Test 3 Flashcards

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1
Q

Complex I can leak what ____ toward the matrix?

A

O2

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2
Q

Complex III generates O2 where?

A

toward both matrix and inter-membrane space

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3
Q

When the cell is stressed it has what moved into the mitochondria.

A

apoptotic pathways, P66^she

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4
Q

P66 ^she is part of apoptosis generating _____ molecules.

A

ROS

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5
Q

How does P66^she accomplish apoptosis.

A

it accomplishes this by subtracting electrons from cytochrome c to produce O2

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6
Q

____ is highly regulated event in a cell. preventing apotosis.

A

ROS production

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7
Q

In a cell that has not signaled apoptosis O2 is dismutated to ____

A

H2O2

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8
Q

what dismutated H2O2

A

Cu, Zn, SOD (Super-oxide dismutatse)

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9
Q

What happens in the mitochondria after O2 is reduced to H2O2.

A

it is reduced to H2O by glutathione peroxidase (GPX) using GSH (glutathione), and the resultant oxidized glutathione (GSSG) is reduced back to GSH by glutathione reductase

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10
Q

A typical mammalian liver mitochondria has roughly ______ copies of the ATP synthase

A

15,000

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11
Q

Homologous versions of the ATP synthase are found?

A

plasma membrane of aerobic, bacteria, the thylakoid membrane of plant chloroplasts, and the inner mt membrane

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12
Q

Recent high-resolution EM work suggests that the two portions of the ATP synthase are connected by___

A

central peripheral stalk

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13
Q

ATP synthesizing enzyme has what two parts

A

F1 head, F0 (Fnot) basal section

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14
Q

F1

A

a spherical head

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15
Q

F0 (Fnot)

A

a basal section embedded in the inner membrane

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16
Q

The generated proton gradient is then used to make ATP via a protein complex known by several names

A

Fnot/F1 complex, ATP synthase, complex V (out of date)

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17
Q

Endergonic process is driven by ______ in energy level of the electron as it passes through.

A

reduction

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18
Q

what two enzymes are not part of the four complexes?

A

cytochrome c, ubiquinone (CoQ)

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19
Q

enzymes that transfer pairs of electrons from substrates to molecules such as the conenzymes NAD+ and FADH are called

A

dehydrogenases

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20
Q

Pathway by which monosaccharides are broken down

A

glycolysis

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21
Q

name an example of a monosaccharide in glycolysis

A

glucose

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22
Q

where does glycolysis occur

A

cytosol of eukaryotic cells and in prokaryotes

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23
Q

what three important molecules are generated during glycolysis

A

2ATP, 2pyruvate, 2NADH

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24
Q

The cyclic pathway that occurs in the matrix of mitochondrion

A

tricarboxilic acid cycle(TCA), citric acid cycle, krebs cycle,

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25
Q

What is a sybstrate for TCA

A

acetyl CoA

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26
Q

How is acetyl CoA formed?

A

via B-oxidation pathway in the mitochondrial matrix and in the peroxisome

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27
Q

by the transition reaction as pyruvate crosses the mitochondrial membranes generates?

A

1 NADH and releases 1 CO2

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28
Q

3 important molecules formed during TCA

A

2 ATP, 6 NADH, 2 FADH2, (2 CO2 are formed)

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29
Q

The high-energy electrons associated with NADH and FADH2 are transferred (dumped) to a series of specific electron carriers that constitute the ______ located in the inner mitochondrial membrane

A

ETC(Electron Transport Chain)

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30
Q

Lowest energy electrons are ultimately passed to molecular oxygen from ____

A

Complex IV

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31
Q

These protein complexes will use energy from the elections to establish a _____

A

H+ gradient withing the inter membrane space

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32
Q

The stored H+ gradient will power the endergonic process of synthesizing ATP via secondary or indirect active transport by the _____

A

F0/F1 complex

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33
Q

The ___ ETC complexes are composed of _____ types of membrane-bound electron carrier proteins

A

4,5

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34
Q

a polypeptide bound tightly to one of two related prosthetic groups

A

flavoproteins

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35
Q

proteins that contain heme prosthetic groups

A

cytochromes

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36
Q

both groups are derived from riboflavin (vitamin B2)

A

Flavin Adenine Dinucleotide (FAD) or Flavin Mononucleotide (FMN)

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37
Q

copper attoms are all located within ___

A

complex IV

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38
Q

Copper atoms alternate between

A

Cu^2+, Cu+1

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39
Q

lipid-soluble molecule containing a long hydrophobic chain composed of 5-carbon isoprenoid units

A

ubiquinone

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40
Q

ubiquinone is able to accept ____ electrons and protons

A

2

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41
Q

Where does ubiquinone reside

A

lipid bi-layer and moves about freely

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42
Q

contain iron not in a heme group, but that is instead linked to inorganic sulfur atoms

A

iron sulfur

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43
Q

iron- sulfur donates ___ electrons

A

single

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44
Q

Glycolisis makes

A

net gain 2 ATP, 2 pyruvate, 2 NADH

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45
Q

TCA cycle, citric acid cycle, and Krebs cycle

A

2 ATP 6 NADH, 2CO2

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46
Q

What is the pathway by which monosaccharides (such as glucose) are broken down

A

glycolysis

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47
Q

Where does glycolysis occur

A

cytosol of eukaryotic cells and in prokaryotes

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48
Q

enzymes that transfer pairs of electrons from substrates to molecules such as the coenzymes NAD+ and FADH (empty wheelbarrows)

A

dehydrogenases

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49
Q

The pathways of glycolyisis and TCA are rich in _____ some termed dehydrogenases

A

proteins

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50
Q

Solution withing inner membrane of the mitochondria is termed

A

matrix

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51
Q

what is the sight of the TCA pathway

A

matrix

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52
Q

Where does the mitochondrial gene expression and genome replication occur

A

matrix

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53
Q

the infoldings of membrane in the mitochondria are termed_____

A

cristae

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54
Q

The space between membranes in the mitochondria is termed the ________

A

intermembrane space

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55
Q

mitochondria is _____ part of the endomembrane system

A

not

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56
Q

mitochondria are ______, meaning they grow and divide within the cell and generate some of the proteins that function there, and take up others from the cytoplasm

A

semiautonomous

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57
Q

Mitochondria have there own

A

DNA and ribosomes

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58
Q

mitochondria are about ____ in diameter

A

1-10um

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59
Q

Glucose moves across the apical plasma membrane against a concentration gradient by

A

Na+ contransport (symport)

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60
Q

The needed Na+ gradient is maintained by _____ by the Na+/K+ -ATPase pump in the basal and lateral membranes of the cells

A

active transport

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61
Q

Finally the glucose molecules move into the blood stream by ____ _____ through a glucose transporter (glucose permease)

A

facilitated diffusion

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62
Q

Tums and Rolaids work by neutralizing

A

acid (H+) in the stomach

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63
Q

Zantac, Pepcid, and Tagamet work instead by

A

blocking receptors on the surface

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64
Q

Over secretion of acid can lead to _______

A

heartburn

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65
Q

The epithelial lining of the stomach contains a _____ which secreetes a solution of concentrated acid (up to 0.16 NHCL) into the stomach chamber

A

H+/K+ -ATP

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66
Q

In the resting state of transport proteins are situated in the membranes of

A

cytosolic vesicles

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67
Q

When food enters the stomach a hormonal message is transmitted to the parietal cell causing the ______ vesicles to move to the ______ cell surface and begin secreting acid.

A

pump-containing, apical

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68
Q

an example binds at a cell surface receptor triggering cellular signal transduction

A

histamine

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69
Q

Driving exergonic reaction here is the use of the Na+ is present to bind simultaneously

A

sodium-glucose symport

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70
Q

Cells lining our intestine are able to take up molecules like glucose or amino acids from the lumen into the cells even when the cellular concentration is higher than the lumen concentration

A

sodium-glucose symport

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71
Q

The subsequent facilitated diffusion of Na+ back across the membrane drives the intake of glucose, and other molecules this is termed

A

indirect active transport or secondary active transport

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72
Q

what pump is found only in animals, although other species accomplish the same tasks with analogous mechanisms and proteins

A

sodium-potassium pump

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73
Q

the sodium -potassium pump has a ____ ____ for Na+ with binding sites oriented towards the cytoplasm

A

high affinity

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74
Q

The sodium-potassium pump has a high affinity for ____ with binding sites oriented towards the cell’s exterior.

A

K+

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75
Q

termed ____ ___ in nonexciteable cells (those other than neurons and muscle)

A

membrane potential

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76
Q

termed a _____ _____ in neurons and muscle cells

A

resting potential

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77
Q

Such _____ movement ofions requires being coupled to an _____ reaction such as

A

endergonic, exergonic

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78
Q

____ depends on integral membrane proteins that selectvely bind a particular solute and move it across the membrane against its concentration gradient in a process driven by energy requiring changes in the protein’s conformation.

A

active transport

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79
Q

proteins that carry out active transport are often referred to as ____

A

pumps

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80
Q

very similar to facilitated diffusion but it moves molecules against a concentration gradient and therefore, requires an energy input

A

active transport

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81
Q

Typically the K+ concentration inside a mammalian is ___

A

higher

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82
Q

typically, the Na+ concentration is ____ on the outside

A

higher

83
Q

Ca+ concentration gradient is very large _____ cell

A

outside of the cell

84
Q

Today there are a considerable number of inherited ion channel diseases named collectively _____ caused by mutations in K+, Na+, Ca2, and Cl- channels that are known to exist in human and animal models.

A

channelopathies

85
Q

once a pore is oen, a few thousand ions pass through the channel per millesecond

A

example of gating

86
Q

most ion channels exist in one of three possible configurations, which is regulated by various stimuli.

A

open, closed, inactivated

87
Q

The ease whith which an ion can go through a single channel

A

ionic permeability

88
Q

voltage gated channels fall in what two categories

A

multimeric, and monomeric

89
Q

what is a multimeric voltage gated channels

A

potassium channel

90
Q

voltage gated monomeric channel

A

sodium channel

91
Q

what is the technique of ______ in studying ion channels.

A

patch clamping

92
Q

gated channels

A

regulated, chemically or ligand gated, voltage-gated, mechanically gated,

93
Q

usually open and allow ions to move back and forth across the membrane without regulation

A

open channels.

94
Q

the most biological membranes are impermeable to charged substances, including small ions such as

A

Na+, K+, Ca2+, and Cl-

95
Q

A variety of proteins termed

_____ have been identified

A

ion channels

96
Q

Most ion channels are highly selective and allow only ___ type of ions to pass through

A

one

97
Q

the diffusion of ions through a channel is ____ ____

A

always down hill, from a high to low concentration

98
Q

ion channels are ___

A

bidirectional

99
Q

how many different ioni channels have been discovered?

A

75

100
Q

movement of water readily from hypotonic solution to a hypertonic solution. Many cells are much more water permeable than explained by simple ____ through the bi-layer.

A

osmosis

101
Q

proteins that allow the passive movement of water from one side to the other

A

aquaporins

102
Q

The hormone _____ stimulates water retention by the collecting ducts of the kidney, by way of these channels

A

vasopressin

103
Q

a mutation in this aquaporin channel, in which persons excrete large amounts of urine because their kidneys don’t respond to vasopressin

A

congenital nephrogenic diabetes insipidus

104
Q

carries a only one kind of solute across the membrane

A

uniport

105
Q

cooperative channel which moves two substances simultaneously in the same directions, e.g. Na+ and glucose. Due to concentration gradient, Na+ moves downhill and releases enough free energy to move glucose uphill.

A

symport

106
Q

exchanges one solute for another by transporting them in opposite directions-e.g. Cl- for HCO3

A

antiport`

107
Q

In a _______ the transport proteins for cyteine and other amino acids is missing from the membrane

A

kidney disease, cystinuria

108
Q

a common form of _____ involves mutations that alter the sequences of transmembrane segments of the transporter preventing transport across the plasma membrane

A

diabetes

109
Q

glucose transporters are actually a family of enzymes that transport the _____

A

6-C sugars

110
Q

D-mannose Km

A

20mM

111
Q

D-glactose Km

A

30mM

112
Q

if glucose ratios are high all the ____ are occupied

A

transporters

113
Q

D-glucose

A

1.5mM

114
Q

l-glucose

A

> 3000mM

115
Q

Transport proteins can be ____ by moleules that resemble the solute normally carried (similar to competitve inhibition in enzymes)

A

ingibited

116
Q

Transport proteins can be _____ with solute, so a maximum transport rate occurs when all binding sites are occupied with solute

A

saturated

117
Q

Transport proteins are ____ for the solutes they transport. There is probably a specific binding site analogous to an enzyme’s active site.

A

specific

118
Q

transport protein remains in place in the membrane and translocates solute by alternating between _ confomations

A

2

119
Q

term applied to some transport proteins that move uncharged molecules like glucose

A

permease

120
Q

proteins that operate in facilitated diffusion are termed _____

A

transport proteins

121
Q

transport proteins were formerly nown as

A

carrier proteins

122
Q

_____ is the movement of a molecule across a membrane by the aid of a protein that does not just form a channel but instead binds the ligand and undergoes a conformational change delivering the molecules across the membrane.

A

facilitated diffusion

123
Q

larger polar molecules such as sugars, amino acids, and phosphorylated intermediates have____ membrane penetrability

A

poor

124
Q

factors that affect the simple diffusion of a molecule

A

partition coefficient, size,

125
Q

a measure of the polarity (or nonpolarity) of a substance

A

partiton coefficient

126
Q

rate of movement through a membrane depends on the compounds

A

size

127
Q

very small uncharged molecules penetrate a membrane very quickly like

A

O2, CO2, NO, H2O

128
Q

GLUT1

A

glucose permease

129
Q

transport protein remains in place in the membrane and _____ solute by alternating between 2 conformations

A

translocates

130
Q

transport protein might bind to solute in one ____ and deposit it on the other side of the membrane in another conformation

A

conformation

131
Q

diffusion is the principle used in what lab technique

A

dialysis

132
Q

two categories for diffusion

A

passive and active

133
Q

____ tells if a reaction can thermodynamically happen, but doesn’t say that it will happen! Rate of a reaction is a function of specialized enzymes.

A

delta G

134
Q

Molecules that ____ react with one another often ___ ____ because they lack sufficient energy.

A

should, do not

135
Q

What does a reaction need to react.

A

delta G, and enough energy to reach Ea

136
Q

The rate of an enzymatic reaction is _____ to the fraction of molecules that have and energy content >= Ea

A

proportional

137
Q

Therefore, the rates of uncatalyzed reactions in cells are very ____.

A

slow

138
Q

life depends on the high Ea to ______ cellular reactions from happening at appreciable rates _____ in the presence of a suitable catalyst

A

prevent, except

139
Q

protein catalysts are called

A

enzymes

140
Q

RNA catalysts are called

A

ribozymes

141
Q

three basic properties of catalysts

A
  1. increase rate of reaction by lowering Ea requirements
  2. Catalysts act by forming transient intermediate complexes with substrate molecules and thus position them in a manner that facilitates their interaction.
  3. catalysts chg only the rate at which equilibrium is reached; no effect on the position of the equilibium
142
Q

Every enzyme contains, somewhere within its 3 prime structure, a characteristic cluster of amino acids forming an ______

A

active site.

143
Q

the location or domain on which the enzymes structure where the actual catalytic action occurs.

A

active site

144
Q

Amino acids most commonly found at active sites

A

cysteine, histidine, serine, aspartate, glutamate, lysine

145
Q

ion groups that are integral parts of enzyme structure

A

prosthetic groups

146
Q

if a _____ is present the reaction occurs about 1x10^9 X faster that if uncatalyzed

A

catalase

147
Q

enzymatic catalysis equation

A

E+S –> E+P

148
Q

maintain a narrow range of cellular temps

A

homeotherms

149
Q

organisms that live in an environment with a higher than average temperature for biotic life such as bacteria that thrive in environments that average 70 degrees C

A

thermophiles

150
Q

most enzymes are ____ sensitive

A

pH

151
Q

enzyme environmental requirements

A

sensitivity to temperatures, sensitivity to pH , sensitivity to ion concentration,

152
Q

the number of substrate molecules converted to product per unit time

A

turnover rate

153
Q

the presence of an enzyme in a cell ______ tgat a given reaction will occur ata rapid rate unless cellular conditions are favorable for enzyme to function

A

may not ensure

154
Q

what is much of our understanding of the hyperbolic relationship between [S] and v is owed to two German enzymologists;

A

Lenor Michaelis and Maud Mentan.

155
Q

michaelis-mentan equation

A

v=vmax[S]/(Km+[S])

156
Q

very low substrate concentration Mand M equation

A

v=Vmax[S]/Km

157
Q

High substrate concentration

A

V=Vmax

158
Q

at a very high [s] the velocity of an enzyme-catalyzed reaction is _____ of changes in [S] and is therefore approximately constant

A

independent

159
Q

the maximum velocity, or upper limiting value, to which v tends as [S] approaches infinity.

A

Vmax

160
Q

substrate concentration equals Km=[S]

A

v=(1/2)Vmax

161
Q

__ is the specific substrate concentration at which the reaction proceeds at 1/2 its upper limit (Vmax)

A

Km

162
Q

the value of Km is termed the ________ ___

A

michaelis constant

163
Q

Enzymes that have a low Km for a specific substrate are said to have a ____ for that substrate.

A

high affinity

164
Q

example of a double reciprocal plot

A

lineweaver-Burk equation

165
Q

lineweaver-burk y intercept=

A

1/Vmax

166
Q

lineweaver-burk x-intercept=

A

-1/Km

167
Q

lineweaver-burk slope=

A

Km/Vmax

168
Q

Enzymes are influenced by the presence of many groups of molecules.

A

poducts, alternative substrates, substrate analogues, toxins, drugs, allosteric effectors

169
Q

usually bind to the enzyme covalently, causing irrevocable loss of catalytic activity

A

irreversible inhibitors

170
Q

irreversible inhibitors is represented as

A

E+I ->->EI

171
Q

inhibitor binds to an enzyme in a dissociable manner, such that the bound and free forms of the inhibitor exist in equilibrium with each other

A

reversible inhibitors

172
Q

Reversible inhibitors can be represented as

A

E+I EI

173
Q

competes with substrate for binding at the active site but cannot be catalyzed

A

competitive inhibitors

174
Q

term applied to chemicals designed to closely resemble a substrate so they bind at an enzyme’s active site while being uncatalyzable. Recall GTP-analogues used to study Dynamin and other GTPases

A

substrate analogues

175
Q

do not bind at the enzyme’s active site, bind at another location on the enzyme, not usually at an allosteric site, binding location maybe an unpredictable location on the enzyme surface

A

Noncompetitve Inhibitors

176
Q

binds to ES complex prevents catalysis, substrate is still taken up from the environment but is locked in an ES form

A

uncompetitive inhibitors

177
Q

those mechanisms that depend directly on substrate-enzyme interactions are termed

A

substrate-level regulation

178
Q

substrate regulation

A

pH, [S], inhibitors, temp

179
Q

enzymes regulated exist in 2 different shapes, in one form the enzyme has a high affinity for substrate…. high reaction rate

A

allosteric regulation

180
Q

In addition to an ___ ___ many enzymes have an _____ ____ located on the _____ ___, at which effectors can bind and alter the shape of the enzyme.

A

active site, allosteric site, allosteric domain,

181
Q

catalyzes this reaction and is inhibited by its own product G-6-P . If G-6-P accumulates hexokinase is inhibited slowing down the further entry of glucose into the pathway.

A

hexokinase

182
Q

almost invariably, enzymes at first or early steps of a multi-step pathways are regulated allosterically.

A

feedback inhibition

183
Q

5 common enzyme regulation methods

A

substrate regulation, allosteric regulation, property of cooperativity, covalent modification, proteolitic cleavage

184
Q

binding at one site increases the affinity for substrate at other sites

A

positive cooperativity

185
Q

binding at one site reduces the affinity for the substrate at other sites

A

negative cooperativity

186
Q

in this form of regulation, the activity of an enzyme is affected by the addition or removal of specific functional groups

A

covalent modification

187
Q

enzymes that catalyze the phosphorylation of other molecules

A

kinases aka phosphorylases

188
Q

most often involves the transfer of the phosphate group from ATP to the hydroxyl group of a

A

serine, threonine, or tyrosine

189
Q

enzymes that catalyze the process of removing a phosphate, i.e. catalyze dephosphorylation

A

phosphoprotein phosphatses

190
Q

The breakdown of glycogen in skeletal muscle cells is catalyzed by ______ ____.

A

Glycogen Phosphorylase

191
Q

How is glycogen phosphorylase kinased?

A

phosphorylase kinase

192
Q

memorize the cyclic AMP

A

chp 6

193
Q

this type of activation involves the one-time, irreversible removal of the polypeptide chain by an appropriate proeolytic enzyme

A

proteolytic cleavage

194
Q

each of these is produced in an inactive form termed a ____ ____

A

zymogen or proenzyme

195
Q

inactive zymogens have modified names….. ____ whatever or whatever-_____

A

pro-, ogen

196
Q

An indicator of the first molecular event during Experimental Pancreatitis

A

TAP

197
Q

TAP stands for

A

trypsin activation protein

198
Q

oxidation-reduction reaction

A

oxidoreductases

199
Q

transfer of functional groups from one molecule to another

A

transferases

200
Q

hydrolytic cleavage of one molecule into two molecules

A

hydrolases

201
Q

removal of a group from, or additionof a group to, a molecule with rearrangement of electrons

A

lyases

202
Q

movement of a functional group within a molecule

A

isomerases

203
Q

joining of two molecules to form a single molecules

A

ligases