Biology and Biochemistry Flashcards

1
Q

competitive inhibition

A

binding site: active site
impact on Km: increases
impact on Vmax: none

*can be overcome by increasing the substrate concentration, so Km will increase (more substrate needed to reach 1/2 Vmax)

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2
Q

noncompetitive inhibition

A

binding site: allosteric site
impact on Km: no change
*active enzyme still has same affinity for substrate
impact on Vmax: decreases
*less enzyme available to react due to allosteric site

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3
Q

mixed inhibition

A

binding site: allosteric site
impact on Km: increases or decreases
impact on Vmax: decreases

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4
Q

uncompetitive enzyme

A

binding site: enzyme-substrate complex
impact on Km: decreases
impact on Vmax: decreases

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5
Q

catalytic efficiency

A

kcat/Km

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6
Q

lower Km means

A

higher enzyme affinity for a substrate

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7
Q

order of circulation

A
superior and inferior vena cava
right atrium
(tricuspid valve)
right ventricle
pulmonary arteries
lungs
pulmonary veins
left atrium
(bicuspid/mitral valve)
left ventricle
aorta
body
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8
Q

blood buffer equation

A

CO2 + H2O ⇌ H2CO3 ⇌ H+ + HCO3-

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9
Q

veins

A

carry blood low in oxygen to the heart

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10
Q

arteries

A

carry oxygen rich blood to body

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11
Q

Vmax is limited

A

if all active sites of enzyme are occupied, adding more substrate does not increase the reaction rate

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12
Q

prokaryote cell wall (gram positive or gram negative)

A

gram positive –> purple : thick layer of peptidoglycan

gram negative –> pink/red : thin, less peptidoglycan

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13
Q

plasmids

A

carry DNA that is no necessary for the survival of prokaryote

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14
Q

binary fission

A

asexual reproduction in prokaryotes

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15
Q

genetic recombination

A

transformation, transduction, and conjugation
integration DNA into genome
-antibiotic resistance
-virulence factors

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16
Q

transformation

A

integration of foreign genetic material into the host genome

gram negative rods

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17
Q

conjugation

A
2 cells form a conjugation bridge to transfer genetic material
donor male (+) and recipient female (-)
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18
Q

transduction

A

virus transfers genetic material from one bacterium to another
ex: bacteriophages

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19
Q

viruses

A

DNA or RNA
do not have the ribosomes
must express and replication genetic info within the host cell

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20
Q

bacteriophages

A

viruses that target bacteria by injecting their genetic material

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21
Q

positive sense

A

genome may be directly translated to functional proteins by ribosomes of host cell (like mRNA)

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22
Q

negative sense

A

template

*carry RNA replicase so complementary strand can be synthesized

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23
Q

retroviruses

A

single stranded RNA viruses

reverse transcriptase –> synthesizes DNA from SS RNA –> integrated into host genome –> replicated and transcribed

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24
Q

lytic life cycle

A

virulent

maximize cell’s functions, no regard for host cell survival

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25
Q

lysogenic cycle

A

viral genes integrated into host genome

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26
Q

prion

A

infectious protein

causes misfolding of protein

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27
Q

viroids

A

small pathogens with short circular SS RNA

no protein

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28
Q

glucogenic amino acid

A

all but leucine and lysine

can be converted into glucose through gluconeogenesis

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29
Q

ketogenic amino acids

A

leucine, lysine, isoleucine, phenylalanine, threonine, tryptophan, tyrosine
converted into acetyl CoA and ketone bodies

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30
Q

ketone bodies

A

transportable forms of acetyl CoA
produced by liver
used by other tissues during prolonged starvation

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31
Q

ketolysis

A

breakdown of ketone bodies
when: during prolonged fast (brain!!)

(pyruvate dehydrogenase is inhibited so glycolysis and glucose uptake decreases to spare essential proteins)

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32
Q

acetyl CoA and oxaloacetate form …

A

citrate

when: beginning of citric acid cycle

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33
Q

Beta oxidation

A

reverse of fatty acid synthesis
*oxidizing and releasing molecules of acetyl CoA
each 4 step cycle releases 1 acetyl CoA and reduces NAD+ and FAD

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34
Q

importance of acetyl CoA (B oxidation producing it)

A
  • it enters the citric acid cycle in muscle
  • in the liver, it stimulates gluconeogenesis by activating pyruvate carboxylase
  • use it to synthesize ketone bodies
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35
Q

types of enzymes

LIL’ HOT

A

Lyase
Isomerase
Ligase

Hydrolase
Oxidoreductase
Transferase

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36
Q

lyases

A

cleavage of single molecule into two products

NO WATER

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37
Q

isomerases

A

rearrangement of bonds

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38
Q

ligases

A

addition or synthesis reactions, requires ATP

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39
Q

hydrolase

A

breaking with water

phosphatase, cleaves phosphate group

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40
Q

oxidoreductase

A

redox reactions

“dehydrogenase”

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41
Q

transferase

A

movement of functional group

kinases: transfer or phosphate

42
Q

cofactors (coenzymes)

A

bind to active site of enzyme and participate in catalysis of reaction
inorganic molecules or metal ions
(vitamins, NAD+, FAD, coenzyme A)

43
Q

high kcat and low Km

A

high turnover (substrate ==> products) and high substrate affinity means higher catalytic efficiency

44
Q

kcat

A

number of substrate molecules “turned over” or converted to product

45
Q

gel electrophoresis

A

separate macromolecules, like DNA and proteins, by size and charge
DNA molecules are negatively charged and migrate toward anode

larger molecules move less

46
Q

SNOW DROP

blots

A

Southern: DNA
Northern: RNA
Western: Protein

47
Q

triaglycerols

A
  • energy storage and insulation
  • carbon atoms are more reduced so oxidation yield twice as much energy
  • hydrophobic –> do not require water for stability
48
Q

saturated fatty acids

A

only single bonds, solid at room temp (greater van der Waals forces)

49
Q

unsaturated fatty acids

A

double bonds –> kinks –> liquid at room temp

50
Q

myelin

A

insulator –> maintains electrical signal within a neuron

increases speed of conduction

51
Q

liver

A

production of bile (stored in gallbladder)
production of urea
synthesis of albumin (bile salts, pigments, cholesterol)
clotting factors
detoxification of chemicals
processing and synthesis of nutrients

52
Q

alveoli

A
  • gas exchange with capillaries
  • lungs –> bronchi –> bronchioles –> alveoli

-blood has low partial pressure of oxygen and high partial pressure of carbon dioxide when it reaches alveoli (TRANSFERRED DOWN CONC GRADIENT)

53
Q

capillaries

A
  • single endothelial layer
  • diffusion of gases, nutrients, wastes
  • allow endocrine signals to arrive at target tissues
54
Q

thyroid hormone

A

TSH –> thyroid –> T3 and T4 (stimulate metabolic activity)

calcitonin (decrease blood calcium concentration)

55
Q

hypothalamus

A

controls pituitary

negative feedback

56
Q

hypothalamus releases

  • GnRH
  • GHRH
  • TRH
  • CRF
A

anterior pituitary releases

  • FSH and LH
  • growth hormone
  • thyroid stimulating hormone
  • ACTH
57
Q

products of anterior pituitary

A
FLAT PEG
(tropic)
FSH
LH
ACTH
TSH
(direct)
Prolactin
Endorphins
GH
58
Q

direct hormones example

A

insulin, prolactin, endorphins, growth hormone

59
Q

tropic hormones

A

require intermediary

60
Q

peptide amino acids hormones

A

ex: ADH, insulin
charged, cannot pass through membrane, so bind to extracellular receptor

first messenger –> binds to receptor and signals second messenger (signaling cascade)

RAPID, SHORT LIVED
WATER SOLUBLE

61
Q

second messengers examples

A

cAMP, IP3, and calcium

62
Q

activation of G protein-coupled receptor

A

activate or inhibit adenylate cyclase –> increase or decrease cAMP
cAMP binds to intracellular targets like protein kinase A
this phosphorylates transcription factors

63
Q

steroid hormones

A

can cross cell membrane
intracellular receptor –> conformational change (dimerization)
SLOW, LONG-LIVED
NOT WATER SOLUBLE

64
Q

amino acid derived hormones

A

2 methods
bind to G protein-coupled receptor –> epinephrine, norepinephrine (FAST)
intracellularly bind (SLOW) –> thyroid hormones

65
Q

functions of proteins involved in muscular contraction:

myosin, actin, troponin

A

myosin: motor protein, hydrolyzes ATP
actin: motor activity but does NOT hydrolyze ATP
troponin: chaperone of actin, activity modulated by calcium

66
Q

vector

A
  • bacterial or viral plasmids that can be transferred to host after adding DNA of interest
  • too large to be inserted into sequence
  • not super precise
67
Q

initiation of skeletal muscle contraction

A

where: neuromuscular junction
acetylcholine binds to receptors on sarcolemma –> depolarization
action potential travels down sarcolemma to T-tubules
travels down T-tubules to muscles tissues (sarcoplasmic reticulum)

68
Q

heteroplasmy

A

variation in mitochondrial composition of DNA

*result of self-replication and cell division by mitochondria

69
Q

transposons

A

genetic elements that can insert or remove themselves from genome

70
Q

most negative free energy

*K, reduction potential (E^o)

A

position reduction potential

K >1

71
Q

ADH

A

makes you pee less

*increases reabsorption of water in collecting duct

72
Q

increased blood volume leads to _____ blood pressure

A

increased

73
Q

glomerular filtration rate

A

rate at which kidneys filter blood

- pressurized blood enters glomerulus

74
Q

osmotic pressure

A

“pulling” force on water into blood due to presence of solutes

75
Q

hydrostatic pressure

A

“pushing” force on water out of blood due to presence of more fluid
*larger volumes of fluid = higher hydrostatic pressure

76
Q

in artery, hydrostatic pressure is ______

A

high

drives fluids out of capillaries into tissues

77
Q

in vein, hydrostatic pressure is _____

A

low

water has been lost

78
Q

aldosterone

A

acts on distal convoluted tubule and collecting duct

increases reabsorption of Na+ and water and secretion of K+

79
Q

gluconeogenesis is ______ by glucagon and ______ by insulin

A

stimulated by glucagon

inhibited by insulin

80
Q

chaperone proteins

A

assist in folding of proteins, prevent nonfunctional aggregates from forming

81
Q

what is the role of calcium in myosin-actin binding during muscle contraction?

A

calcium binds to troponin, which allows tropomyosin to move, allowing myosin and actin to interact

82
Q

how can you reduce the action potential transmission?

A

increase neuron-firing threshold

influx of anions (hyperpolarizes neuron)

83
Q

how to measure activity of Na+ K+ ATPase?

A

rate of ATP hydrolysis
rate of ADP production
change in ion concentration

84
Q

how many Na+ and K+ ions are pumped across membrane, and which direction?

A

3 Na+ out of the cell

2 K+ into the cell

85
Q

how do enzymes alter rate of chemical reactions?

A
  • co-localizing substrates
  • altering local pH
  • altering substrate shape
86
Q

what is the role of endothelial cells?

A

they are in direct contact with blood

gas exchange!

87
Q

action potential steps

A
  1. stimulus causes cell to depolarize toward threshold potential
  2. if threshold reached, voltage-gated Na+ channels open and membrane depolarizes
  3. at peak, K+ channels open and K+ leaves cell, Na+ channels close
  4. membrane becomes hyperpolarized as K+ leaves cell (membrane enters refractory period where it cannot fire)
  5. K+ channels close and Na+/K+ pump restores resting potential
88
Q

what is depolarization?

A

when membrane potential increases

89
Q

what channels open as a result of depolarization?

A

voltage-gated calcium channels open, influx of calcium leads to release of neurotransmitter

90
Q

GLUT 1

A

brain and erythrocytes

high affinity for glucose (low Km) –> insulin independent

91
Q

GLUT 2

A

liver and pancreas

lower affinity for glucose (high Km) –> insulin independent

92
Q

GLUT 3

A

brain

high affinity for glucose (low Km) –> insulin independent

93
Q

GLUT 4

A

muscle, adipose, heart
medium affinity for glucose
INSULIN DEPENDENT

94
Q

NADPH

A

important for biosynthesis of fatty acids and cholesterol

electron donor

95
Q

NADH

A

high-energy carrier
electron acceptor
ETC to indirectly produce ATP

96
Q

tight junctions

A

prevent solutes from leaking

restrict passage of solutes

97
Q

reduction potential

A

likelihood of being reduction

how much oxidizing agent wants to take electrons

98
Q

for galvanic and electrolytic cells: electrons go from _____ to ______

A

anode to cathode

99
Q

what is the function of salt bridges in the electrolytic/galvanic cells?

A

allow counter ions not involved in the reaction to balance out the charges

100
Q

cations move to the

A

cathode

101
Q

anions move to the

A

anode