Chapter 1 Flashcards
(114 cards)
1
Q
hydrolysis
A
how most macromolecules are broken apart
2
Q
dehydration
A
how most molecules are formed
3
Q
lipid
A
any biological molecule that has low solubility in water and high solubility in nonpolar organic solvents
4
Q
6 types of lipids
A
fatty acids, triacyglyceroles, phosopholipids, glycolipids, steroids and terpenes
5
Q
fatty acids
A
long chains of carbons, COOH at the end
6
Q
saturated fatty acids
A
contain only single carbon-carbon bonds
7
Q
unsaturated fatty acids
A
1 or more C-C double bonds
8
Q
fatty acid oxidation
A
liberates large amounts of chemical energy for a cell
9
Q
fats reach cells as
A
fatty acids
10
Q
triacylglyercols/triglycerides
A
3 Carbon backbone called glycerol, which is attached to 3 fatty acids
11
Q
adipocytes
A
(fat cells), specialized cells whose cytoplasm contains almost nothing but triglycerides
12
Q
phospholipids
A
glycerol backone, polar phospate group replaces one one of the fatty acid – phosphate group at the opposite side of the glycerol
13
Q
amphipathic
A
one end polar, one end non polar
14
Q
glycolipids
A
1 or more carbohydrates attached to the 3 carbon glycerol backbone
15
Q
steroids
A
4 ringed structures
16
Q
terpenes
A
vitamin A
17
Q
lipoproteins
A
how lipids are transported in the blood, have a hydrophobic core and a hydrophilic shell
18
Q
proteins/poly peptides
A
chain of aminoacids, linked together by peptide bonds
19
Q
essential amino acids
A
cannot be produced in the body (10 of them)
20
Q
digested proteins
A
reach cells as single amino acids
21
Q
primary structure
A
and sequences of amino acids in a polypeptide
22
Q
alpha helix
A
single chain of AA twist itself into
23
Q
beta pleated sheet
A
AA chains lie along itself, lie parallel or antiparalled
24
Q
secondary structure
A
alpha helix and beta sheets, contribute to the conformation of the protein, reinforced by hydrogen bonds between the carbonyl oxygen and the hydrogen on the amino group
25
teritary structure
3D shape formed when peptide chain curls and folds
26
5 forces that contribute to teritary structure
covalent disulfide bonds, electrostatic interaction, hydrogen bonds, van der Waals forces, hydrophobic side chains
27
quaternary structure
2 or more polypeptides bound together
28
proline
induces ftursn in the polypeptide disrupt both alpha helix and beta pleated sheet formation
29
denatured
when protein conformation is disrupted
30
globular proteins
enzymes, hormones, membrane pumps and channels, membrane receptors, osmotic regulators, intra and intercellular transport and storage
31
structural proteins
maintain and add strength to cellular and matrix structure
32
glycoproteins
proteins with carb groups attached
33
see nitrogen
think protein
34
cytochromes
proteins that require a prosthetic heme group in order to function
35
carbohydrates
made from carbon and water
36
six carbon carbohydrate
glucose
37
glucose
essentilaly all digested carbs reaching body cells have been converted to ____ by the the liver or enterocyes
38
alpha glucose
hydroxyl group on the anomeric carbon and the methoxy group are on opposite sides of the ring
39
beta glucose
hydroxyl group and methoxy group are on the same side of the carbon ring
40
enough ATP glucose is polymerized to the polysaccharide
glycogen or converted to fat
41
glycogen
found in all animal cells, large amounts in muscle and liver cells
42
liver cells
capable of reforming glucose from glycogen and releasing back into blood stream
43
cells capable of absorbing glucose against concentration gradient
certain epithelial cells in the digestive tract and the proximal tubule of the kidney (done via secondary active transport)
44
how cells absorb glucose
facilitated diffusion
45
without insulin only ____ and ___ are capable of absorbing sufficient amounts of glucose via facilitated transport system
neural and hepatic cells
46
plants form __ and ___ from glucose
starch and cellulose
47
types of startch
amylose and amylopectin
48
amylose
isomer of cellulose that may be ranched or unbranched, same alpha linkages as glycogen
49
amylopectin
resembles glycogen has a different branching structure
50
cellulose
beta linkages
51
most animals
only have enzymes to digest alpha linkages of starch and glycogen
52
nucleotides
5 carbon sugar, nitrogenous base, phosphate group
53
polymers of nucleotides
nucleic acids -- DNA and RNA
54
nucleotides joined together by
phosphodiester bonds btwn phosphate group of one nucleotide and 3rd carbon of the pentose of the other nucleotide forming long strands
55
nucleotides written
5' --> 3'
56
DNA
two strands joined together by hydrogen bonds to make double helix
57
2 h bonds
adenine and thymine
58
3 h bonds
cytosine and guanine
59
DNA is written
top strand -- 5' --> 3' ; bottom strand 3' --> 5'
60
RNA
single strand, uracil replace thymine
61
important nucleotides
ATP, cyclic AMP, NADH, FADH2
62
minearls
dissolved inorganic ions inside and outside the cell, assist transport of substances entering and exiting cells by creating electrochemical gradient, also act as cofactors
63
enzymes
globular proteins, act as catalyst, don't change eq of a reaction
64
substrates
reactants upon which an enzymes works
65
active site
position on the enzymes where substrate binds
66
enzyme-substrate complex
enzyme bound to substrate
67
enzyme specificity
enzymes only work on a specific substrate or group of closely related substrates
68
lock and key theory
active site of the enzyme (lock) has a specific shape that only fits a specific substrate (key)
69
induced fit
shape of enzyme and substrate altered upon binding
70
saturation kinetics
relative concentration, rate of rxn increases, to a lesser and lesser degree until Vmax is reached
71
Vmax
proportional to enzyme concentration,
72
Km
substrate concentration at which rxn rate = to 1/2 Vmax, doesn't vary when enzyme concentration is changed
73
temperature and pH and enzymes
optimal temp == 37 C , optimal pH depends on enzyme eg -- pepsin below 2, trypsin works best between 6 and 7
74
cofactor
non protein component that many enzymes need to reach optimal activity, coenzymes or metal ions
75
coenzymes
vitamins or their derivatives
76
irreversible inhibitors
bind covalently to enzymes and disrupt their function, toxic
77
competitive inhibitors
bind reversibly with covalent bonds to the active site, raise Km don't change Vmax
78
noncompetitive inhibitors
bind non-covalently to an enzyme at a spot other than the active site, change the conformation of the enzymes, don't resemble substrate, commonly act on more than one enzyme, lower Vmax, Km is the same
79
inactive form of an enzyme
zymogen or proenzyme, when specific peptide bonds are cleaved -- irreversibly activated
80
allosteric interactions
modification of the enzyme configuration resulting from the binding of an activator or inhibitor at a specific binding site on the enzyme
81
negative feedback / feedback inhibition
product downstream in a rxn comes back and inhibits enzymatic activity in an early reaction, shut down mechanism
82
positive feedback
product returns to activate the enzyme
83
allosteric regulation
feedback inhibitors bind to an enzyme and cause conformational change
84
allosteric inhibitors and activators
both exist, alter Km w/o changing Vmax
85
positive cooperativity
first substrate changes the shape of the enzymes allowing other substrates to bind more easily
86
negative cooperativity
occurs as well
87
enzymes
"-ase"
88
lyases
catalyzes the addition of one substrate to a double bond of a second substrate
89
ligase
require energy from ATP
90
kinase
phosphorylates something
91
phosphotates
dephosphorylates something
92
metabolism
all cellular chemical reactions
93
respiration
energy acquiring stages
94
anaerobic respiration
respiration where oxygen is not required
95
glycolysis
glucose broken down into 2 3C molecules of pyruvate, 2 net molecules of ATP, 2 molecules of NADH, occurs in the cytosol
96
substrate level phosphorlyation
formation of ATP from ADP and inorganic phosphate using the energy released from the decay of high energy phosphorylated compounds as opposed to using the energy from diffusion
97
fermentation
anaerobic respiration, glycolysis, reduction of pyruvate to ethanol or lactic acid and oxidation of NADH back to NAD+
98
aerobic respiration
requires oxygen
99
products of glycolysis
move into matrix of a mitochondria, pyruvate and NADH pass via facilitated diffusion
100
inner mitochondrial matrix
less permeable, pyruvates moves in via facilitated diffusion, NADH require hydrolysis of ATP to move in
101
inside matrix pyruvate becomes
acetyl CoA, rxn produces NADH and CO2
102
Krebs Cycle
each turn produces 1 ATP, 3 NADH and 1 FADH2
103
ATP Production occurs via
substrate level phosphylation
104
metabolism of fats
fatty acids converted into acyl CoA, brougth into matrix, acetly CoA produced, produces FADH2 and NADH for every 2 C of the original fatty acid
105
metabolism of proteins
AA deminated in liver, this product is converted to pyruvic acid or acetyl CoA or it may enter Krebs cycle at various stages
106
Electron transport chains
proteins in the inner membrane of mitochondria
107
1st protein complex
oxidizes NADH by accepting its high energy electron, electrons passed down series
108
Electrons passed down
ultimately accepted by oxygen to form water,
109
proton motive force
protons are pumped into intermembrane space for each NADH as electrons are passed along,
110
ATP synthases
protons propelled through this to produce ATP
111
Oxidative phosphorylation
uses energy released by the oxidation of products to create ATP
112
pH of intermembrane space
lower than that of the matrix
113
glucose + oxygen
carbon dioxide and water, combustion reaction
114
Amount of ATP Made in total
36 ATP
