Biochemistry Final Exam

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98 Terms

1
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What amino acids are Nonpolar?

GIVPALM

  • Glycine, Isoleucine, Valine, Proline, Alanine, Leucine, Methionine

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What amino acids are Aromatic?

FYM

  • Phenylalanine, Tyrosine, Tryptophan

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What amino acids are Polar, Uncharged?

STCNQ

  • Serine, Threonine, Cysteine, Asparagine, Glutamine

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What amino acids are Negative?

ED

  • Glutamic Acid, Aspartic Acid

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What amino acids are Hydrophobic?

FLAVI

  • Phenylalanine, Leucine, Alanine, Valine, Isoleucine

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What amino acids are Hydrophilic?

REKHN

  • Arginine, Glutamic Acid, Lysine, Histidine, Asparagine

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What amino acids are Positive?

KRH

  • Lysine, Arginine, Histidine

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What nucleic acids are purines?

Adenine and Guanine

“as pure as gold” - 2 rings

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What nucleic acids are pyrimidines?

Cytosine, Uracil, Thymine

“cut” - 1 ring

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Difference between DNA and RNA

DNA (B Form) - deoxyribose

RNA (A Form) - ribose

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Peptide Bonds

C=ONH; strongest bond; cleaved by peptidase

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Secondary Structure

Alpha-helix, right handed. Beta-sheets are parallel and antiparallel (antiparallel is stronger since the hydrogen bonding is head on)

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Tertiary Stucture

Disulfide bonds stabilize cystine and forms a bond

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N terminus

Considered positive therefore negative amino acids are located here

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C terminus

Considered negative therefore positive amino acids are located here

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Glycine and Proline

Glycine is the only amino acid that is not chiral (has two Hydrogens)

Proline is the only amino acids that is an imino acid (not amino)

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Molten Globule

Hydrophobic effect stabilizes the initial intermediate. Hydrophobic collapse determines stability

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KD

Dissociation constant, inverse to KA (association constant)

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<p></p>

Lower the KD the tighter the binding

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Myoglobin

Binds to oxygen in low KD (stays bound) storage molecule

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Hemoglobin

High and low KD (in lung low = picks up oxygen); R and T state. Binds to 4 O2 molecules max

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Tense

HIS HC3 is protonated (pulls ion out of plate and O2 cannot bind). The ion binds to O2 and HIS HC3 (thermodynamically more stable)

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Relaxed

HIS HC3 is deprotonated (less stable thermodynamically). 2,3-bPG stabilizes T state (donut hole of hemoglobin)

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What is a nontoxic way to transport ammonia to the liver?

GLN (glutamine)

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Urea Cycle: Step 1

Ornithine + carbomyl phosphate → citrulline + Pi

  • Catalyzed by ornithine transcarbamolyase

  • Citrulline exported to cytosol

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Urea Cycle: Step 2

Citrulline + aspartate → arginosuccinate

  • Catalyzed by arginosuccinate synthetase. 2 more phosphate bonds cleaved (to adenylate to activate the citrulline). 1 more amino group enters

  • Activation of citrulline. AMP excellent leaving group as aspartate is added. Incorporates second amino acid

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Urea Cycle: Step 3 and 4

  • Arginase catalyzes hydrolysis of arginine

Arginine + H2O → ornithine + urea

  • Arginosuccinase catalyzes:

Arginosuccinate → fumarate + arginine

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Glycerophospholipids

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Will be asked how many times B-oxidation takes place

For example: 8C = 3 steps → 4 AcCoA

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Know the general names of the pathway (ex: thiolase, dehydrogenase, etc)

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What is the starting material for B-oxidation?

Malonyl CoA (not Acetyl CoA)

32
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What do hydratases work on?

Trans Delta 2 bonds

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Metabolic catabolism and anabolism

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What units are utilized in fatty acid synthesis?

Acetyl and Malonyl Coa

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What is the active group of the acyl carrier protein?

Thiol group (SH)

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Fatty Acid Synthesis

Step 1: Condensation

  1. KS catalyzes condensation of 2C and 3C units

  2. Acetate added to malonate

  3. Release of CO2 drives reaction forward (2C + 3C - 1C = 4C)

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Fatty Acid Synthesis

Step 2: Reduction

  1. Catalyzed by KR (ꞵ-ketoacyl-ACP reductase)

  2. Electron donor is NADPH

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Fatty Acid Synthesis

Step 3: Dehydration

  1. Catalyzed by DH (ꞵ-hydroxy acyl-ACP dehydratase)

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Fatty Acid Synthesis

Step 4: Second Reduction

  1. Catalyzes by ER (enoyl-ACP reductase)

  2. NADPH is the electron donor

  3. Product is an acyl group that is 2C long than the substrate primer linked to ACP

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Know the aspects of a Reaction Coordinate Diagram

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41
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What does ΔG‡ mean?

How fast a reaction will occur

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What does ΔG’o mean?

How likely a reaction will occur

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Do enzyme impact ΔG’o?

No

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Lower the Km

The higher the affinity for enzyme to substrate

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Graph and Equation for Enzyme Kinematics

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What state is enzyme kinematics always looked under?

Steady State (Rate of formation = Rate of breakdown)

47
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Solve for Vmax given data

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Competitive Inhibition

Binds to enzyme

Calculate for Vmax and Km

<p>Binds to enzyme</p><p>Calculate for Vmax and Km</p>
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Uncompetitive Inhibition

Binds to enzyme substrate complex

Identify values in graph (Km and Vmax are altered)

<p>Binds to enzyme substrate complex</p><p>Identify values in graph (Km and Vmax are altered)</p>
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Mixed Inhibition

Km and Vmax are altered

<p>Km and Vmax are altered</p>
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HIV Protease

Water directly attacks the peptide bond and releases the peptide

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Enolase

Utilizes Mg2+ ions to stabilize the transition state

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What is Keq?

[Products] / [Reactants]

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Know the equation

ΔG = -RTln (K’eq)

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How are unfavorable reactions able to proceed?

Via product removal, coupling, or tagging with a good leaving group

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<p></p>

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What is the movement of electrons?

From lower affinity to higher affinity

58
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Know what an oxidizing and reducing agent is?

OIL RIG

59
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Know what an aldose and ketose is

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60
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What is the difference between a D and L isomer?

D (OH is on the right) and L (OH is on the left)

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What form of amino acids do we use?

L amino acids

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What form of sugars do we use?

D sugars

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What is the difference between 𝛂 and 𝛃 anomers?

𝛂 (below the plane) 𝛃 (above the plane)

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What are the two phases of glycolysis?

Prep Phase - making intermediates to drive reaction

Payoff Phase - regenerate NADH)

6C sugar to 2 3C sugars

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What are the 3 bypass steps?

1, 3 (point of no return), 10

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Glucokinase

(Hexokinase IV) has a very low affinity for glucose (found in liver) which is where we store our glucose

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What are the energy yielding steps of Glycolysis?

6, 7, and 10

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What are the PDH cofactors?

E1 (TPP), E2 (lipoamide), E3 (FAD)

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What is the result of the PDH complex?

Removal of CO2 (decarboxylation) and formation of Acetyl-CoA

70
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What is the result of the Citric Acid Cycle?

1 turn = 1 GTP, 3 NADH, 1 FADH2, and 2 CO2

(amphibolic cycle - intermediates can come and leave at various points)

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What does high levels of Acetyl CoA do?

It will turn off the PDH complex but activate pyruvate carboxylase (reciprocally regulated)

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Malate-Aspartate Shuttle

NADH → NADH2

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Glycerol-3-Phosphate Shuttle

NADH → FADH2

Brings electrons to electron transport chain

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Electron Transport Chain

Movement of e- from complex I to ubiquinol is a favorable reaction. Ubiquinol donates e- to complex III (half cycle due to cytochrome) e- get dropped off to Complex IV

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Electron Transport Chain Complex II

Electron donor is succinate, converted to fumarate

FADH pushes 6 protons (1.5 ATP)

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Electron Transport Chain Complex IV

Loose (ADP bound), Tight (ATP bound), Open (nothing)

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Glycogenesis

Making of glycogen molecules (highly fed state)

Glucose-6-phosphate → glucose-1-phosphate (via phosphoglucomutase)

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What is the starting product for Glycogenesis?

UDP glucose (allows for the synthesis of glycogen)

79
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What does glycogen synthase catalyze the formation of?

𝛂 1→4 linkages (branching enzymes make 1→6 linkages)

80
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How do we get amino acids?

From dietary amino acids, or non-dietary protein breakdown

81
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What occurs in the Liver?

Glutamate acting as a nitrogen sink (transamination reaction) donate amino group to alpha-keto acid to mane an amino acid (glutamate in the liver is the carrier of the amino group)

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Transdeamination

Removing of amino group in the cytosol (done by enzyme glutamate dehydrogenase)

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What occurs in the extrahepatic tissue?

carry 2 molecules of ammonia

L-glutamate → L-glutamine

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What occurs in the muscle?

It can take an alternative pathway (glucose-alanine cycle). Amino acids are broken down and put onto glutamate. Donate NH4 and get converted to alanine

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Urea Cycle

Think about what is the input (glutamate or glutamine), how much ATP is being input (1 ATP in step 1) (put in 3 ATP) (get 2.5 molecules ATP out)

<p>Think about what is the input (glutamate or glutamine), how much ATP is being input (1 ATP in step 1) (put in 3 ATP) (get 2.5 molecules ATP out)</p>
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Glycerophospholipids

Glycerol + 2 fatty acids + alcohol + PO4

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Sphingolipids

Sphingosine + fatty acid + PO4 + Choline

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Sterols

Rings (function as hormones in our body)

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What are the signaling molecules in our body?

PIP2 (Phosphoenol phosphate)

They are usually going to be something with a phosphate attached to it

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Membrane Fluidity

Saturated fatty acid (melting point is high)

Unsaturated fatty acid (low melting point)

Trans fatty acid (extremely low)

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What are occurring at the same time?

B-oxidation and gluconeogenesis

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Fate of Glycerol

1 net molecule of ATP

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Carnitine

Transport of fatty acids from cytosol to mitochondria

Acyl carnitine is what is being transferred across the membrane

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4 steps of B-oxidation

Oxidation, hydration, oxidation, cleavage

1st step the e- acceptor is FAH, 2nd step the e- acceptor is NAD

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Breakdown of a 16C molecule

Acyl-CoA → Acetyl-CoA and C14 molecule

We then run 7 cycle of B-oxidation

16C molecule yield 106 molecules of ATP

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Monounsaturated Fatty Acid

Cis-delta-3 → Trans-delta-2 (via an isomerase)

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Polyunsaturated Fatty Acid

1st enzyme is reductase and 2nd is an isomerase allowing B-oxidation to proceed

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How can CoA pools be regenerated?

The formation of ketone bodies