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Micro exam 2
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Preguntas del test (136)
1What does the outer membrane of a gram - cell envelope compare to?
- AAn ionic screen.
- BA molecular screen.
- CA lipid screen.
2What is the permeability of the outer membrane of a gram - cell envelope?
- ASelectively permeable.
- BNot permeable.
- CCompletely permeable.
3What does the bilamminar outer membrane of a gram - cell envelope contain a lot of?
- AGlycolipid
- BMonosaccharide
- CPeptidoglycan
4How many layers does a gram - cell envelope contain?
- A4
- B3
- C2
5What does the thin cell wall of a gram - cell envelope contain?
- AGlucose
- BPeptidoglycan
- CLipopolysaccharide
6What are the three layers of a gram negative cell envelope?
- Aouter mem, thin cell wall (peptidoglycan), then cell mem
- Benvelope, outer mem, thin cell wall, cell mem
- Cthin cell wall, cell mem
7What does the outer membrane of a gram - cell envelope do?
- Ablocks all antibiotics, bile salts, and enzymes.
- Bblocks enzymes, bile salts, and some antibiotics
- Cblocks enzymes and some antibiotics.
8What is bacterial lipopolysaccharide made up of?
- ADiphosphoryl Lipid A (2 phosphate groups), a core pholysaccharide (unusual sugars), and an outer (A polysaccharide, A antigen)
- BDiphosphoryl Lipid A (2 phosphate groups), a core pholysaccharide (unusual sugars), and an outer (O polysaccharide, O antigen)
- CDiphosphoryl Lipid A (1 phosphate groups), a core pholysaccharide (unusual sugars), and an outer (O polysaccharide, O antigen)
9What is the inner leaflet of a bacterial lipopolysaccharide?
- Aphospholipid bilayer
- Blipid bilayer
- Cglycogen layer
10What is the outer leaflet of a bacterial lipopolysaccharide?
- ALipopolysaccharide
- BMonosaccharide
- CPolysaccharide
11What bacterial type is bacterial lipopolysaccharide present?
- AGram -
- BGram +
12What is the arrangement of the bacterial cell membrane?
- Aouter to inner
- Binner to outer
13chemical composition of the bacterial cell membrane?
- A- Lipopolysaccharide (O polysaccharide, Lipid A), Cell wall (outer mem, peptidoglycan), plasma mem
- B- Cell wall (outer mem, peptidoglycan),Lipopolysaccharide (O polysaccharide, Lipid A), plasma mem
- CLipopolysaccharide (O polysaccharide, Lipid A), plasma membrane, cell wall
14What does the bacterial cell wall do?
- A- completely permeable
- Site of glycolysis
- Point of attachment for flagella or pili- LPS
- binds to specific receptors (CD14, TLR4) on macrophage, B cells, and other cells
- stim production and release of acute phase cytokines (interluin 1,6, TNF, prostaglandins)
- fever production - B- Selectively permeable
- Site of electron transport chain
- Point of attachment for flagella or pili
- LPS
- activate inflammatory response
- binds to specific receptors (CD14, TLR4) on macrophage, B cells, and other cells
- stim production and release of acute phase cytokines (interluin 1,6, TNF, prostaglandins)
- fever production - C- Selectively permeable
- Site of krebs cycle
- Point of attachment for flagella or pili
- LPS
- activate inflammatory response
- binds to specific receptors (CD14, TLR4) on macrophage, B cells, and other cells
- stim production and release of acute phase cytokines (interluin 1,6, TNF, prostaglandins)
- fever production
- A- completely permeable
15What protein is bacterial flagellum made of?
- Aflagellin
- Bflagellis
- CRna
16Size of bacterial flagellum?
- A- rigid helix about 20nm in diameter and several times the length of the bacteria
- B- rigid helix about 15nm in diameter and several times the length of the bacteria
- C- rigid helix about 10nm in diameter and several times the length of the bacteria
17Bacterial flagellum shape?
- ASquare
- BHelix
- CSphere
18arrangements flagella may have?
- A- polar or monotrichous
- tuft or lophotrichous
- around the entire cell or peritrichous - B- polar or monotrichous
- around the entire cell or peritrichous - C- non polar or monotrichous
- tuft or lophotrichous
- around the entire cell or peritrichous
- A- polar or monotrichous
19State the mechanism of flagellar movement.
- A- rotary motor
- clockwise- straight line - B- rotary motor
- clockwise- straight line
- counterclockwise- random change in direction - C- move with no motor
- clockwise- straight line
- counterclockwise- random change in direction
- A- rotary motor
20What is the difference between prokaryotic and eukaryotic flagella?
- A- prokaryotic made up of a single protein repeated called flagellin
- Eukaryotic made of the 9+2- 9 doublets of microtubules and 2 single microtubules in the middle - B- prokaryotic made up of a single protein repeated called amino acids
- Eukaryotic made of the 9+2- 9 doublets of microtubules and 2 single microtubules in the middle - C- prokaryotic made up of a single protein repeated called flagellin
- Eukaryotic made of the 9+1- 9 doublets of microtubules and 2 single microtubules in the middle
- A- prokaryotic made up of a single protein repeated called flagellin
21Structure of the bacterial pilus?
- Aprotein filaments considerably shorter than flagella, thin, 3-15nm
- Bprotein filaments considerably longer than flagella, thin, 20-30nm
- Cprotein filaments considerably shorter than flagella, thin, 3-20nm
22Function of bacterial pilus?
- Aadherence of bacteria to prokaryotic cells – important in initiation of disease
- Badherence of bacteria to eukaryotic cells – important in initiation of disease
- Cadherence of bacteria to eukaryotic cells – important in stopping a disease
23Location of bacterial pilus?
- APoles of the cell or spread over the surface
- BOnly at poles.
- COnly spread over the surface.
24biochemical makeup of bacterial pilus?
- Aglycoproteins specific for sugar residue on host peptidoglycan
- Bmonosaccharides specific for sugar residue on host glycoprotein
- Cglycoproteins specific for sugar residue on host glycoprotein
25biochemical makeup of the bacterial capsule?
- Apolysaccharide
- Bmonosaccharide
- Cdisaccharide
26Location of bacterial capsule?
- Athe outer envelope of a bacterial cell.
- Bthe outer membrane of a bacterial cell.
- Cthe inner membrane of a bacterial cell.
27Function of a bacterial capsule?
- A- prevents antibody response
- inhibit phagocytosis by WBCs makes them slippery - B- stim antibody response
- inhibit phagocytosis by WBCs makes them slippery - C- stim antibody response
- inhibit phagocytosis by WBCs makes them dry.
- A- prevents antibody response
283 examples of pathogenic bacteria that have capsules.?
- A- Lyme disease
- Streptococcus pneumoniae
- Hemophilus influenzae - B- Neisseria meningitides
- Streptococcus pneumoniae
- Hemophilus influenzae - C- Neisseria meningitides
- Bacillus anthracis
- Hemophilus influenzae
- A- Lyme disease
29structure of bacterial ribosome?
- Asubcellular organelles, 70s, subunits of a 50s and a 40s (large and small subunits)
- B70s, subunits of a 50s and a 30s (large and small subunits)
- Csubcellular organelles, 70s, subunits of a 50s and a 30s (large and small subunits)
30Function of a bacterial ribosome?
- Asite of protein packaging
- Bsite of atp generation
- Csite of protein synthesis
31Which antibiotic binds to 50S portion and inhibits formation of peptide bond – interferes with the peptidyl transferase
- ATetracycline
- BStreptomycin
- CErythromycin
- DChloramphenicol
32Which antibiotic interferes with attachment of tRNA to mRNA- ribosome complex- binds to 30s subunit?
- ATetracycline
- BChloramphenicol
- CErythromycin
- DStreptomycin
33Which antibiotic changes shape of 30s portion, causes code on mRNA to be read incorrectly – shifts the mRNA- misreading= wrong amino acid inserted?
- AErythromycin
- BStreptomycin
- CTetracycline
- DChloramphenicol
34Which antibiotic binds to 50s portion, prevents translocation- movement of ribosome along mRNA?
- AStreptomycin
- BChloramphenicol
- CTetracycline
- DErythromycin
35mechanism of bacterial resistance to Chloramphenicol?
- AAcetylation rxn
a. Add an acetyl group to the antibiotic- the antibiotic no longer functions normally
b. Str. + Ac CoA- (acetylase (bacteria))- str.-Ac +CoA (inactive) - Bchlor + Acetyl CoA chlor-AC + CoA (inactive)
a. Acetylase- bacterial enzyme - Cresistant strains pump antibiotic out of the cell
- Dmethylation (add a methyl group CH3) of 2 adenine residues on 23S rRNA on large subunit. a. 23S rRNA has 2 methyl groups- has enzyme methylase
- AAcetylation rxn
36mechanism of bacterial resistance to Streptomycin?
- Aresistant strains pump antibiotic out of the cell
- BAcetylation rxn
a. Add an acetyl group to the antibiotic- the antibiotic no longer functions normally
b. Str. + Ac CoA- (acetylase (bacteria))- str.-Ac +CoA (inactive) - Cmethylation (add a methyl group CH3) of 2 adenine residues on 23S rRNA on large subunit. a. 23S rRNA has 2 methyl groups- has enzyme methylase
- Dchlor + Acetyl CoA chlor-AC + CoA (inactive)
a. Acetylase- bacterial enzyme
37mechanism of bacterial resistance to tetracycline?
- Amethylation (add a methyl group CH3) of 2 adenine residues on 23S rRNA on large subunit. a. 23S rRNA has 2 methyl groups- has enzyme methylase
- BAcetylation rxn
a. Add an acetyl group to the antibiotic- the antibiotic no longer functions normally
b. Str. + Ac CoA- (acetylase (bacteria))- str.-Ac +CoA (inactive) - C1. Chloramphenicol: chlor + Acetyl CoA chlor-AC + CoA (inactive)
a. Acetylase- bacterial enzyme - Dresistant strains pump antibiotic out of the cell
38mechanism of bacterial resistance to Erythromycin?
- Amethylation (add a methyl group CH3) of 2 adenine residues on 23S rRNA on large subunit. a. 23S rRNA has 2 methyl groups- has enzyme methylase
- BAcetylation rxn
a. Add an acetyl group to the antibiotic- the antibiotic no longer functions normally
b. Str. + Ac CoA- (acetylase (bacteria))- str.-Ac +CoA (inactive) - Cresistant strains pump antibiotic out of the cell
- Dchlor + Acetyl CoA chlor-AC + CoA (inactive)
a. Acetylase- bacterial enzyme
39Which of these is NOT a mechanism of the selective toxicity of these anti-ribosomal antibiotics?
- AMitochondria have 70S
- BRER in eukaryotes cells have 80S ribosomes
- CRER in eukaryotes have 30S ribosomes
- DMore toxic to target (bacteria) than to host
40Is an endospore a survival structure?
- AYes
- BNo
41What is an endospore NOT resistant to?
- Aheat
- B>6 hours boiling and autoclaving
- Cchemicals
- Dradiation
42What does a non-enveloped virus NOT include?
- Aphospholipid bilayer of host cell
- Bprotein capsid
- Cspike proteins on the virus itself
43Where is the viral protein embedded in an enveloped virus?
- AmRNA
- Bnucleic acid
- Cphospholipid bilayer
- Dthe envelope
44Which of these is an enveloped double stranded DNA virus?
- APolio
- BHIV
- CFlu
- DHerpes
45Which of these is an enveloped single-stranded RNA virus that produces DNA?
- APolio
- BHIV
- CFlu
- DHerpes
46Which of these is a non-enveloped single-stranded RNA + strand virus?
- APolio
- BHIV
- CFlu
- DHerpes
47Which of these is an enveloped multiple strand of RNA virus?
- APolio
- BHIV
- CFlu
- DHerpes
48Do viruses possess a cell structure?
- AYes
- BNo
49T or F- viruses do not possess a cell structure because they are not a cell particle, they are assembled.
- AT
- BF
50What does a virus NOT contain?
- ANucleic acid
- BOuter shell of protein
- CLipid of host cell origin
- DBoth DNA and RNA
51Do viruses have to be inside a cell to survive and do its job?
- AYes
- BNo
52T or F: viruses divide but don't assemble.
- AT
- BF
53Does a virus use a host cell?
- AYes
- BNo
54What does a virus NOT lack?
- Aorganelles
- Bsensitivity to interferon
- CATP synthesis enzymes (glycolysis, krebs, ETC)
- Denzymes for macromolecular biosynthesis (nucleic acids, protein, polysaccharides, phospholipids)
55Which of these is NOT a portal of entry?
- ARespiratory
- BUrogenital
- COral, fecal, GI
- DParental
- ENone of the above
56Pick the correct order of the viral replication cycle.
- APortal of entry, Absorption to a host cell surface , Entry into host cell, Uncoating, Viral genome replication, Absorption to a host cell surface, Late protein synthesis, Maturation and assembly, Release from the host cell
- BPortal of entry, Entry into host cell, Absorption to a host cell surface, Uncoating, Early viral protein synthesis, Viral genome replication, Late protein synthesis, Maturation and assembly, Release from the host cell
- CPortal of entry, Absorption to a host cell surface , Entry into host cell, Uncoating, Early viral protein synthesis, Viral genome replication,Maturation and assembly, Late protein synthesis, Release from the host cell
- DPortal of entry, Absorption to a host cell surface , Entry into host cell, Uncoating, Early viral protein synthesis, Viral genome replication, Late protein synthesis, Maturation and assembly, Release from the host cell
57ENTRY- how do non and enveloped viruses enter a host cell?
- Areceptor- mediated exocytosis (cells plasma membrane folds inward to form holes) and fusion (viral envelope fuses with the plasma membrane and releases the capsid into the cells cytoplasm).
- Breceptor- mediated endocytosis (cells plasma membrane folds inward to form vesicles) and fusion (viral envelope fuses with the plasma membrane and releases the capsid into the cells cytoplasm).
- Creceptor- mediated endocytosis (cells plasma membrane folds inward to form vesicles) and fusion (viral envelope fuses with the capsid and releases the capsid into the cells cytoplasm).
- Dreceptor- mediated exocytosis (cells plasma membrane folds outward to form vesicles) and fusion (viral envelope fuses with the plasma membrane and releases the capsid into the cells cytoplasm).
58ABSORPTION- what is the separation of the viral nucleic acid from its protein coat? Some animal viruses use lysosomal enzymes to degrade the proteins of the viral capsid.
- AUncoating
- BCoating
- CSpouting
- DRelease
59Which step is this- enzymes (RNA polymerase, R polase). Toxic factors to shut down host macromolecular biosynthesis.
- AEarly viral protein synthesis
- BLate protein synthesis
- CBiosynthesis
- DTranslation
60VIRAL GENOME REPLICATION- Which virus has a + strand (mRNA) must be first transcribed from the - viral genome before proteins can be synthesized. Additional - strands are transcribed from mRNA. - strands are incorporated into capsid.
- APolio
- BHerpes
- CHIV
- DFlu
61Which step is the release from host cell of mature infectious viron?
- ARelease
- BMaturation
- CMaturation and release
- DBudding release
62Non-envelope release?
- ABudding
- BPopping
- CLytic
- DVesicle
63enveloped release?
- Abudding
- Blytic
- Cvesicle
- Dslow
64What step
i. Structural proteins (collagen)
1. Capsid proteins- called capsomere- structure and is composed of capsomeres (individual prot)
2. Spike protein- Alate protein synthesis
- Bearly protein synthesis
- Cmaturation
- Drelease
65What types of flu virus types are there?
- AA, B
- BA
- CB, C-
- DA, B, C-
66What flu types infect humans?
- AC-
- BB, C-
- CA, B, C-
- DA, B
67T or F- A type flu infects humans, birds, domesticated fowl, and pigs. B only affects humans.
- AT
- BF
68Does flu type A have 16 H's and 9 N's?
- AYes
- BNo
69What is the structure of the flu virus?
- AHA and NA spikes, envelope, 8 RNA sequences diff lengths.
- BHA, envelope, 8 RNA sequences diff lengths.
- CHA and NA spikes, envelope, 6 RNA sequences diff lengths.
- DNA spikes, non-enveloped, 8 RNA sequences diff lengths.
70Function of HA spikes?
- Ainvolved in release of the bud from host cell mem
- Brecognition
- Crecognition and involved in attachment to host
71NA spike function?
- Aprotection of virus
- Binvolved in release of the bud from host cell mem
- Cattachment and recognition
72What is antigenic drift?
- Ayear to year variation- variation of genetic makeup of virus- slow change throughout course of the year
- BSlow year to year change accounts for epidemic flu
- Cchange in nucleotide sequence die to RNA polase errors- mutation can result in diff amino acid protein.
- Dstructure changes diff antigenic structures.
- Eall of the above
73What is antigenic shift?
- Avariation of genetic makeup of virus- slow change throughout course of the year
- Bchange in nucleotide sequence
- Cdiff amino acid protein
- Dsudden dramatic results in flu virus genome that’s new to our immune system- produces HA not seen by host immune system before- can produce pandemic influenza
74T or F- - PIGS CAN AT THE SAME TIME BE INFECTED WITH PIG FLU, AVIAN FLU, AND HUMAN FLU- RNA sequences get mixed up and pig infected with “new virus”-combo of three- CAN INFECT HUMANS- problem bc it’s a completely new flu
- AT
- BF
75How does the drift and shift relate to the evolution of the flu?
- Athe virus selects for the mutation that the immune system is not yet immune to so that it is one step ahead of the immune system
- Bantigenic shift creates a new flu so it will spread rapidly bc our immune system has not seen it before
- Cboth of these
76What is the relationship between antigenic drift, and the need for a new influenza vaccine each year?
- Athe HA glycoprotein slowly changes throughout the year and the vaccine only protects against a specific HA protein- when change need new vaccine for new HA protein
- Bthe NA glycoprotein slowly changes throughout the year and the vaccine only protects against a specific NA protein- when change need new vaccine for new NA protein
- Cthe HA glycoprotein quickly changes throughout the year and the vaccine only protects against a specific HA protein- when change need new vaccine for new HA protein
- Dthe HA glycoprotein slowly changes throughout the year and the vaccine only protects against a specific NA protein- when change need new vaccine for new HA protein
77Describe the process of antigenic shift within humans, birds, and pigs.
- A-pig, human, and bird flu all infect pig at same time- the RNA strands mix so there are a few strands from each flu to make up a new flu
- B-pig, human, and bird flu all infect pig at same time- the DNA strands mix so there are a few strands from each flu to make up a new flu
- C-pig, human, and bird flu all infect pig at same time- the RNA strands mix so there is one strand from each flu to make up a new flu
- D-pig, human, and bird flu all infect pig at a different time- the RNA strands are the same so there is no new flu.
78What is metabolism?
- Aprocesses synthesize and assemble subunits of macromolecules that `makeup the cell structures- USE ATP
- Bprocesses harvest the energy released during the breakdown of compounds and use it to MAKE ATP
- Cthe sum total of all biological reactions within a cell
79What is catabolism?
- Aprocesses harvest the energy released during the breakdown of compounds and use it to MAKE ATP
- Bprocesses synthesize and assemble subunits of macromolecules that `makeup the cell structures- USE ATP
- Cthe sum total of all biological reactions within a cell
80What is anabolism?
- Aprocesses harvest the energy released during the breakdown of compounds and use it to MAKE ATP
- Bprocesses synthesize and assemble subunits of macromolecules that `makeup the cell structures- USE ATP
- Cthe sum total of all biological reactions within a cell
81Define the term activation energy.
- AThe amount of energy it takes for an reaction to take place in a physiological system
- BThe amount of energy it takes for an reaction to take place in a biological system
- CThe amount of energy it takes for an reaction to take place within a cell.
- DThe amount of energy it takes for an reaction to take place in a human.
82Do enzymes lower the activation energy in a reaction or make it higher?
- AHigher
- BLower
83Oxidation rxn example?
- AC6H12O6--> 6CO2
- Bo2-->H2O
- Cadding water
- Dmake bond
84Reduction rxn example?
- AC6H12O2-->6CO2
- Bo2-->H20
- Cadding water
- Dmake bond
85example of hydrolysis?
- Aadding water and breaking a bond
- Bo2--->H20
- CC6H12O6--> 6O2
- Dmake bond
86Biosynthesis example?
- Amake bond
- Bprotein from amino acids. make macromolecules.
- Cadding water
- Dbreaking a bond
87What is the unique characteristic of biological systems that allows chemical reactions that normally require high temperatures and pressures to occur at room temperature and one atmosphere of pressure?
- Aglycolysis
- Bproteins
- Cenzymes
- DETC
88Describe the 3 characteristics of an enzyme catalyzed reaction
- Aincrease reaction rate (substrate to product)
- lower the activation energy required for reaction
- not used up by reaction so it is reused - Bincrease reaction rate (substrate to product)
- higher the activation energy required for reaction
- not used up by reaction so it is reused - Cincrease reaction rate (substrate to product)
- lower the activation energy required for reaction
- used up by reaction - Ddecrease reaction rate (substrate to product)
- lower the activation energy required for reaction
- not used up by reaction so it is reused
- Aincrease reaction rate (substrate to product)
89What class of macromolecules do enzymes belong to?
- Asugars
- Bcarbs
- Cproteins
90what physical factors affect enzyme activity?
- ApH
- Btemp
- Cchemicals
- DpH and temp
91what is a substrate?
- Athe substance on which an enzyme acts
- Bthe molecule on which an enzyme acts
- Cthe macromolecule on which an enzyme acts
92T or F: peptide bond, the carboxyl group (COOH) of one amino acid bonds with the amino group (NH2) of another, forming the sequence CONH and releasing water (H2O).
- AT
- BF
93How is a peptide bond formed by dehydration synthesis?
- A- dehydration synthesis is when a water molecule is added and a peptide bond is formed by the attachment of C and N
- B- dehydration synthesis is when a water molecule is removed and a peptide bond is formed by the attachment of H and N
- C- dehydration synthesis is when a water molecule is added and a peptide bond is formed by the attachment of H and N
- D- dehydration synthesis is when a water molecule is removed and a peptide bond is formed by the attachment of C and N
94Primary structure of an enzyme?
- Anumber, type, and sequence of amino acids (polypeptide strand)
- BAlpha helix
- CBeta pleated sheet
- DGlobular (folds)
95Secondary structure of an enzyme?
- Ahelix and pleated sheets (with 2 polypeptide strands)
- Bfolded helix sheet
- Chelix and pleated sheets (with 3 polypeptide strands)
- Dpleated sheet
96Tertiary structure of an enzyme?
- Atwo or more polypeptides in their folded states
- Bfolded helix and pleated sheet
- Chelix sheet
- Dpolypeptide strand
97What bonds are associated with a tertiary structure?
- AHydrogen bond, disulfide bridge (between cysteine molecules), lysine R, Valine R G.P
- BHydrogen bond, disulfide bridge
- CHydrogen bond
- Dlysine R, Valine R G.P
98Niacin is a coenzyme. What does it do?
- ARiboflavin- FAD (proton acceptor
- Bcoenzyme used in electron transport
- Cvitamin- produces coenzyme NAD (Proton and electron acceptor)
99Vitamin B2 is a coenzyme. Function?
- Acoenzyme used in electron transport
- BRiboflavin- FAD (proton acceptor)
- Cinvolved in carob dioxide fixation reaction and fatty acid synthesis
100What is biotin?
- AA coenzyme that is involved in carob dioxide fixation reaction and fatty acid synthesis
- BA coenzyme used in electron transport
- CA coenzyme that produces NAD
101Where is the enzyme vitamin K used?
- AKrebs cycle
- Bfermentation
- Cglycolysis
- Delectron transport chain
102What are the two types of enzymes based on site of activity?
- A- Extracellular and Intercellular enzymes
- B- intercellular and Intracellular enzymes
- C- Extracellular and Intracellular enzymes
103What is an extracellular enzyme?
- Aan enzyme that is secreted by a cell and functions outside of that cell.
- Ban enzyme that is secreted by a cell and functions inside of that cell.
104What is an intracellular enzyme?
- Aan enzyme that functions within the cell in which it was produced.
- Ban enzyme that functions outside the cell in which it was produced.
105What type of reactions are catalyzed by extracellular enzymes?
- Aenergy production and biosynthesis
- Bhydrolases- break bonds by the insertion of water
106What type of reactions are catalyzed by intracellular reactions?
- Aenergy production and biosynthesis
- Bbreak bonds by the insertion of water
107T or F: - pH: most bacteria grow at pH 7 or less enzyme activity at 6 – yeast and mold grow in acidic environments
- ATrue
- BFalse
108T or F: most enzymes function at 40 deg C, increase in temp= denaturation--> less of enzyme activity and loss of 2 and 3 degree structures
- ATrue
- BFalse
109What causes protein denaturation?
- Athe loss of primary and tertiary structure (S-S, h bonds, hydrophobic interactions, ionic bonds)
- Bthe loss of secondary structure
- Cthe loss of tertiary structure
- Dthe loss of secondary and tertiary structure (S-S, h bonds, hydrophobic interactions, ionic bonds)
110Describe the role of substrate concentration on enzyme reaction rate.
- A- Enzyme works at diff rate until all of the active sites are full with substrate- no more enzymes will be made
- B- Enzyme works at the same rate until all of the active sites are full with substrate- more enzymes will be made
- C- Enzyme works at the same rate until all of the active sites do not have substrates- no more enzymes will be made
- D- Enzyme works at the same rate until all of the active sites are full with substrate- no more enzymes will be made
111Define the term reaction rate.
- AReaction rate is the speed at which a chemical reaction proceeds
- BReaction rate is the speed at which a chemical reaction declines.
112T or F: - -an enzyme under high substrate concentration is in saturation that is its active site is always occupied by substrate or product molecules. it is catalyzing a specific reaction at its maximum rate.
- AT
- BF
113Active site?
- Aa region on an enzyme that interacts with the substrate
- Bsite on an enzyme at which a noncompetitive inhibitor binds
114allosteric site?
- Aa region on an enzyme that interacts with the substrate
- Bsite on an enzyme at which a noncompetitive inhibitor binds
115T or F: Active site is involved in regulation of enzyme activity
- AT
- BF
116o This regulation is called feedback inhibition or end product
- A- Allosteric site is involved in regulation of enzyme activity
- B- Active site is involved in regulation of enzyme activity
117T or F: o When a concentration of product is high enough it binds to allosteric site of 1st enzyme pathway so it stops
- AT
- BF
118what fills the active site of an enzyme and competes with the normal substrate for the active site? It can do this because its shape and chemical structure are similar to those of the normal substrate
- Acompetitive inhibition of enzyme activity
- Bnon-competitive inhibition of enzyme activity
119T or F: penicillin is a competitive inhibitor of bacterial enzyme transpeptidase- looks for Ala-ala
- AT
- BF
120What do not compete with the substrate for the enzymes active site they interact with something else like the allosteric site ?
- Acompetitive
- Bnon-competitive
121What is meant by end-product or feedback inhibition of enzyme activity?
- A- When there is enough end product it binds to the allosteric site of the second enzyme in the sequence this changes the active site shape and then shuts off the pathway
- B- When there is not enough end product it binds to the allosteric site of the first enzyme in the sequence this changes the active site shape and then shuts off the pathway
- C- When there is enough end product it binds to the allosteric site of the first enzyme in the sequence this changes the active site shape and then shuts off the pathway
- D- When there is enough end product it binds to the active site of the first enzyme in the sequence this changes the active site shape and then shuts off the pathway
122what way do cells NOT use chemical energy in the form of ATP?
- A- Transport work- requires ATP to move things across membrane
- B-diffusion
- C- Biosynthesis- Duplication of cell components- cell division
- D- Mechanical work- flagella rotation
123Define the term cellular energy metabolism.
- A- Convert the chemical energy present in reduced organic compounds (C6H12O6)
- B- Convert the chemical energy present in reduced organic compounds (C6H12O6) into the metabolically usable energy of ATP (glycolysis, kerbs, ETC)
- C- Convert the chemical energy present in reduced organic compounds (C6H12O6) into the metabolically usable energy of NAD+ (glycolysis, kerbs, ETC)
- D- Convert the chemical energy present in dehydrated organic compounds (C6H12O6) into the metabolically usable energy of ATP (glycolysis, kerbs, ETC)
124What reactions are energy yielding reactions- make ATP
- ABiological
- BOxidation
- CReduction
125What reaction gets rid of its proton and electron to NAD?
- ABiological
- BOxidation
- CReduction
126What reaction gains a proton and electron from glucose?
- ABiological
- BOxidation
- CReduction
127Describe the steps in the successive oxidation of methane to carbon dioxide.
- A- Methane (4 H)
- Formaldehyde (2 H) aldehyde
- Formic acid (1 H) acid
- CO2
- As the 4 H atoms are removed there is a stepwise loss of available energy - B- Methanol (3 H) alcohol
- Methane (4 H)
- Formaldehyde (2 H) aldehyde
- Formic acid (1 H) acid
- CO2
- As the 4 H atoms are removed there is a stepwise loss of available energy - C- Methane (4 H)
- Methanol (3 H) alcohol
- Formaldehyde (2 H) aldehyde
- Formic acid (1 H) acid
- As the 4 H atoms are removed there is a stepwise loss of available energy - D- Methane (4 H)
- Methanol (3 H) alcohol
- Formaldehyde (2 H) aldehyde
- Formic acid (1 H) acid
- CO2
- As the 4 H atoms are removed there is a stepwise loss of available energy
- A- Methane (4 H)
128Define the term cellular respiration?
- Ais a set of metabolic reactions and processes that take place in the cells of organisms to convert biochemical energy from nutrients into adenosine triphosphate (ATP), and then release waste products.
- Bis a set of metabolic reactions and processes that take place in the cytoplasm of cells of organisms to convert biochemical energy from nutrients into adenosine triphosphate (ATP), and then release waste products.
- Cis a set of metabolic reactions and processes that take place in the mitochondria of cells of organisms to convert energy from nutrients into adenosine triphosphate (ATP), and then release waste products.
- Dis a set of metabolic reactions and processes that take place in the cells of organisms to convert biochemical energy from nutrients and then release waste products.
129Where does cellular respiration in eukaryotic cells?
- Ain cell, krebs on mitochondria, ETC mitochondria
- Bin cell and ECT on cell mem
130Where does cellular respiration occur prokaryotic cells?
- Aglycolysis- in cell, krebs on mitochondria, ETC mitochondria
- Bin cell and ECT on cell mem
131Fermentation carbon flow
- Aorganic compounds --> fermentation products (lactic acid, gas)
- Borganic compounds --> fermentation products (lactic acid, alcohol, gas)
- Corganic compounds --> fermentation products (alcohol, gas)
132Fermentation electron flow
- Ainternal oxidation reduction- substitute for O2 (some intercellular compound serve as H+ and e- acceptor)
- Binternal oxidation reduction- substitute for O2 (some intracellular compound serve as H+ acceptor)
- Cinternal oxidation reduction- substitute for O2 (some intracellular compound serve as e- acceptor)
- Dinternal oxidation reduction- substitute for O2 (some intracellular compound serve as H+ and e- acceptor)
133T or F: fermentation electron flow net gain is 2 ATP
- AT
- BF
134Respiration carbon flow
- Aorganic compounds--> O2 (completely oxidized no more potential energy)
- Borganic compounds-->CO2 (completely oxidized no more potential energy)
- Corganic compounds-->CO2 ( not completely oxidized no more potential energy)
- Dorganic compounds--> CO2 (not completely oxidized, more potential energy)
135electron flow respiration
- AO2 (terminal H+ and e- acceptor)
- BO2 (neither an H+ or e- acceptor)
- CO2 (terminal H+ acceptor)
- DO2 (t e- acceptor)
136ATP net gain respiration
- A35
- B43
- C36-38
- D38-40
Información
- Descripción
- Test sobre Micro exam 2, creado por Madeline Mondoro el 15/03/2019.
- Autor
- Madeline Mondoro
- Idioma
- English
- Visitas
- 12
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