Week 1 Flashcards

0
Q

What happens to the Lac Operon when you have high glucose levels?

A

When glucose is high, cAMP is low so cAMP can no longer bind CAP. CAP = gene activator protein. Thus, the gene is operon is turned off.

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1
Q

Explain what happens to the Lac Operon when Lactose levels are high.

A

When lactose levels are high, allolactose levels are high. Allolactose binds to the repressor protein and removes it from the DNA.

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2
Q

What two things need to happen for the Lac Operon to be turned on?

A

Glucose level must be low (high cAMP and high CAP so activator CAP is bound to DNA)
Lactose level must be high (high allolactose which binds to the Lac repressor protein and frees it from the DNA, allowing the DNA to be transcribed)

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3
Q

What happens if you have high glucose and high lactose with a bacterial cell that has the Lac Operon?

A

First the bacteria will use the glucose and then it will use the lactose. First the glucose will prevent the production of cAMP and CAP and prevent the activator from binding to the DNA. Then when glucose is no longer present, the activator will bind and (allolactose from lactose removes the repressor) and then the DNA will be transcribed. The first gene, Lac Z, will produce a produce that splits lactose into glucose and galactose

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4
Q

What molecule exhibits positive cooperativity?

A

Oxygen binding to hemoglobin. This is when an oxygen molecule binds to a single heme (at this pt. hemoglobin has relatively low affinity for oxygen) and then makes the oxygen affinity increase, allowing the second molecule to bind more easily and the third and fourth even more easily. This behavior makes the affinity curve for hemoglobin more sigmoidal, rather than hyperbolic - like myoglobin’s.

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5
Q

What are the shapes of hemoglobin and myoglobin’s affinity curves?

A

Hemoglobin - sigmoidal

Myoglobin - hyperbolic

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6
Q

Eukaryotic Translation: eEF-1

A

One of the factors that carries out elongation. It has an alpha and beta-gamma subunit. It mediates the entry/binding of the aminoacyl tRNA to the binding site [Like EF-Tu]

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7
Q

Eurkaryotic Translation Factor: eEF-2

A

Catalyzes the translocation of the tRNA and mRNA down the ribosome at the end of each round of polypeptide elongation [EF-G]

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8
Q

Xeroderma Pigmentosum

A
  • Genetically heterogeneous, autosomal recessive disease of defective DNA repair. Causes extra sensitivity to UV radiation.
  • Patients have shortened life span (less than 30 yrs) and are more susceptible to skin cancers along with brain, lung and GI cancers
  • Most XP mutation are found in the genes that code for NER (nucleotide excision repair) like exonucleases
  • Associated with families that inbreed - India caste system
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9
Q

NER (nucleotide excision repair) [DNA repair mech./mutation associated with Xeroderma Pigmentosa]

A
  • Usually mutations cause by dimers (pyrimidine or thiamine)
    1. After mutation is detected, then excision nuclease cuts out a chunk of DNA strand and DNA helicase helps unwind things
    2. Then DNA polymerase reads the correct base and adds the correct pair along with DNA ligase
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10
Q

Base Excision Repair

A

Cuts out single base and puts in correct one

  1. Deaminated C is detected
  2. Uracil is removed by Uracil DNA glycosylase
  3. AP Endonuclease and phosphodiesterase remove the sugar phosphate (backbone)
  4. DNA polymerase adds new nucleotides, DNA ligase seals the nick
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11
Q

[Strand-directed] Mismatch Repair

A
  • Happens after DNA synthesis mechanisms are all done
    1. There is an error in the strand that is detected and bound by mismatch proofreading proteins (MutS)
    2. Mut L is bound to MutS and works by scanning the DNA nearby for a nick.
    3. When the nick is found, MutL triggers the degradation of the nicked strand all of the way back through the mismatch.
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12
Q

What is the order of events in RNA polymerase mediated transcription in bacteria?

A
  1. Sigma factor binds to the polymerase complex
  2. The complex binds to the promoter
  3. DNA is unwound and transcription begins
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13
Q

What is the rho factor?

A

rho is a termination factor that binds late in the transcription process

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14
Q

Wobble Base Pairing

A

Allows some mismatches at the third position of the codon. tRNAs do not require accurate base-pairing at all three positions of the mRNA codon.

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15
Q

What are the redox cofactors?

A

NAD+, NADP+, FAD, FMN, Ascorbic Acid, Metals

16
Q

What are the activation transfer cofactors?

A

TPP (thiamine pyrophosphate), Lipoate, PLP, Biotin, Cobalamin, Coenzyme A (CoASH)

17
Q

Dietary source: Niacin (Vitamin B3) - meat, whole grains, fortified cereals
Pathologies associated with deficiency: Pellagra [dermatitis, diarrhea and demetia (glossitis: bright red, smooth tounge) -alcoholism & corn diets

A

NAD+!
Types of rxns: fuel oxidation, lactate dehydrogenase (lactate -> pyruvate), pyruvate dehydrogenase (pyruvate -> acetyl CoA)
-Can serve as an allosteric inhibitor of other enzymes and determine if a pathway is on or off

18
Q

DS: Niacin (VB3) -meat, whole grains, fortified cereals

PAw/D: Pellagra - dermatitis, diarrhea, demetia - glossitis

A

NADP+!
Types of rxns: biosynthetic & detoxification reactions (cytochrome p450 - fxn is to add O2 to chemicals and make them more easy to secrete)

19
Q

DS: Riboflavin (Vitamin B2) - Milk, eggs, organ meats, legumes & mushrooms
PAw/D: Cheilosis -sores on edge of mouth, Glossitis

A

FAD!
Types of Rxns: (redox) Creating and breaking double bonds/disulfide bonds [ex: Succinate dehydrogenase (complex II) transforms succinate to fumarate
–Bound to enzyme tightly and accepts electrons one at a time
–Deficiency occurs with malabsorption and malnutrition

20
Q

DS: Riboflavin (VB2) -Milk, eggs, organ meats, legumes & mushrooms
PAw/D: Cheilosis, glossitis

A

FMN!
Type of rxn: redox - creating and breaking double bonds & disulfide bonds
[Ex: FAD synthetase to make FAD]
–Accepts one electron at a time
–Deficiency can occur with malabsorption and malnutrition

21
Q

DS: Vitamin C - citrus fruits and vegetables

PAw/D: Causes scurvy- characterized by defects in connective tissue

A

Ascorbic Acid
Types of rxns: redox cofactor for hydroxylase enzymes - imp for collagen synthesis, neurotransmitter synthesis and oxygen sensing
Ex: prolyl and lysyl hydroxylase – allow cross-linking of collagen peptides to form collagen fibers
–Enhances HIF prolyl hydroxylase activity (HPH)

22
Q

Metals

A

Types of rxns: Electron conducting cofactors in oxidation reduction reactions - iron sulfur complexes help transfer electrons in NADH dehydrogenase (fuel metabolism)
Vitamin precursor: Iron (heme), copper, cobalt, manganese, molybdenum

23
Q

DS: Thiamin (VB1) - meat (pork), legumes, whole grains, fortified cereals (water soluble, heat liable)
PAw/D: Beriberi (headache, malaise, peripheral neuropathy & heart failure), Wernicke encephalopathy (confusion, mental status change), Karsokoff Psychosis

A

TPP (thiamine pyrophosphate)!
Types of reactions: Decarboxylation reactions
Example of enzyme: Carbanion of TPP attaches to pyruvate and CO2 is given off (DECARBOXYLATION) - produces ionized hydroxyethyl-TPP

24
Q

DS: No particular precursor, can be synthesized from glucose and other amino acids in diet [fatty acids, carbs and amino acids in diet]
PAw/D: Deficiency not described

A

Lipoate!!
Rxn type: transfers acyl groups
Enzyme example: lipoate forms covalent bond with lysine residue side chains [Ex: E2 subunit of pyruvate dehydrogenase]

25
Q

DS: Vitamin B6 - fortified cereals, meat, bananas, rice, etc.
PAw/D: Pyridoxal phosphate deficiency (adults - peripheral neuropathy) (children-seizures, diarrhea, anemia, EEG abnormalities)

A

PLP (pyridoxyl phosphate)!

Rxns: Cofactor for enzymes that metabolize amino acids e.g. transaminases - helps with transamination

26
Q

DS: Widespread in foods
PAw/D: deficiency is rare but ppl get it from eating raw eggs - symptoms are scaly dermatitis, thinning hair and alopecia [avidin in egg whites binds to biotin and makes it indigestible]

A

Biotin!!
Rxn type: Carboxylation
Cofactor for four carboxylases - acetyl CoA carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, methylcrotinyl CoA carboxylase

27
Q

Competitive Enzyme Inhibitors

A
  • Compete with the substrate binding site
  • Prevent substrate from binding
  • No change in Vmax
  • It increases Km
  • Binds at active site
  • Not permanent
28
Q

Non-competitive Enzyme Inhibitors

A
  • Inactivates the enzyme
  • Makes a covalent bond between inhibitor & active site - prevents substrate bindingn
  • Cannot be removed unless enzyme is destroyed
  • Permanent
  • Decreases Vmax and no change in Km
  • Binds to active site
29
Q

Allosteric Enzyme Inhibitors

A
  • Change Michaelis-Menton plot from hyperbolic to sigmoidal (remember AMP graph)
  • Both Km and Vmax may be changed
  • Binds to enzyme distant from the active site & prevents substrate binding (induces conformational change which alters the substrate binding site)
  • DOESN’T BIND ACTIVE SITE
  • Not permanent
  • Ex: Fructose 2,6 bisphosphate is an allosteric activator which does the reverse of inhibitors – increases the effect of a substrate
  • Can’t describe using M-M kinetics
30
Q

Myoglobin structure?

Alzheimers - what secondary structure is associated with it?

A

High alpha helix content

Beta pleated sheets

31
Q

2,3 BPG (bisphosphoglutarate) or a drop in pH. . .

A

. . .increases the amount of O2 delivered to the tissue

32
Q

Sickle Cell Anemia is cause by. . .

A

When a valine at position 6 in beta chain creates a stick patch that can be associated with a sticky receptor on another hemoglobin molecule. “Sickle-ing” [In normal hemoglobin, Glutamate exists at position 6!]

33
Q

Genetics of Sickle cell disease

A

HbSS - most severe sickle cell anemia
HbAA - normal
HbSA- sickle cell trait
HbS_ <– anything other than A will cause disease
HbS/beta+ - sickle beta plus thalassaemia
Hbs/beta0 - sickle beta zero thalassaemia