Biology Lecture 2

Front 1

An enzyme is a

Back 1

Biological catalyst

Front 2

Enzymes speed up

Back 2

Chemical reaction without being consumed by the reaction

Front 3

Enzymes lower

Back 3

The activation energy of a chemical reaction

Front 4

Energy must be

Back 4

Absorbed by the reactants in order to break bonds

Front 5

If the reaction is

Back 5

Exergonic, triangle G will be repaid with dividends because the new bonds release more energy than the energy invested in breaking the old bonds

Front 6

An enzyme is specific in its

Back 6

Reaction

Front 7

Enzyme can

Back 7

Catalyze only a particular substrate

Front 8

Substrate

Back 8

Is a substance upon which an enzyme acts

Front 9

Lock and key hypothesis

Back 9

Substrate attaches to the active site of an enzyme like a key fits to a lock. There is a rearrangement of the atoms in the substance.

Front 10

Induced fit hypothesis

Back 10

Attachment of the substrate to the active site of an enzyme induces structural changes in the enzymes, causing the substrate and the enzyme to fit more tightly. Rearrangement of the atoms in the substrate.

Front 11

The conversion of the substrate to end product is catalyze for by the

Back 11

Side chains (R groups) of a few of the amino acids that make up the active site.

Front 12

Enzymes

Back 12

Saturated if all its active sites are engaged by the substrate.

Front 13

Factors affecting enzyme activity

Back 13

Temperature, pH, salt concentration, cofactors

Front 14

Most enzymes

Back 14

The pH optimum is in the range of 6-8

Front 15

Pepsin works best at

Back 15

PH 2

Front 16

Trypsin has a pH optimum of

Back 16

8

Front 17

Most enzymes cannot tolerate

Back 17

High salt concentration

Front 18

Cofactor

Back 18

Inorganic part of an enzyme

Front 19

The cofactors are usually metal ions of

Back 19

Calcium, magnesium, zinc, iron or copper

Front 20

Coenzyme

Back 20

Organic, non protein portion of an enzyme

Front 21

Most vitamins are

Back 21

Coenzyme

Front 22

Apoenzyme

Back 22

Protein part of an enzyme

Front 23

The entire enzyme

Back 23

Apoenzyme plus coenzyme or Cofactor

Front 24

Entire enzyme

Back 24

Holoenzyme

Front 25

Enzyme is irreversibly inhibited

Back 25

If the enzyme inhibitors bind covalently to it

Front 26

competitive inhibition

Back 26

two different substances, one is a normal substrate and the other is an inhibitor compete for the same active site on an enzyme. This enzyme cannot function if its active site is occupied by the inhibitor

Front 27

noncompetitive inhibition

Back 27

type if enzyme inhibition in which an inhibitor binds to a site best to the active site of an enzyme, and physically blocks the active site for the normal substrate

Front 28

allosteric inhibition

Back 28

in this type of inhibition, an enzyme which is constructed from two or more polypeptide subunits can occur in two conformations: active form and inactive form. Each polypeptide subunit has its own active site. The allosteric site is usually located where the subunits are joined. if a negative modulator (inhibitor) binds to the allosteric site of the enzyme which is in inactive form, the enzyme cannot change to an active form. The activity of the enzyme is thus inhibited.

Front 29

end product inhibitor

Back 29

aka negative feedback inhibition

the inhibition of an enzyme activity is due to the accumulation of end products. The enzyme that can be inhibited by an end product is called a regulatory enzyme. an example is the synthesis of isoleucine from threonine.(end product inhibition)

Front 30

magnification

Back 30

is how much larger the object appears compared to its real size

Front 31

resolving power

Back 31

is the ability to distinguish two adjacent points as two separate points

Front 32

two types of electron microscopes

Back 32

transmission electron microscope & scanning electron microscope

Front 33

transmission electron microscope (TEM)

Back 33

is used to study the internal ultrastructure of cells

Front 34

SEM scanning electron microscope

Back 34

used for detailed study of the surface of a specimen.

Front 35

cytology

Back 35

study of cell structure

Front 36

prokaryotic cell does not have

Back 36

a true nucleus

Front 37

prokaryotic cells genetic material is located

Back 37

in a nucleoid

Front 38

eukaryotic cell

Back 38

has all cellular organelles and a true nucleus which is surrounded by a nuclear membrane

Front 39

two factors that limit cell size are the

Back 39

surface area to volume ratio, and the requirement for a single nucleus to control the entire cytoplasm

Front 40

larger cell has a less

Back 40

surface area to volume ratio than a small cell making it inefficient in carrying out its metabolism

Front 41

eukaryotes compensate

Back 41

for small surface to volume ratio by having internal membranes

Front 42

non dividing cell

Back 42

chromosomes are dispersed as a mass of material known as chromatin

Front 43

human cells have

Back 43

46 of chromosomes = 23 pairs

Front 44

the sex cells (sperm & egg)

Back 44

have 23 chromosomes

Front 45

nucleolus

Back 45

is not enclosed by a membrane

Front 46

ribosomes

Back 46

an organelle that sites of protein synthesis

Front 47

smooth endoplasmic reticulum

Back 47

organelle synthesis of lipids, carbohydrate metabolism, & detoxification of drugs, alcohol, and poisons

Front 48

rough endoplasmic reticulum

Back 48

synthesis of secretory protein

Front 49

which organelles are involved in signal hypothesis?

Back 49

ribosomes & rough (glandular) endoplasmic reticulum

Front 50

the golgi apparatus

Back 50

dictyosome, cis face, and trans face

Front 51

golgi apparatus

Back 51

is responsible for storage, modification and packaging of secretory products

Front 52

lysosomes aka

Back 52

suicide bags

Front 53

lysosomes

Back 53

-digestion of food particles and bacteria

-autophagy of the old & dead cells

-developement of the organisms (destruction of the cells in a tadpole's tail, and the digestion of tissues between the fingers of the webbed hands of human embryos

Front 54

pompe's disease

Back 54

is causes by the accumulation of glycogen in the liver due to the lack of an enzyme needed to break down the polysaccharide

Front 55

tay-sach's disease

Back 55

brain becomes impaired due to the accumulation of lipid as the lysosome lack a lipid-digesting enzyme

Front 56

glyoxysomes

Back 56

are often in the fat storing tissues of the germinating seedlings.

their enzymes convert fats to sugar, and energy source for the seeding until it can produce its own sugar by photosynthesis

Front 57

contractile vacuoles pump

Back 57

excess water out of the cell

Front 58

central vacuole is found

Back 58

in a mature plant cell. it stores organic compounds and inorganic ions.

Front 59

central vacuole functions as

Back 59

a lysosomes, and serves as a disposal site for metabolic wastes. it may contain pigment molecules which give color to the petals to attract pollinating insects. it may also contain chemicals that are poisonous or unpalatable to predators

Front 60

which two organelles are related to nuclear envelop?

Back 60

rough er & smooth er

Front 61

the nuclear envelope is an extension of

Back 61

rough er which in turn is connected to the smooth er

Front 62

which two organelles are energy transducers

Back 62

mitochondria and chloroplasts

Front 63

mitochondria are the sites of

Back 63

cellular respiration in which organic compounds are broken down to generate ATP

Front 64

chloroplasts are found only in

Back 64

plants

Front 65

mitochondria is enclosed by

Back 65

two membranes

Front 66

cristae

Back 66

only in mitochondria

Front 67

plastids are found only in

Back 67

plants

Front 68

amyloplasts

Back 68

leucoplasts

are white or colorless plastids that store starch in roots and tubers

Front 69

in order of increasing diameter (narrowest to widest)

Back 69

microfilaments

intermediate filaments

microtubules

Front 70

in order of decreasing diameter (widest to narrowest)

Back 70

microtubules

intermediate filaments

microfilaments

Front 71

chloroplasts are

Back 71

-green plastids which contain chlorophyll, enzymes, and other molecules that function in the photosynthesis

Front 72

thylakoids

Back 72

-disklike structures upon which chlorophylls are arranged

Front 73

granum

Back 73

stack go thylakoids

Front 74

microtubules are found in all

Back 74

eucaryotes

Front 75

functions of microtubules

Back 75

1.)maintenance of cell shape

2.)intracellular movement of organelles, nutrients and secretory vesicles

3.)separation of chromosomes during cell division

4.) cell movement

Front 76

diff in cilia & flagella

Back 76

1.) cilia are more numerous than flagella

2.) cilia are shorter than flagella

3.) cilia has motility and movement of food particles, & flagella has motility

4.) cilia's movement is in synchronization, unlike flagella

5.) 9+2 arrangement of microtubules in cilia & flagella

6.) ensheathed in an extension of plasma membrane in cilia & flagella

Front 77

where is the cilium and flagellum are anchored in the cell by

Back 77

basal body

Front 78

actins are

Back 78

proteins

Front 79

myosin are

Back 79

proteins

Front 80

functions of microfilaments are

Back 80

1.) they func in support. They support the villi which increases the surface area for nutrient absorption

2.) they contraction of the microfilaments cause the invagination of cell membrane during cell division

3.) they are responsible for the elongation and contraction of pseudopodia during amoeboid movement

4.) they cause cytoplasmic streaming (cyclosis) in cells

Front 81

intermediate filaments diameter is

Back 81

larger than the microfilaments but smaller than the microtubules

Front 82

cell walls are found in

Back 82

plants, bacteria and fungi

Front 83

the functions of the glycocalyx of animal cells

Back 83

1.) it strengthens the cell surface & helps glue cells together

2.) it is responsible for cell recognition and contract inhibition

Front 84

plant cells have

Back 84

plasmodesmata

Front 85

plasmodesmata

Back 85

are cytoplasmic connection between adjacent cells

Front 86

animal cells have

& common where

Back 86

three types of intercellular junctions:

1.) tight

2.) desmosomes

3.) gap

common in cells of the epithelial tissue

Front 87

cellulose found in both

Back 87

primary and secondary cell wall of plant cells

Front 88

phospholipids is an

Back 88

amphipathic molecule which has a hydrophilic head and a hydrophobic tail

Front 89

davson and danielli model of a cell membrane

Back 89

proposed the sandwich model in which phospholipid bilayer is sandwiched between between two layers of protein

Front 90

4 parts of the cell membrane

Back 90

integral protein, phospholipid bilayer, peripheral proteins, and cholesterol

Front 91

which chemical NOT used in freeze fracture (freeze etching) techniques?

Back 91

gold

Front 92

the cell membrane is relatively impermeable to

Back 92

ions and larger uncharged polar molecules such as glucose and other sugars

Front 93

uniport

Back 93

carries single solute across the cell membrane

Front 94

symport

Back 94

carries two different solutes simultaneously in one direction across cell membrane

Front 95

antiport

Back 95

carries one solute into the cell and another solute out of the cell

Front 96

diffusion

Back 96

movement of particles from a region of higher concentration to a regain of lower concentration.

Front 97

in diffusion, how much energy is spend by the cell?

Back 97

none

Front 98

osmosis

Back 98

the movement of water molecules from a region of higher concentration yo a region of lower concentration through a semi permeable membrane

Front 99

three types of solutions

Back 99

hyperosmotic (hypertonic) solution

hypesmotic (hypertonic) solution

isoomoyic (isotonic) solution

Front 100

if a cell is placed in hypertonic solution

Back 100

cell will shrink

Front 101

plasmolysis

Back 101

process of cell shrinking

Front 102

crenation

Back 102

the shrinking of red blood cells when they are placed in a hypertonic solution

Front 103

if a cell is placed in hypotonic solution

Back 103

it will swell

Front 104

cell swelling

Back 104

plasmoptysis

Front 105

hemolysis

Back 105

bursting of red flood cells when they are placed in hypotonic solution

Front 106

facilitated diffusion

Back 106

the movement of particles from a region of higher concentration to a region of lower concentration through a semi permeable membrane with the help of a carrier molecule.

Front 107

how much energy is used in facilitated diffusion?

Back 107

none

Front 108

in facilitated diffusion, transport

Back 108

protein remains in place in the membrane. it undergoes conformational changes

Front 109

active transport is the

Back 109

movement of particles from a region of lower concentration to a region of higher concentration through a semi permeable membrane with the help of a carrier molecule(permease)

the cell has to spend energy accomplishing this

Front 110

sodium potassium pump

Back 110

an example of active transport

Front 111

macromolecules make a

Back 111

minor contribution to the membrane potential

Front 112

selective permeability of the membrane to various

Back 112

ions is a major factors that contributes to the membrane potential bc potassium ions move out faster than sodium ions move into the cell

Front 113

sodium potassium pump

Back 113

removes three sodium ions out of the cell.

for every two possum ions, it pumps into the cell

Front 114

electrogenic pump

Back 114

protein that generates voltage across a membrane

Front 115

major electrogenic pump in animals

Back 115

sodium potassium pump and that os a plants, bacteria and fungi is proton pump which transports hydrogen ions out of the cells

Front 116

cotransport is an

Back 116

ATP driven pump which pumps hydrogen ions out of the cell

Front 117

two types of endocytocysis

Back 117

phagocytosis & pinocytosis

Front 118

phagocytosis

Back 118

process of cell eating

Front 119

pinocytosis

Back 119

process of cell drinking

Front 120

ligands are

Back 120

substances that in receptor mediated endocytosis binds the receptors

Front 121

An end product may serve as

Back 121

A competitive inhibitor or an allosteric inhibitor in end product inhibition

Front 122

What was types of micro bodies

Back 122

Peroxisomes & glyoxysomes

Front 123

What was types of micro bodies

Back 123

Peroxisomes & glyoxysomes

Front 124

Microbodies

Back 124

They are enclosed by a single membrane

Front 125

Fermentation

Back 125

Is the breakdown of organic compounds, namely carbohydrates, without the use of oxygen

Front 126

Fermentation

Back 126

Is the breakdown of organic compounds, namely carbohydrates, without the use of oxygen

Front 127

Cellular respiration

Back 127

Is the breakdown of organic compounds (glucose) to form CO2 and water with the production of ATP molecule

Front 128

Cellular respiration

Back 128

Catabolic pathway is exergonic

Front 129

Phosphorylation of ADP

Back 129

Is an endergonic process

Front 130

Glycolysis

Back 130

The breakdown of glucose to two molecules of pyruvic acid. It takes the place in the cytosol

Front 131

Krebs cycle

Back 131

Breakdowns a acetyl coenzyme A of to carbon dioxide. It takes the place on the mitochondria

Front 132

Electron transport chain & oxidative phosphorylation use

Back 132

the energy of electrons released from food molecules during glycolysis and Krebs cycle to synthesize ATP by the oxidative phosphorylation of ADP

Front 133

Most ATP is made by

Back 133

Oxidative phosphorylation, driven by an energy-coupling mechanism called chemiosmosis

Front 134

Most ATP is made by

Back 134

Oxidative phosphorylation, driven by an energy-coupling mechanism called chemiosmosis

Front 135

Electron transport chain

Back 135

An apparatus that pumps protons across the inner membrane from the mitochondrial matrix to the intermembrane space

Front 136

The electrons transport chain uses

Back 136

Energy released by glycolysis and Krebs cycle

Front 137

Reduction

Back 137

Is an addition of electrons or hydrogen atoms to a molecule or the removal of oxygen atom from a molecule

Front 138

Reduction

Back 138

Is an addition of electrons or hydrogen atoms to a molecule or the removal of oxygen atom from a molecule

Front 139

Oxidation

Back 139

The loss or removal of electrons or hydrogen atoms from a molecule or the addition of oxygen to a hydrogen

Front 140

Cytoplasm is

Back 140

Negatively changed

Front 141

Cytoplasm is

Back 141

Negatively changed

Front 142

Extra cellular fluid

Back 142

Positively charged in a resting cell

Front 143

Cytoplasm is

Back 143

Negatively changed in a resting cell

Front 144

Sodium is the

Back 144

Electrical donor aka reducing agent

Front 145

Reduction is a chemical process results in

Back 145

Storage of energy

Front 146

Oxidation results in

Back 146

Liberation of energy

Front 147

Cl

Back 147

Is the electron acceptor

Front 148

Glycolysis

Back 148

Breakdown of glucose to two molecules of pyruvic acid

Front 149

Glycolysis takes the place of

Back 149

Cytoplasm

Front 150

NADH

Back 150

Is electrically neutral

Front 151

Nicotinamide adenine dinucleotide

Back 151

Special electron acceptor

Front 152

Nicotinamide adenine dinucleotide

Back 152

Is a coenzyme

Front 153

Flavor adenine dinucleotide

Back 153

Another coenzyme

Front 154

Krebs cycle

Back 154

Aka citric acid cycle or tricarboxylic acid cycle

Front 155

How much oxygen is used in glycolysis

Back 155

None

Front 156

Is oxygen used in krebs oxygen?

Back 156

Yes

Front 157

Is oxygen used in krebs oxygen?

Back 157

Yes

Front 158

Electron transport chain & oxidative phosphorylation requires

Back 158

Oxygen

Front 159

Is oxygen used in krebs oxygen?

Back 159

Yes

Front 160

Electron transport chain & oxidative phosphorylation requires

Back 160

Oxygen

Front 161

Oxidative phosphorylation

Back 161

Production of ATP by the electron transport chain

Front 162

Ubiquinones

Back 162

Only carrier not bound to a protein

In the electron transport

Front 163

Exergonic reaction

Back 163

Electron transfer from NADH to oxygen

Front 164

Electron transport chain does not make

Back 164

ATP

Front 165

What's the function of electron transport chain do?

Back 165

Creates a proton gradient across the mitochondrial membrane

Front 166

What's the function of electron transport chain do?

Back 166

Creates a proton gradient across the mitochondrial membrane

Front 167

Chemiosmosis

Back 167

The use of a proton motive force to couple exergonic chemical processes to endergonic processes

Front 168

What's the function of electron transport chain do?

Back 168

Creates a proton gradient across the mitochondrial membrane

Front 169

Chemiosmosis

Back 169

The use of a proton motive force to couple exergonic chemical processes to endergonic processes

Front 170

In Krebs cycle

Back 170

One molecule of ATP & FADH2 and three molecules of NADH are produced

Front 171

What's the function of electron transport chain do?

Back 171

Creates a proton gradient across the mitochondrial membrane

Front 172

Chemiosmosis

Back 172

The use of a proton motive force to couple exergonic chemical processes to endergonic processes

Front 173

In Krebs cycle

Back 173

One molecule of ATP & FADH2 and three molecules of NADH are produced

Front 174

Cyanide blocks

Back 174

Passage of electrons from cytochrome a3 to oxygen

This is how cynide interferes with the chemiosmosis mechanism

Front 175

Cytochromes

Back 175

Which have a heme group surrounding a single iron atom

Front 176

The complete breakdown of one glucose molecule to CO2

Back 176

Yields 38 ATP molecules in procaryotes and 36 ATP molecules in eucaryotes

Front 177

Glycolysis

Back 177

Oxidizes glucose to two molecules of pyruvic acid

It's an exergonic reaction

Front 178

Glycolysis

Back 178

Oxidizes glucose to two molecules of pyruvic acid

It's an exergonic reaction

Front 179

Fermentation is the

Back 179

Catabolism of organic compounds

This generates ATP by substrate level phosphorylation as long as there is NAD+ to accept electrons

Front 180

Glycolysis

Back 180

Oxidizes glucose to two molecules of pyruvic acid

It's an exergonic reaction

Front 181

Fermentation is the

Back 181

Catabolism of organic compounds

This generates ATP by substrate level phosphorylation as long as there is NAD+ to accept electrons

Front 182

2 most common kinds of fermentation

Back 182

Alcohol fermentation & lactic acid fermentation

Front 183

Glycolysis

Back 183

Oxidizes glucose to two molecules of pyruvic acid

It's an exergonic reaction

Front 184

Fermentation is the

Back 184

Catabolism of organic compounds

This generates ATP by substrate level phosphorylation as long as there is NAD+ to accept electrons

Front 185

2 most common kinds of fermentation

Back 185

Alcohol fermentation & lactic acid fermentation

Front 186

Yeasts and many bacteria carry out

Back 186

Alcohol fermentation under anaerobic conditions

Front 187

Glycolysis

Back 187

Oxidizes glucose to two molecules of pyruvic acid

It's an exergonic reaction

Front 188

Fermentation is the

Back 188

Catabolism of organic compounds

This generates ATP by substrate level phosphorylation as long as there is NAD+ to accept electrons

Front 189

2 most common kinds of fermentation

Back 189

Alcohol fermentation & lactic acid fermentation

Front 190

Yeasts and many bacteria carry out

Back 190

Alcohol fermentation under anaerobic conditions

Front 191

Certain fungi & bacteria perform

Back 191

Lactic acid fermentation in the product of cheese & yogurt.

Front 192

Glycolysis

Back 192

Oxidizes glucose to two molecules of pyruvic acid

It's an exergonic reaction

Front 193

Fermentation is the

Back 193

Catabolism of organic compounds

This generates ATP by substrate level phosphorylation as long as there is NAD+ to accept electrons

Front 194

2 most common kinds of fermentation

Back 194

Alcohol fermentation & lactic acid fermentation

Front 195

Yeasts and many bacteria carry out

Back 195

Alcohol fermentation under anaerobic conditions

Front 196

Certain fungi & bacteria perform

Back 196

Lactic acid fermentation in the product of cheese & yogurt.

Front 197

Human muscle cells make

Back 197

Lactic acid under anaerobic conditions during strenuous exercise

Front 198

Glycolysis

Back 198

Oxidizes glucose to two molecules of pyruvic acid

It's an exergonic reaction

Front 199

Fermentation is the

Back 199

Catabolism of organic compounds

This generates ATP by substrate level phosphorylation as long as there is NAD+ to accept electrons

Front 200

2 most common kinds of fermentation

Back 200

Alcohol fermentation & lactic acid fermentation

Front 201

Yeasts and many bacteria carry out

Back 201

Alcohol fermentation under anaerobic conditions

Front 202

Certain fungi & bacteria perform

Back 202

Lactic acid fermentation in the product of cheese & yogurt.

Front 203

Human muscle cells make

Back 203

Lactic acid under anaerobic conditions during strenuous exercise

Front 204

Lactic acid fermentation in muscle cells cause

Back 204

An "oxygen debt" which is paid back when oxygen is replenished

Front 205

Human muscle cells make

Back 205

Lactic acid under anaerobic condition during strenuous exercise

Front 206

Aerobic respiration

Back 206

Uses electron transport

Mosh oxidative some substrate level phosphorylation

Front 207

Aerobic respiration

Back 207

Uses electron transport

Mosh oxidative some substrate level phosphorylation

Front 208

Anaerobic respiration

Back 208

Uses electron transport chain

Oxidative phosphorylation

Front 209

Aerobic respiration

Back 209

Uses electron transport

Mosh oxidative some substrate level phosphorylation

Front 210

Anaerobic respiration

Back 210

Uses electron transport chain

Oxidative phosphorylation

Front 211

Fermentation

Back 211

Aerobic or anaerobic

Does not use electron transport chain

Substrate level phosphorylation

Front 212

Fermentation

Back 212

Is the breakdown of carbohydrates without the use of oxygen to produce ATP

Front 213

Fermentation

Back 213

Is the breakdown of carbohydrates without the use of oxygen to produce ATP

Front 214

Facultative anaerobes

Back 214

Yeasts and many bactera

Produce ATP by fermentation or respiration depending on whether oxygen is present

Front 215

Fermentation

Back 215

Is the breakdown of carbohydrates without the use of oxygen to produce ATP

Front 216

Facultative anaerobes

Back 216

Yeasts and many bactera

Produce ATP by fermentation or respiration depending on whether oxygen is present

Front 217

A gram of fat contains

Back 217

twice the amount of energy ATP as gram of carbohydrate

Front 218

Fermentation

Back 218

Is the breakdown of carbohydrates without the use of oxygen to produce ATP

Front 219

Facultative anaerobes

Back 219

Yeasts and many bactera

Produce ATP by fermentation or respiration depending on whether oxygen is present

Front 220

A gram of fat contains

Back 220

twice the amount of energy ATP as gram of carbohydrate

Front 221

Fats more

Back 221

Energy than carbohydrate

Front 222

Glycolysis slowd

Back 222

Down if ATP or citric acid accumulates

Front 223

During (all of or one complete cycle of) cellular respiration

Back 223

38 ATP molecules are liberated

Front 224

During the aerobic phase of cellular respiration

Back 224

36 ATP molecules are liberated

Front 225

During the aerobic phase of cellular respiration

Back 225

36 ATP molecules are liberated

Front 226

During the anaerobic phase of cellular respiration

Back 226

2 ATP molecules are liberated