Biochem Flashcards
(167 cards)
1
Q
helps in the conversion of energy to ATP
A
Thiamin (B1)
2
Q
for energy production, cellular function and metabolism
A
riboflavin (B2)
3
Q
helps in energy conversiin and creatiin and repair of DNA
A
niacin (B3)
4
Q
used to make coenzyme A, for breakdown of fatty acids
A
pantothenic acid (B5)
5
Q
maintain proper levels of the amino acid homocysteine
A
pyridoxine (B6)
6
Q
for healthy hair, skin, nails
A
biotin (B7)
7
Q
for pregnancy
A
folate and folic acid (B9)
8
Q
helps form red blood cells and DNA
A
Cobalamin (B12)
9
Q
inactive enzyme found in the stomach
A
pepsinogen
10
Q
cannot be made by the body; must be from the food
A
essential amino acid
11
Q
bodies can produce
A
non essential amino acids
12
Q
food that can supple all nine essential amino acids
A
complete proteins
13
Q
do not contain adequate anounts of one or more essential amino acids
A
incomplete proteins
14
Q
first step in breaking down food proteins
A
transamination
15
Q
glutamate loses its amino acid, forming ammonium and reforming a ketoglutarate
A
oxidtive deamination
16
Q
building block of proteins
A
amino acids
17
Q
required in the human diet and nit synthesized by the body
A
essential
18
Q
type of structure where most carbonyl grouos of peptide bonds forms a hydrogen bond with the amide nitrogen of another peptide bond
A
alpha helix
19
Q
when the amino acid alanine added to a solution with a ph 7.3, it becomes
A
an anion
20
Q
increasing the solubility of a protein in solution by adding ions
A
salting in
21
Q
local spatial arrangement of a polypeptide backbone atoms without regard to the conformation of its side chain
A
secondary structure
22
Q
more likely to found in a proteins interior away from aqueous solvent molecules (hydrophobic; nonpolar amino acid)
A
Val, Leu, Ile, Met, Phe
23
Q
most likely to reside in the membrane-anchoring domain of a membrane protein
A
isoleucine, valine, ohenylalanine
24
Q
primry stabilizing force of a protein secondary structure
A
hydrogen bonds
25
two types of b-pleated sheets
prallel and antiparallel
26
protein that have a specific chemical structure and function
domains
27
quaternary structure of a proteins
intertwining of two or more polypeptide
28
hemoglobin
4 polypeptide chains: 2 a chains and 2 b chains
29
action of disrupting the 3D shape of protein
denaturation
30
least afftected in protein denaturation
primary structure
31
imino acid froound in the protein structure
proline
32
bonds in the protein structure that are not broken on denaturation
peptide bonds
33
nature of the peptide bond
a partial double bond
34
function of enzyme
catalysts
35
conjugated enzyme
apoenzyme
36
enzyme cofactors that bind covalently at the active site of an enzyme
prodthetic grouos
37
an enzyme active site is the location in an enzyme where substrate molecules
undergo change
38
optimal temperature range for the majority of enzymes
35-40C
39
reactants of an enzyme catalyzed reaction
substrates
40
where binding occurs
active site
41
enzyme catalyzes reactions by
decreasing the free energy of activation
42
apoenzyme
without cofactors
43
NAD+, FAD and FMN are all cofactors for
oxidireductases
44
rate of second order rxn depends on
two substrate
45
site of amino acid catabolism
liver
46
first step in catabolism of amino acids
removal of amino group
47
true about urea
the primary ni trogenous waste products of humans
48
a glucogenic amino acids is one which is degraded to
pyruvate or citric acid cycle internediates
49
transamination
a-amino group is removed fron the amino acid
50
transamination is the transfer of an amino
group from n amino acid to a keto acid
51
rate determining step of michaelic menten kinetics
the complex dissociation step to produce product
52
competitive inhibitor of an enzyme works by
fitting into the enzymes active site of an
53
if n enzyne is described by the michaelis menten, a conpetitive inhibitor will
increase the Km but not change the vmax
54
binds to an enzyme at its active site
reversible competitive inhibitor
55
competitive inhibitor of enzyme
structurally similar to the substrate
56
uncompetitive inhibitor binds to
ES
57
reversible inhibitor that can bind to either E alone
non competitive inhibitor
58
in lineweaver burk plot, conpetitive inhibitor shows
it changes the x intercept
59
non competitive inhibitor of an enzyme catalyzed reaction
decreases vmax, binds to ES
60
classical uncompetitive inhibitor is a compound that binds
reversibly to the enzyme substrate complex yielding an inactive ESI complex
61
some enzymatic regulatiin is allosteric
an enzyme with more than one subunit
62
glucose + fructose
sucrose
63
galactose + glucose
lactose
64
glucose + glucose
maltose
65
glucose and fructose are examples of of
single sugars
66
not a polysaccharide
sucrose
67
more complex sugar
starches
68
what does insulin do
inhibit gluconeogenesis and stimulate glycolysis
69
describe the flow of genetic information ithin biological system
central dogma
70
three structutal subunits of each nucleotides
sugar, heterocyclic base, phosphodiester
71
nucleotides
nucleoside + phospate
72
major energy curency of the cell
ATP
73
guanine
cytosine
74
adenosine
thymine
75
dna coils around a core of proteins
histones
76
DNA + histones
nucleosome
77
nit considered a pyrimidine
guanine
78
base present only in RNA
uracil
79
role of hydrogen bond in the structure of DNA
connect base pairs
80
whise xray work aided watson and crick in discovery of double helix
R. Franklin
81
fragments move most quickly through a gel
small fragments
82
nucleotide bases and aromatic amino acids absorb light at
260 and 280 nm
83
found in RNA but not DNA
uracil
84
true about pairing bases in DNA
purines always pair with pyrimidines
85
both strands of dna serve aa templates concurrently in
replication
86
repairs nicked DNA
dna ligase
87
replication of chrimosmes by eukaryotes occurs in relatively short period of time because
each chromosme contain multiple replicons
88
DNA molecule is precisely synthesized
replication
89
enzymes adds complementary bases during replication
polymerase
90
enzymes unwind short stretches of DNA helix immediately ahead of replication fork
helicases
91
dna plymerase removes RNA primers in DNA synthesis
polymerase I
92
dna replication takes place in which direction
5' to 3'
93
enzyme responsible for proofreading base pairing
dna polymerase
94
5' and 3' related to the
carbon number in sugar
95
main damaging effect of UV radiation on DNA
formation kf thymine dimers
96
enzyme used for synthesis of RNA under direction of DNA
RNA polymerase
97
product of transcription
mRNA
98
RNA bind to amino acid
tRNA
99
recognition/binding site of RNA polymerase
promoter
100
mrna transcript of gene contains
start codon, stop codon, terminator
101
where DNA transcribed into mRNA
nucleus
102
site of protein synthesis
ribosome
103
indicate an active site for protein synthesis
polysomr
104
not necessary for protein synthesis to occur once transcription is completed
DNA
105
during process of translation
peptide is passed from trna in the P site to A site
106
nucleolus of the nucleus is the site where
rRNA is transcribed and ribosomal subunits are assembled
107
ribosome are composed of
proteins and RNA
108
required for protein synthesis
trna, mrna, rrna
109
mRNA binds
to the small subunit
110
ribosomes select the correct tRNAs
solely on the basis of their anticodons
111
amino acids starts all proteins synthesis
methionine
112
macromolecules that does not dissolve in water
lipids
113
monomers of lipids
fatty acids and glycerol
114
lipids function except
enzyme action
115
fats that have fatty acids with only single covalent bonds in their carbon skeleton
saturated
116
polymer
nucleic acid
117
higher melting point
triglyceride containing only stearic acid and glycerol
118
hydrolysis of a triglycerides
fatty acids and glycerol
119
important function of cholesterol
modulate membrane fluidity
120
fat soluble vitamin that regulates blood clot
vit K
121
breaking down of molecules
catabolism
122
123
building up of molecules
anabolism
124
release of energy from glucose compled to ATP synthesis
cellular respiration
125
atp phosphate bond has _ energy
7.3 kcal energy
126
cellular respiration takes place
mitochondria
127
glycolytic pathway regulation involves
allosteric stimulation by adp
allosteric inhibitiin by atp
feedback inhibitiin by atp
128
glycolysis occur
cytoplasm
129
released energy obtained by oxidation of glucose stored as
atp
130
enzymes of glycolysis located in
cytosol
131
atp is from which general category of molecules
nucleotides
132
regulates glycolysis steps
phosphofructokinase, hexose kinase, pyruvate kinase
133
not a mechanism for altering the flux of metabolites
block active sites
134
phophofructokinase is inhibited and activated by
atp and adp
135
biological redox rxn involves
oxidizing agent, gain of electrons, teducing agent
136
coenzyme Q involved jn electron transport as
a lipid soluble electron carrier
137
FAD is reduced FADH2 during
Krebs cycle
138
during glycolysis, electrons removed from glucose are passed to
NAD
139
co2 is primary product of
krebs cycle
140
not oresent during the TCA cycle
O2
141
correct order of stages
glycolysis, pyrivated oxidation, citric acid cycle, oxidative phophorylation
142
products of citric acid cycle
NADH, ATP, FADH2 and CO2
143
krebs cycle begins when pyruvic acid produced by glycolysisi enters
mitochondrion
144
the NADH produced by glycolysis ultimately donates its high energy electrons to
electron transport chains in mitochondiria
145
main purpose of transport chains
convert adp to atp
146
oxidative phosphorylation requires
electron transport system
147
proteins of electron transport chains located
mitochondrial inner membrane
148
atp synthase for most atp synthesis in the body located
inner side of the inner mitochondria membrane
149
final electron acceptor
oxygen
150
functioning anaerobically
lactate
151
glucagon activate what
gluconeogenisis and glycogenolysis
152
not a way of producing ATP in humans
alcohol fermentation
153
aerobic product of pyruvate catabolic metabolism
acetyl CoA
154
TCA cyle
controlled by the ADP/ATP ratio and the NADH concentration
155
hormonal levels is true
after running 20miles, epinephrine and glucagon are high and insulin is low
156
considered umeukryotes
archaea
157
spherical bactera
coccus
158
organism completely dependent on atmospheric oxygen for growth
obligate aerobe
159
organism grows best above 50C
thermophilic
160
food preservation by using salts and sugars works by
creating hypertonic environment
161
using microbes to clean
bioremediation
162
mucus helps in protecting against pathogens by
restricting access to mucosal surfaces
163
production of citric acid
aspergillus niger
164
starvation proteins
stationary phase
165
period between inoculation of bacteria in a culture medium and beginning of multiplcation
lag phase
166
batch fed, substrate is added how
periodically throughout the fermentation
167
