3
131
separates proteins based on isoelectric point; needs to have a stable pH gradient established
isoelectric focusing
132
this nucleotide contains 2 rings and 1 carbonyl
guanine
133
this nucleotide contains 2 rings with no carbonyl
adenine
134
this nucleotide contains 1 ring with 1 carbonyl
cytosine
135
this nucleotide contains 1 ring with 2 carbonyls
thymine
136
higher affinity corresponds to a higher or lower Kd (Km)
lower Kd (Km)
137
hormone that is hydrophilic and soluble in blood
peptide hormone
138
interactions that contribute to stabilization of protein structure
disulfide, hydrogen bonds, and salt bridges
139
what attaches nucleotides together but is NOT used to stabilize protein structure
phosphodiester bonds
140
inhibitor that binds to their target enzymes only when the substrate is first bound (only binds to enzyme-substrate complex); both Km and vmax decrease
uncompetitive inhibitor
141
inhibitor that binds active site but doesnt allow reaction to proceed forward
irreversible inhibitor
142
if someone is hypoglycemic, what needs to be produced more in order maintain homeostasis
consume more glucose; b/c our body usually breaks down glycogen into glucose, so with low levels of glycogen, there will be low levels of glucose
143
without acetylcholine receptors, what won't occur
depolarization
144
what tissue produces fatty acids, glucose, and ketone bodies
adipose tissue
145
location on chromosome where certain genes are known to be located; where alleles are for a gene
locus
146
a type of frameshift mutation that usually produces nonfunctional protein, but if inserted towards end of gene, could potentially produce functional protein
insertion mutation
147
methylation increases or decreases stability
increases
148
stability of DNA and RNA is largely dependent on what
amount of GC pairs
149
melting temperature (Tm) definition
point when 50% of molecules have been denatured
150
in aqueous solution, what areas will tend to aggregate together so that polar areas will have maximal contact with one another/the solution
hydrophobic
151
1 amino acid weight in Da
110 Da
152
when dealing with melting point, what do you look at on amino acids compared to other molecules?
Look at both NH2 and COOH- those alone contribute to interactions that would lead to higher melting point than say a ethanol; don't just look at side chain
153
only alters rate and activation energy; not Gibbs or delta H
enzyme
154
disruption of protein complex means breaking of which bonds
H bonds (second, tert, quat structures)
155
structure that has deoxyribose and purine
ATP
156
structure that has ribose and pyrimidine
UTP
157
more CO2 produced does what to blood
lowers pH of blood
158
in the endosymbiotic theory, mitochondria were said to resemble prokaryotic or eukaryotic origin
prokaryotic
159
what makes erythrocytes a good model to study plasma membranes
their simple structure; no organelles or nucleus
160
at the active site of enzyme, polar molecules are attracted to what molecules on substrate binding site
polar; and vice versa for nonpolar
161
at the active site of enzyme, positive charges are attracted to what charges on substrate binding site
negative
162
at the active site of enzyme, hydrophobic amino acids attract what on substrate binding site
hydrophobic amino acids; and vice versa with hydrophilic
163
where does fatty acid oxidation occur
cytoplasm
164
ACTH released by anterior pituitary to increase what hormone production
cortisol
165
Complex I of ETC is reduced by what; then it reduces what
reduced by NADH; then reduces coenzyme Q
166
Complex II of ETC is reduced by what; then it reduces what
reduced by FADH2; then reduces coenzyme Q
167
Complex III is reduced by what; then reduces what
reduced by coenzyme Q; then reduces cytochrome c
168
Complex IV is reduced by what; then reduces what
reduced by cytochrome c; reduces oxygen
169
in the absence of oxygen, will the amount of acetyl-CoA increase or decrease and why
decrease; b/c products of glycolysis will favor lactic acid fermentation
170
at pH of 7, how many protons do carboxylic acids and phosphate groups lose?
carboxyl loses 1; phosphate group loses 2 if it has 2 OH's attached
171
if blood pH is higher, the conc. of what is lower and does acid dissociate?
conc. of H+ is lower; but acid will dissociate
172
a gene being continuously expressed is found in hetero or euchromatin?
euchromatin
173
fatty acid structure: head and tail
head: carboxyl group
tail: long hydrocarbon chain
174
from endo and mesoderm
bladder
175
interactions of amino acids w/ OPPOSITE CHARGE where atleast 2 heavy atoms lie within a hydrogen bonding distance
salt bridge
176
as pH rises, what usually happens, protonation or deprotonation
deprotonation
177
3 monosaccharides to know
glucose, fructose (5 membered ring), galactose
178
3 disaccharides to know
lactose, sucrose, maltose
179
crumpling proteins up into specific tertiary or quaternary structures does what to water molecules
maximizes the freedom of water molecules to move
180
what denatures a protein's tertiary and quaternary structure?
pH; b/c deals with ionic bonds (+ and - charges)
181
what denatures the secondary, tertiary, and quaternary structures of proteins
temp, chemicals, and
182
denaturation does not disrupt what structure of a protein?
primary
183
alpha helix breakers
glycine and proline
184
cysteine is in its reduced form intra or extracellularly
intracellularly
185
cystine is in its oxidized form intra or extracellularly
extracellularly
186
what amino acid can form a covalently bonded dimer
cysteine; disulfide bridge
187
cooperative processes have what shape curve
sigmoidal
188
using Native PAGE and SDS-PAGE, how many bands will you see if you use a homodimer and why
1 band for both; you would think you would see two b/c its a dimer..but you won't b/c since it's "homo", the two dimers have the same weight and therefore would occupy position of one single band
189
complex formed b/t 2 substrate molecules and an enzyme
ternary complex
