Microbiology Unit 2 Exam

Front 1

Energy ( E)

Back 1

Capacity to do work

Front 2

Prokaryotes utilize______ to do work

Back 2

Energy

Front 3

Chemical Energy

Back 3

Breaking bonds, & joining and linking elements through bonding.

Front 4

Metabolism

Back 4

Sum total, the complete collection of all the biochemical reactions required to produce the energy needed to survive.

Front 5

Survival involves:

Back 5

Reproduce, maintain, repair, function

Front 6

2 Major groups of metabolic reactions:

Back 6

Catabolism & Anabolism

Front 7

Metabolic pathways the 2 major groups are

Back 7

opposite

Front 8

Catabolism:
release E
Degredation of a substance
Process of oxidation involved- loss of electron which would result in a positive charge on the ion

Back 8

Anabolism
E is aquired, stored & used
Synthesis of a substance
Reduction is involved- gain of electron, which would result in a negative charge on an ion

Front 9

ATP ( Adrenosine Triphosphate Production)

Back 9

Quantity that an organism produces

Front 10

ATP -------->ADP + P (----->E)
Catabolize- degrading, so it is ADP- "disulfide"
Seperated a phosphate & E is released
ADP-------->AMP+P (---->E)
M-mono- one phosphate left & attached to a phosphate & releasing energy so the prokaryote can utilize E to complete the metabolic pathway.

Back 10

ATP <===> ADP + P (<---E)
Anabolism-Aquiring energy, adding phosphate to AMP, yielding ADP, aquiring E, phosphate added to ADP, yielding ATP.
Utilizing the stored energy & synthesizing a substance for ATP.

Front 11

Basic mechanism of an Enzyme

Back 11

Enzyme has an active site & there's a specific substrate for that active site on the enzyme. When a specific substrate fits the active site of a specific enzyme, it becomes a complex, yielding in end products.

Front 12

Characteristics of a Simple Enzyme "aka" Apoenzyme

Back 12

1) Is a protien
2) Is organic
3) It's a catalyst.
4)Speeds up biochemical reactions
5) Enzymes reycycle
6) (substrate/reactant)A+B (enzyme)---> C+D (end products)
7) A depletion or deletion of an enzyme will shut down a metabolic pathway.
8) "Lock & key Model"
9) ex. Substrate- lactose----> enzyme Lactase
10) The words of all enzymes end in -ase

Front 13

Characterisitcs of Holoenzyme "aka" Conjugated enzyme

Back 13

APO (apoenzyme) + cofactor-----> Holoenzyme
Cofactor is non-protein

Front 14

2 Types of Cofactors:

Back 14

1) APO+ ORGANIC-----> Holoenzyme
2) APO+ INORGANIC------> Holoenzyme

Front 15

Organic cofactors are called

Back 15

Coenzymes
Ex. NAD ( Nicotinamide Adenine Dinucleotide
NAD is derived from Niacine

Front 16

Inorganic cofactors are called

Back 16

Metallic Ions
Ex. Iron

Front 17

What 4 major factors influence enzomatic action?

Back 17

1. pH
2. Temperature
3. Substrate concentration:
Constitutive- Always present in constant amounts. (Adding substrate doesn't increase the amount)
Induced- present normally in trace amounts.
(Adding substrate DOES increase amount.)
4. Inhibitors

Front 18

2 Categories of Enzyme Inhibitors

Back 18

Competitive inhibition vs. Active site
&
Non- Competitive inhibitor vs Allosteric Site

Front 19

Competitive Inhibitor

Back 19

A substrate of similar structure can fit an active site an therefore, will compete with the specific subtrate. If it occupies the active site it will block normal metabolic pathways.

Front 20

Non- Competitive Inhibitor

Back 20

Non-Competitive vs. Allosteric Site

Front 21

Allosteric Site-

Back 21

Additional regulatory site on an enzyme.
If an enzyme has an allosteric site it is called an allosteric enzyme.

Front 22

Allosteric Enzyme

Back 22

When an End Product (substrate) fits into the allosteric site, the enzyme can't bind with the substrate in the active site, resulting in feedback inhibition. The active site then becomes altered.

Front 23

Enzymes consume nutrients:

Back 23

Nutritional Patterns

Front 24

Phototroph

Back 24

organism that utilizes light energy to synthesize nutrients.

Front 25

Chemotroph

Back 25

derives energy from biochemical reactions and then utilizes it to synthesize nutrients.

Front 26

Autotroph

Back 26

Synthesizes its own food
ex. plants- photosynthesis

Front 27

Heterotroph

Back 27

seeking pre-formed or pre-existing organic nutrients.

Front 28

Photoautotroph

Back 28

light energy and Co2 to synthesize it's nutrients.
Ex. Photosynthetic bacteria , plants & algae

Front 29

Photoheterotroph

Back 29

uses light energy & organic C to synthisize it's nutrients.
Ex. Purple & non- sulfur bacteria

Front 30

Chemoautotroph

Back 30

derive energy from chemical reactions and Co2 to synthesize nutrients.
Ex. Nitrobactor

Front 31

Chemoheterotrophs

Back 31

derive energy from chenical reactions & organic C to synthesize nutrients.
Ex. Most bacteria & all animals

Front 32

Energy Formation for Chemoheterotrophs

Back 32

Aerobic & Anaerobic Respiratio, and Fermentation

Front 33

Glycolysis "aka"

Back 33

Embden Meyerhof Parnas

Front 34

Glycolysis

Back 34

catabolize glucose to anabolize ATP.
occurs in cytoplasm

Front 35

Glucokinase

Back 35

utilize an ATP.
Glucose-----> 2 Pyruvic Acid
glucose yields 2 ATP--> 2 ADP--->2 NAD (coenzyme that picks up H ion and carry them all the way through the process)--->2 NADH (6 ATP)--->2 ADP--->2 ATP--->2 ADP--->2 ATP
so 6 ATP + 2 ATP + 2 ADP= Net 8 ATP

Front 36

2 Alternate Pathways for bacteria:

Back 36

PPP- Pentose Phosphate Pathway &

EDP- Enter-Doudoroff Pathway

Front 37

PPP ( Pentose Phosphate Pathway) "aka"

Back 37

Hexose Monophosphate Shunt

Front 38

PPP Example

Back 38

PPP<-- Glycolysis--->Aerobic
/
Anaerobic
Glycolysis and PPP occur simultaneously. Produces ATP.

Front 39

EDP Example

Back 39

EDP PPP <---Glycolysis----> Aerobic
/
Anaerobic
Does not occur with any other pathway or glycoysis. All on it's own. Utilized by SOME Gram Negative. Don't utilize glucose.

Front 40

Example that uses PPP

Back 40

Escherichia coli

Front 41

Example that uses EDP

Back 41

Pseudomonas- It grows everywhere, and causes many things.

Front 42

Example of pathways

Back 42

EDP PPP<--- Glycolysis
/ \
Anaerobic Aerobic
/ \
Fermentation Kreb Cycle
\
ETS

Front 43

If it occurs under Anaerobic conditions.

Back 43

Oxygen was limited. Which causes Fermentation.

Front 44

Fermentation

Back 44

lack of oxygen
end products are Lactic Acid (animal)& Ethanol (plant)
2 Pyruvic Acid
I (2 NAD)
I (2 NADH) = 6ATP
Lactic Acid & Ethanol

Front 45

If it occurs under Aeobic Conditions
The Traditional Pathway

Back 45

Uses the Kreb Cycle
In the cytoplasm

Front 46

Kreb cycle
Uses NAD & FAD ( not as successful)- coenzymes
1 FAD--> 2 ATP
1 NAD--> 3 ATP

Back 46

2 Pyruvic Acid
} 2 NAD
} 2 NADH = 6ATP
Acetyl Coa
\
\_______Citric Acid
2 NAD-->2 NADH{ } 2 NAD--> 2 NADH= 6 ATP
=6 ATP
2 FAD-->2 FADH { } 2 NAD--> 2 NADH= 6 ATP
=4 ATP 2 ADT<---2 ADP = 2 ATP

Total ATP= 30

Front 47

FAD

Back 47

Is part of the vitamin B complex, derived from Riboflavin
(Vitamins must be used to complete pathway.)

Front 48

With Glycoysis =_8_ ATP
&
With Kreb =__30__ATP
Total ATP=_____

Back 48

38 ATP

Front 49

ETS- Electron Transport System

Back 49

In the cell membrane, Cytochrome

Front 50

Equation of Aerobic Respiration:
Glucose and oxygenated environment in the process of carrying through with attaching phosphate groups that yields 6 molecules of CO2 and 6 molecules of water and finally 38 ATP.

Back 50

(Glucose)C6 H12 O6 + (oxygen) 6O2 + 38 ADP + 38P--->

(carbon dioxide) 6CO2 + 6H2O (water) + 38 ATP

Front 51

Oxidative Phosphorylation Process

Back 51

occuring in an oxigenated environment with the accumulation of phosphates, creating ATP

Front 52

NADH

Back 52

moves into the membrane and carried into the membrane, shot out across the membrane with the use of a pump after transport.

Front 53

Proton pump

Back 53

fueled by ATP, Generates and shoots H ions across the membrane to re-enter the organism, exchanging H ions for Phosphates. Carrying Phosphates.

Front 54

Aeobic Pathway produces

Back 54

ATP, H2O, & CO2

Front 55

Genetics

Back 55

Discussing DNA

Front 56

Chromosomes

Back 56

Cellular structure that carries genes

Front 57

Gene

Back 57

A segment of DNA

Front 58

DNA

Back 58

sequence of nucleotides

Front 59

Genome 1995 science magazine

Back 59

Haemophilus influenzae

Front 60

Genotype

Back 60

Genetic composition in DNA ( not seen)

Front 61

Phenotype

Back 61

Physically expressed . ( can be seen; rods flagella)

Front 62

Synthesize protein

Back 62

DNA---> RNA---> Protein

Front 63

DNA

Back 63

Deoxyribose Nucleic Acid

Front 64

DNA

Back 64

is a polymer composed nucleotides- the monomers

Front 65

Polymers

Back 65

Carbos- polysaccharides
Lipids
protein
nucleic acid

Front 66

monomers

Back 66

monosaccharides
glycerol & Fatty acids
Amino acids
nucleotides

Front 67

nucleic acids are composed of nucleotides. What will change in the nucleotide?

Back 67

the base

Front 68

DNA Structure

Back 68

on one side are the deoxyribose sugar & phosphate group
the bonds in between are Hydrogen
The other side are the bases:
G-Guanine,C- Cytosine,A- Adenine,T- Thymine

Front 69

Primes

Back 69

location on a structure- a poimt of attachment
3' prime & 5' prime

Front 70

DNA have 4 bases divided into 2 groups:

Back 70

Adenine & Guanine- the Purines
Thymine & Cytosine- are the pyrimidine

Front 71

RNA- Ribo Nucleic Acid

Back 71

RNA "DOES NOT" have a pyrimidine of Thymine, instead there is U- Uracil
single strand
with sugar- ribo nucleic acid
Uracil is in the base with RNA

Front 72

Purine + pyrimidine= DNA structure

Back 72

A+T
A+U
G+C

Front 73

Complimentary Base Pairing

Back 73

A T C G
| | | |
T A G C
| | | |
A U C G

Front 74

DNA

Back 74

is anti-parrallel
base matches with base

Front 75

DNA --(Transcription)--> mRNA---(Translation)--> Protein
To write To Read

Back 75

mRNA transcribes and carries message

Front 76

DNA Semiconservative Replication

Back 76

process that replicates using original DNA strand

Front 77

Replication Fork (Y)

Back 77

At the point where the DNA seperates & replicates

Front 78

Leading Strand

Back 78

continuous moving from 5' to 3'.

Front 79

Lagging Strand

Back 79

The lagging moves from 3' to 5' & completes connecting using enzymes

Front 80

Denature

Back 80

DNA unwinds & unzips. (Blue template)The original strand will be used to replicate more DNA. New strands will develope by more neucleotides arriving from the cytoplasm.

Front 81

Joining

Back 81

Old strand or parental strand with the new strand. New strand is called the daughter strand.

Front 82

DNA Polymerase

Back 82

Controlling enzyme, called an editor. Removing the primers, repairing, etc.

Front 83

Ligase

Back 83

In the lagging strand of DNA structure, will bind together the pieces of DNA called the okazaki fragments are linked together with enzyme ligase.

Front 84

Making more DNA at the point of the replication fork involving enzymes in certain directions.

Back 84

In the language of DNA

Front 85

DNA carries instructions for making protein. Protein is the polymer. the monomer is amino acid (aa).

Back 85

aa-(peptide bond)-aa-aa

Front 86

DNA carries instructions and must be written in RNA language to read and carried out by messenger RNA the message will be a nucleic acid to make that protein.

Back 86

Once translated in RNA, Amino acids will be collected in the exact order of request to create a specific protein.

Front 87

Condon

Back 87

RNA language is grouped into 3's (triplets) called

Front 88

We frame each codon for easier view.

Back 88

There are 64 Codons.

Front 89

There are 20 different types of amino acids

Back 89

RNA is formed in frame of a codon.

Front 90

AUG- For Start ( amino acid)

Back 90

Amino acid for stop- UAA,UAG, & UGA

Front 91

A codon is a representative for a word.
genetic code for amino acids. Creates a specific protein.

Back 91

examples
CAU-Histidine
UUC-Phenylalanine
CGC- Arginine

Front 92

Transcription

Back 92

synthesized a complementary strand of RNA now called the message. From the instructions in DNA.

Front 93

Denature

Back 93

DNA seperated, used original template called the sense strand, RNA nucleotides from the cytoplasm come in and match up with the RNA bases, creating messenger RNA .Enzyme involved is RNA Polymerase( used to write the message in RNA language). In orde to read it is the process of translation which is looking at the genetic code chart and reading the message. Other RNA's involved in this process. To read it we use Transfer RNA (tRNA), that has a Reading mechanism called the anticodon.

Front 94

The message in a prokaryote is located

Back 94

in the nuclear region but with other RNA we are moving the message to.

Front 95

Ribosomes

Back 95

Composed of ribosomal RNA. Used in protein synthesis

Front 96

Translation

Back 96

Reading the message of RNA to synthesize a protein in the ribosome.

Front 97

Operon Model

Back 97

Traditional method of explaining transcription & translation. The environment can have a great effect upon gene expression many substances or compounds can be used.

Front 98

Differences between Prokaryotes & Eukaryotes

Back 98

Prokaryote- mRNA is not processed & Traslation of mRNA begins as it's being transcribed.

Eukaryote- The mRNA transcript is transported out of the nucleaus so that it can be translated in the cytoplasm.

Front 99

LAC

Back 99

Lactose Operon Model

Front 100

Escherichia coli

Back 100

lactose metabolized by protein synthesis

Front 101

Representation of lactose

Back 101

Absence of lactose

Front 102

Induction of lactose

Back 102

presence of lactose

Front 103

Operon Off during-

Back 103

repression

Front 104

Operon On during-

Back 104

Induction

Front 105

LAC is an

Back 105

iducible model

Front 106

1st component: Regulator

Back 106

Gene that codes for repression or for repressor

Front 107

2nd component: Control Locus-

Back 107

a promoter
an operator- initiate transcription of the structural genes

Front 108

3rd component: Structural Locus-

Back 108

3 enzymes act upon:
1. beta galactoseidase- catabolizing lactose
2. permease
3. transacetylase

Front 109

Operon off is repression

Back 109

no lactose is present. Regulator- regulating gene.
operator
structural gene 1- lactose is off

Front 110

Operon on repressor

Back 110

active site- altered
lactose will alter active site & unlock it
repressor no longer blocks, operator can proceed & lactose is metabolized

Front 111

Possible mutations

Back 111

DNA(sense strand) T A C G G A G G G T T T

RNA A U G C C U C C C A A A

Front 112

Mutation

Back 112

a permanent & inheritable change in the base sequence of DNA

Front 113

Point Mutation (base substitution)

Back 113

missense- amino acid substitution ( changes the protein)

Front 114

Nonsense

Back 114

involves a substitutive stop (stops the protein to continue)

Front 115

Frameshift mutation

Back 115

addition or loss of a base from codons. this can terminal or deadly

Front 116

Mutation can be either

Back 116

induced (planned)
or
spontaneous (unexpected)

Front 117

Examples of mutations

Back 117

MRSA
Methicillin- Med. to treat Staph.
Staphylococcus aureus

Front 118

3 Types of Transmissions or Mechanisms

Back 118

1. Conjugation- Bacterial sex. Cell to cell contact of 2 related species through a pilus. Plasmids (non-essential DNA) are transferred, resistance factors ( resistant to certain antibiotic) typically gram (-) rods. Donor & recipient are alive.

2.Transformation- transfer of naked DNA fragments. Dead or dying donor. Recipient is alive.

Front 119

Transduction

Back 119

Involves bacteriophage (virus that attacks bacteria) Serves as a carrier of genetics. Both donor & recipient are alive.

Front 120

Recumbant DNA

Back 120

1971 opened/spliced out certain bacteria chromosomes & inserted other chromosomes.

Front 121

Transgenetics

Back 121

inducing foreign gene into bacteria called GEMS (Genetically Engineered Microbes) Can iduce with plants & animals

Front 122

Industrial developed insulin & growth hormones

Back 122

Use certain GEMs

Front 123

DNA or Parental running into 3' to 5' prime strand continuously synthesizes DNA til the end.

Back 123

True

Front 124

Aerobic respiration essay

Back 124

The equation for aerobic respiration
C6 H12 O6 + 6O2 + 38 ADP + 38 P ---> 6 CO2 + 6 H2O + 38 ATP

Front 125

Aerobic essay contin.

Back 125

Glycolysis catabolizes glucose to anabolize ATP which occurs in cytoplasm. Glucose yields a total of 8 ATP. Coenzymes are used to pick up H ions and carry them all the way through the process. The end products are 2molecules of Pyruvic acid that then continue on through the aerobic pathway using the Krebs cycle that is still occurring in the cytoplasm. During the Krebs cycle, coenzymes, NAD Nicotinamide Adenine Dinucleotide which is derived from Niacin & FAD which is derived from riboflavin are used to produce 30 ATP. Now there is a total of 38 ATP. Moving now into the cell membrane the electron transport system occurs. The process of Oxidative Phosphorylation occurs. This is in an oxygenated environment with the accumulation of phosphates, to create ATP. NADH moves into the membrane and carried into the membrane, shot out across the membrane with the use of a pump after transport. The pump is known as a proton pump, fueled by ATP, Generates and shoots H ions across the membrane to re-enter the organism, exchanging H ions for Phosphates. Carrying Phosphates. So glucose and oxygenated environment goes through the process of carrying with it attaching phosphate groups that yield 6 molecules of co2 and 6 molecules of water and finally 38 ATP. There are alternate pathways. The anaerobic which lacks oxygen, goes through the process of fermentation which yields end products of Lactic acid and Ethanol. Two alternate pathways include the PPP, pentose phosphate pathway, which is utilized by Escherichia coli. Glycolysis and PPP occur simultaneously to produce ATP. EDP, Enter- Douordoff Pathway, which is utilized by Pseudomonas; does not occur with any other pathway. It’s all on its own and is used by some gram (-) bacteria. They typically don’t utilize glucose.

Front 126

Basic mechanism of an Enzyme

Back 126

Enzyme has an active site & there's a specific substrate for that active site on the enzyme. When a specific substrate fits the active site of a specific enzyme, it becomes a complex, yielding in end products. An Apoenzyme is also known as a simple enzyme. It is a protein and organic. It’s also a catalyst which speeds up biochemical reactions. A substrate and an enzyme yields end products, so enzymes recycle. A depletion or deletion of an enzyme will shut down a metabolic pathway. It is known for its lock & key model. Enzymes end in –ase. For example lactose will become lactase. If you add an APO with a cofactor it will yield holoenzymes also called conjugated enzyme. A cofactor is not a protein. There are two types of cofactors. Organic& inorganic. Organic cofactors are called coenzymes. An example would be NAD (Nicotinamide Adenine Dinucleotide), which is derived from Niacin. Inorganic cofactors are called Metallic Ions. An example would be iron. Four major factors that influence enzymatic action are pH, temperature, substrate concentration and inhibitors. Substrate concentrations are either constitutive meaning they are always present in constant amounts. Adding substrate doesn’t increase the amount. Or they are induced, meaning they are present normally in trace amounts. Adding substrate does increase amount. There are two categories of enzyme inhibitors; competitive inhibition vs. active site and non-competitive vs. allosteric site. Competitive inhibitor is where a substrate of similar structure can fit in the active site and therefore will compete with the specific substrate. If it occupies the active site it will block normal metabolic pathways. The allosteric site is an additional regulatory site on an enzyme. If an enzyme has an allosteric site it is call an allosteric enzyme. When an end product or substrate fits into the allosteric site, the enzyme can’t bind with the substrate in the active site, resulting in feedback inhibition. The active site then becomes altered. Enzymes consume nutrients. Phototrophs utilize light energy to synthesize nutrients. Chemotrophs derive energy from biochemical reactions to synthesize nutrients. Autotrophs synthesize their own food, such as plants. Heterotrophs seek pre-formed or per-existing organic nutrients. Photoautotrophs use light energy and carbon dioxide. An example is photosynthetic bacteria, plants & algae. Photoheterotrophs use light energy and organic carbon. An example is purple & non-sulfur bacteria. Chemoautotrophs derive energy from chemical reactions and carbon dioxide to synthesize nutrients, such as Nitrobactor. Chemoheterotrophs derive energy from chemical reactions & organic carbon to synthesize nutrients, which are most bacteria and all animals. Energy formation for chemoheterotrophs are aerobic, anaerobic, and fermentation.

Front 127

List and detail mechanisms of genetic transfer.

Back 127

1.Conjugation

Bacterial sex
Cell to cell contact of 2 related species through a pilus.
Plasmids (non-essential DNA) are transferred,
resistance factors ( resistant to certain antibiotic)
typically gram (-) rods.
Donor & recipient are alive.

2. Transformation-
transfer of naked DNA fragments
. Dead or dying donor.
Recipient is alive.

3. Transduction
Involves bacteriophage (virus that attacks bacteria)
Serves as a carrier of genetics.
Both donor & recipient are alive.