Carbohydrates and Lipids

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Questions and Answers

Why does the ketose family have half the number of stereoisomers compared to the aldose family for a given number of carbon atoms?

  • The ketone functional group in ketoses eliminates a chiral center present in aldoses. (correct)
  • Ketoses are only found in L-isomeric forms, reducing the variety.
  • Cyclization of ketoses is less favorable, limiting the diversity of cyclic forms.
  • Ketoses are less stable than aldoses, leading to fewer possible structures.

In a Fischer projection, horizontal lines represent bonds angled away from the viewer, while vertical lines represent bonds angled towards the viewer.

False (B)

During the cyclization of an aldose sugar like D-glucose, which carbon atom typically attacks the carbonyl carbon, and what new functional group is formed as a result?

The 5th carbon atom attacks the carbonyl carbon, forming a hydroxyl group.

The only triose sugar in the ketose family is ______.

<p>dihydroxyacetone</p> Signup and view all the answers

Match the following monosaccharides with their classification:

<p>D-Glucose = Aldohexose D-Fructose = Ketohexose Dihydroxyacetone = Ketotriose D-Ribose = Aldopentose</p> Signup and view all the answers

How does the length of a saturated fatty acid affect its melting point?

<p>Longer saturated fatty acids have higher melting points. (C)</p> Signup and view all the answers

Unsaturated fatty acids have a positive correlation between their length and melting point.

<p>False (B)</p> Signup and view all the answers

What is the primary function of triacylglycerols (TAGs) in the body?

<p>long-term energy storage</p> Signup and view all the answers

The process of splitting a triacylglycerol into three fatty acids and glycerol is called ______.

<p>lipolysis</p> Signup and view all the answers

During beta oxidation, what molecule is generated every two carbons that are cleaved from a fatty acid?

<p>Acetyl-CoA (D)</p> Signup and view all the answers

If an 18-carbon fatty acid undergoes beta oxidation, how many molecules of acetyl-CoA will be produced?

<p>9 (C)</p> Signup and view all the answers

Carbohydrates are better suited for long-term energy storage compared to triacylglycerols due to their higher energy density.

<p>False (B)</p> Signup and view all the answers

Match the energy storage molecule with its characteristic.

<p>Carbohydrates such as Glycogen = Short-term energy storage Triacylglycerols = High energy density Carbohydrates = Hydrophilic</p> Signup and view all the answers

Why do multiple branches in glycogen provide an advantage for animals?

<p>Branches create more non-reducing ends, enabling more enzymes to bind and break down glucose simultaneously. (C)</p> Signup and view all the answers

What role do the surrounding amino acids in the enzyme pocket play in an enzymatic reaction?

<p>They create the optimal environment for both the substrate and the transition state. (D)</p> Signup and view all the answers

Lipids are defined primarily by their chemical structure, particularly the presence of a glycerol backbone.

<p>False (B)</p> Signup and view all the answers

What is the primary difference between amylose and glycogen in terms of structure?

<p>Amylose has only 1,4-glycosidic linkages, creating a linear structure, while glycogen has both 1,4- and 1,6-glycosidic linkages, resulting in a branched structure.</p> Signup and view all the answers

In the enzymatic process represented as E + S ↔ ES → EP ↔ E + P, the conversion of ES to EP is always an irreversible reaction.

<p>False (B)</p> Signup and view all the answers

In the omega naming system for fatty acids, the position of the last double bond is determined by counting backwards from the ______ carbon.

<p>omega</p> Signup and view all the answers

In an enzymatic reaction, what is the significance of ensuring that the enzyme is regenerated at the end of the process?

<p>To be reused for further catalysis</p> Signup and view all the answers

Match the following characteristics with the appropriate polysaccharide:

<p>Amylose = Helical structure with 1,4-linkages, used for energy storage in plants. Glycogen = Branched structure with 1,4- and 1,6-linkages, used for energy storage in animals.</p> Signup and view all the answers

In the enzymatic reaction E + S ↔ ES → EP ↔ E + P, ES and EP represent reaction ________.

<p>intermediates</p> Signup and view all the answers

Which of the following is a key distinction between ether and ester linkages in lipids?

<p>Ether linkages are more resistant to breakdown compared to ester linkages. (B)</p> Signup and view all the answers

Match the energy states with their relative stability and impact on the enzymatic reaction:

<p>E + S = Less stable than ES; initial state of the reaction. ES = More stable than E + S; intermediate complex formation. E + P = Lowest energy state; drives the reaction forward.</p> Signup and view all the answers

Cis-bonded fatty acids are less common in biological systems than trans-bonded fatty acids.

<p>False (B)</p> Signup and view all the answers

A fatty acid is designated as 20:2n-6. What does this naming convention indicate about the fatty acid's structure?

<p>The fatty acid has 2 double bonds, 20 carbons and the last double bond is located 6 carbons from the methyl end. (A)</p> Signup and view all the answers

How do enzymes increase the rate of a reaction?

<p>By lowering the activation energy (A)</p> Signup and view all the answers

The ΔG of a reaction provides information about the kinetics of the reaction.

<p>False (B)</p> Signup and view all the answers

What is the significance of geometric and electronic complementarity in enzyme-substrate interactions?

<p>specificity</p> Signup and view all the answers

Enzymes use ________ to separate and concentrate bio-components in specific subcellular sections.

<p>compartmentalization</p> Signup and view all the answers

Match the following terms related to enzyme function with their correct description:

<p>Active Site = The region of an enzyme where the substrate binds and catalysis occurs. Regulatory Site = A secondary binding site on an enzyme that modulates activity. Allostery = The modulation of enzyme activity through binding at a site other than the active site. Transition State = A high-energy intermediate state during a chemical reaction that an enzyme stabilizes.</p> Signup and view all the answers

What is the primary function of the active site in an enzyme?

<p>To bind the substrate and catalyze the reaction (A)</p> Signup and view all the answers

Stabilizing the transition state too much can increase the efficiency of an enzyme.

<p>False (B)</p> Signup and view all the answers

Besides expression or substrate availability, what other mechanism provides a layer of control over enzyme activity?

<p>regulatory sites</p> Signup and view all the answers

Which of the following is NOT a general characteristic of enzyme binding sites?

<p>They occupy a large portion of the enzyme volume (B)</p> Signup and view all the answers

To react, molecules need to collide with high enough ________ and the correct orientation.

<p>energy</p> Signup and view all the answers

In a Lineweaver-Burk plot, what does the slope of the line represent?

<p>$K_m / V_{max}$ (A)</p> Signup and view all the answers

$V_{max}$ is a constant value published for every enzyme, as it is an intrinsic property of the enzyme itself, independent of experimental conditions.

<p>False (B)</p> Signup and view all the answers

Define the term 'turnover number' ($K_{cat}$) in enzyme kinetics.

<p>The turnover number is the maximal number of substrate molecules converted to product per second by a single active site.</p> Signup and view all the answers

The catalytic efficiency of an enzyme is defined as ______.

<p>$K_{cat} / K_m$</p> Signup and view all the answers

Which type of reversible enzyme inhibitor binds only to the enzyme-substrate (ES) complex?

<p>Uncompetitive inhibitor (B)</p> Signup and view all the answers

How does a competitive inhibitor affect $K_m$ and $V_{max}$?

<p>Increases $K_m$, no change in $V_{max}$ (C)</p> Signup and view all the answers

Noncompetitive inhibitors impact $K_m$, but do not impact $V_{max}$.

<p>False (B)</p> Signup and view all the answers

Match the type of reversible inhibitor with its effect on $K_m$ and $V_{max}$.

<p>Competitive = Increases $K_m$, no change in $V_{max}$ Uncompetitive = Decreases both $K_m$ and $V_{max}$ Noncompetitive = No change in $K_m$, decreases $V_{max}$ Mixed = Affects $K_m$ and $V_{max}$ differently depending on binding preference</p> Signup and view all the answers

Flashcards

Aldose

Has an aldehyde functional group on its backbone.

Ketose

Has a ketone functional group on its backbone.

Fischer Projection

Vertical lines are dashes (away), horizontal lines are wedges (towards).

Sugar Forms

Sugars can exist in both open-chain (linear) and ring (cyclic) forms and interconvert between the two.

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Cyclization of Aldoses

In the case of aldoses, the hydroxyl group on the 5th carbon attacks the carbonyl carbon (C1), forming a ring.

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Enzyme Pocket Geometry

Amino acids in the enzyme's active site create the ideal environment for substrate binding and transition state stabilization.

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Enzyme Catalysis

Enzymes lower the activation energy by stabilizing the transition state.

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Enzymatic Reaction Equation

E + S ↔ ES → EP ↔ E + P; describes substrate binding, then transition state, followed by release.

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Enzyme Regeneration

Enzymes are not consumed; they are regenerated to catalyze more reactions.

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Cofactor

A molecule that assists an enzyme, is regenerated, and without it the enzyme is non-functional.

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Amylose (Starch)

A polysaccharide of a-D-glucose used for energy storage in plants, featuring a helical structure with about 8 glucose residues per turn and standard 1,4 linkages.

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Glycogen

A polysaccharide of a-D-glucose used for energy storage in animals, with 1,4 linkages and 1,6 linkages creating branches every 8-10 residues for faster glucose release.

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Lipids

Organic compounds that are insoluble in water, used for energy storage, structural components (cell membranes), and signaling molecules.

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Ether Linkages

Chemical bonds which are generally harder to break compared to ester linkages.

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Fatty Acids

Carboxylic acids with aliphatic chains, which can be saturated (no double bonds) or unsaturated (one or more double bonds).

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Polyunsaturated Fatty Acid

Fatty acids containing more than one double bond in their backbone.

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Omega Naming (Fatty Acids)

A naming convention counting carbons from the omega (final) carbon to the first carbon in the double bond.

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Naming Fatty Acids

Requires the number of carbons, number of double bonds, and position of the last double bond counting from the omega carbon.

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Saturated Fatty Acids & Melting Point

Melting point increases with chain length.

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Unsaturated Fatty Acids & Melting Point

Melting point decreases with chain length.

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Triacylglycerols (TAGs)

Glycerol molecule esterified to three fatty acids.

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Function of TAGs

Long-term energy storage in adipocytes.

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Lipolysis

Breaking down TAGs into fatty acids and glycerol.

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Beta-oxidation

Oxidation of fatty acids to generate acetyl-CoA, NADH, and FADH2.

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Carbohydrate Energy Storage

Easily metabolized, hydrophilic, and lower energy density.

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Beta Oxidation: Last Step

Two acetyl-CoA molecules are produced.

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Enzyme Compartmentalization

Separation and concentration of bio-components in specific cell areas, increasing reaction efficiency.

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Catalysts

Substances that lower activation energy, speeding up reactions without being consumed.

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Activation Energy

The energy required for a reaction to occur. Catalysts lower this energy.

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Transition State

A high-energy, unstable state that reactants must pass through to become products.

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Enzyme Active Site

The specific region of an enzyme where the substrate binds and catalysis occurs.

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Geometric and Electronic Complementarity

The shape and charge compatibility between an enzyme's active site and its substrate.

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Enzyme Regulatory Site

A secondary binding site on an enzyme that modulates the enzyme's activity.

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Allostery

The alteration of an enzyme's activity through the binding of a molecule at a regulatory site.

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Enzyme Specificity

To selectively bind to a specific target molecule.

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Transition State Stabilization

Enzymes stabilize the transition state in a reaction, increasing its affinity and promoting its formation.

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Lineweaver-Burke Plot

Graphical representation of the Michaelis-Menten equation, producing a linear relationship which allows determination for Km and Vmax values.

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Turnover Number (Kcat)

The maximal number of substrate molecules converted to product per second by a single active site.

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Catalytic Efficiency

A measure of how efficiently an enzyme converts a substrate into product.

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Enzyme Inhibitor

Molecule that reduces enzymatic reaction rate by interfering with substrate binding or catalysis.

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Competitive Inhibitor

Inhibitor that competes with the substrate for the enzyme's active site.

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Uncompetitive Inhibitor

Inhibitor that binds only to the enzyme-substrate (ES) complex at a site distinct from the active site.

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Noncompetitive Inhibition

Inhibitor that binds equally well to both the enzyme (E) and the enzyme-substrate (ES) complex.

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Mixed Inhibition

Inhibitor binds to a site seperate from the active site, to either the enzyme (E) or enzyme-substrate (ES) complex.

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Study Notes

Lecture 11: Carbohydrates

  • Glucose metabolism is important for respiration and energy

Functions of Carbohydrates

  • Energy storage is a primary function
    • Achieved with large polymers
  • Protein targeting
    • Proteins recognize and associate with carbohydrates
    • Chains can recruit proteins to different locations
  • Cell identification and recognition
    • Carbohydrates act as physical structures on protein/cell/receptor surfaces
    • Influence physical interactions
  • Blood type determination
    • Unique carbohydrate sequences on cell surfaces determine blood type
    • Square/circle shapes represent carbohydrate monomers
    • Differing branches represent different cell surface carbohydrates, each unique to a blood type
    • Immune issues during blood mixing arise from immune cells recognizing carbohydrate chains as foreign, leading to binding interaction

Structure and Components

  • Cell walls and insect shells contain carbohydrates
  • Chains of carbs have structural uses
  • Act as components in other biomolecules
    • Antibiotics, enzyme cofactors, and nucleic acids
  • Serve as Lubrication in joints
  • Glucose is a monosaccharide
  • Sucrose is a disaccharide
  • Amylose is a polysaccharide/starch

Basic Knowledge

  • Monosaccharides, disaccharides, and polysaccharides exist
  • Monosaccharides have a basic cyclic ring structure
    • Glucose and fructose
  • Aldoses have a functional aldehyde group
  • Ketoses possess a functional ketone group
    • C3: triose
    • C4: tetraose
    • C5: Pentose
    • C6: Hexose

Basic Trioses

  • Trioses contain 3 carbon sugars
  • Glyceraldehyde has two stereoisomers
    • D and L
    • The Hydroxyl is in different place in space
      • Hydroxyl on right (D)
      • Hydroxyl on left (L)
  • Ketoses always have one less chiral center
    • Dihydroxyacetone has no D or L due to the absence of a chiral center, but is a ketose.
  • Vertical lines in the Fischer Projection represent dashes angled away
  • Horizontal lines indicate wedges angled towards viewer
  • Longer Fischer sugars can transition to cyclic molecules

Ketose Family

  • Biochem generally focuses on D sugars
  • Ketose family is stunted
  • Dihydroxyacetone is the only triose
  • Chirality dictates the unique structure names at the other two carbs

Aldose Family

  • There are 8 possible hexoses instead of 4 from the ketose versions

Cyclization

  • Sugars can be linear or cyclic and interconvertible
  • During cyclization
    • Aldoses: the carbonyl on D-glucose is the target
    • The 5th carbon attacks the 1st carbon
    • The carbonyl becomes a hydroxyl group and the oxygen from the 5th hydroxyl becomes part of the ring
    • The oxygen shows where the anomeric carbon is
  • The hydroxyl can point up or down becomes the C1 which becomes a chiral center or anomeric form
  • Alpha is on the opposite side of C6
    • CH2OH and OH are opposite
  • Beta is on the same side as C6
    • CH2OH and OH are on same side
  • For D-sugars, C6 is above the ring and always the same -Alpha is down (trans) -Beta is up (cis)
  • Cyclization is reversible
    • Anomers interchange with mutarotation (relinearize and recyclize)
    • Beta switches to Alpha
  • Mutarotation requires a hydroxyl and no other group on its anomeric carbon
  • In ketoses
    • A 5-membered ring is smaller where the same hydroxyl attacks an earlier carbon making C2 the anomeric carbon instead of C1
  • Pyranose form sugars
    • Have the basic sugar structure and there is an oxygen in a ring and the rest are carbons (6 membered)
  • Furan Form Sugars
    • Have the same criteria as above, but 5 membered
  • Most sugars will be in pyranose form but a small percentage of sugars will be in furanose form
  • Furanose Sugars are unstable
    • Stacked hydroxyls are unfavorable

Glycosidic Bond Formation

  • Monosaccharides are combined with a glycosidic bond between monomers
  • Glycosidic bonds are covalent
    • Occurs between hemiacetal group of one carbohydrate
    • A hydroxyl group (often C4) on another carbohydrate molecule
    • condensation or dehydration occurs (water molecule is popped out)
  • Notation indicates involved carbons and anomeric forms
  • The name indicates carbon origin, destination, and α/β arrangement
  • Example is 1-4 α-glycosidic bond

Disaccharides

  • Naming scheme
    • Even with beta or alpha both you indicate the numbers
  • Lactose and maltose
    • One monomer can relinearize and switch to alpha or beta if the reducing anomeric carbon has a hydroxyl open to change
  • Sucrose
    • Cannot linearize
    • It would require breaking the glycosidic bond before any mutarotation

Polysaccharides

  • Important for 2 different functions in biological systems through different glycosidic bonds
    • Energy storage
    • Protection and structure

Important Polysaccharides

Cellulose (structural polysaccharide)
  • Has with β-d-glucose that provides structure in plants
  • Glucose links in a β-1,4-linkage with an alternating structure
    • Every other glucose flips relative to the previous one
    • This occurs to maximize interactions and forms a linear chain
  • Chains stack due to their structure
  • Interchain happen between different chains
  • Intrachain interactions happen within the one chain
  • Combined interactions create lateral and vertical stabilization creating high tensile strength which makes for a very fibrous structure
Chitin (structural polysaccharide)
  • It utilizes β -D-glucose polysaccharides with modifications on each glucose residue before placement, (acetamide group added on C2)
  • Offers more opportunities for Hydrogen bonding because of N's
  • Chitin is stronger than cellulose, providing bulk strength
  • Beetles and hermit crabs make use of this structure
Energetic Polysaccharides
  • Forms of glycosidic bonds distinguish energetic from structural
    • B-1,4 in structural
    • A-1,4 in energetic
  • Lacks hydrogen-hydrogen interchain bonds
  • Results in helical structures without tensile strength
Starch (amylose)
  • Has α-D-glucose used for energy storage in plants
  • Helical structure has roughly 8 glucose residues per turn
  • Standard 1,4 linkage and no branches
  • Human enzymes break α linkages to use energy
Glycogen
  • Utilizes α -D-glucose for energy storage in animals
  • Main linkages occur in 1,4 linkages but after 8-10 residues a 1,6 linkage occurs
  • Multiple branches speed up breakdown and utilization, which benefits animals
    • Enzymes bind to non-reducing ends
    • Rate of glucose release is faster
    • Human enzymes more easily break alpha linkages

Lecture 12: Lipids

  • Lipids have organic compounds not soluble in water
    • Classifying characteristic based on solubility and not structure

Lipid Uses

  • For a variety of options based on structure
    • Energy storage: longer term compared to carbohydrates
    • Structural components: found in cell membrane
    • Signaling molecules: exist intracellulary and intercellulary
  • Storage lipids have neutral charge
  • phospholipids, sphingolipids are some of the membrane lipids

Ether vs Ester Linkages

  • Ether more difficult to break

Fatty Acids

  • Carboxylic acids
  • Aliphatic chains
    • Can be saturated or unsaturated according to bonds
    • Polyunsaturated contains more than one double bond
  • Cis-bonded more common than trans

Naming Fatty Acids

  • Use omega naming - Number carbons in fatty acid (from eg. 18 - Number of double bonds (eg. 3) - Position of the last bond (eg. 3) - Omega carbon is last carbon in the chain, count backwards from the omega carbon to find the first carbon in double bond. Example: 18:3n-3 3 Double bond 3 Omega carbon
Fully Saturated Fatty Acid
  • 18:0 is example

Melting Points

  • Saturated
    • Positively correlated
    • Longer length the higher the melting point
  • Unsaturated
    • Negatively correlated - Longer lengths lower melting point - Cis double bonds cause a bend and makes it harder to align with each other - Less stable intermolecular forces

Triacylglycerols (TAGs)

  • Body stores with fatty acid
  • Esters derived from glycerol and three fatty acids
  • Constitutes about 90 percent of dietary lipids
  • Storage - Major form of energy storage in humans - Carbs (glycogen) = short term - TAGS = long term
  • Simple have one fatty acid and mixed have multiple
  • Ester linkages links fatty acids to glycerol

TAG Catalysis

  • Two Phases
    • Lipolysis - Splits TAGS into fatty acids and a glycerol
    • Fatty acid break down in beta oxidation - Oxidizes to reduce NAD/FAD and Generate acetyl-CoA - Fatty acids cycle - Depending on length of chain (more energy with longer chains) Every two carbons an Acetyl-CoA is produced The last step splits into Acetyl-CoA 18 Carbon chain yields 9 Acetyl-CoA

Energy Storage

  • Carbohydrates
    • Short term and hard to store
    • Hydrophilic = significant increase in pressure but easier transport
  • Lipids
    • Long term that is easy to store
    • Hydrophobic lower in osmotic pressure and harder transport
  • Higher is better and lipids are better

Lipoproteins

  • Lipidproteins consist of composite structres with a monolayer (tails point in) with apolipoproteins

Eicosanoids

  • Hormones derived from acid
    • autocrine and paracrine
    • immune response
    • inhibit with COX - Aspirin is example - Irreversible inhabitation that stays bound

Sterols

    - subset to steroids
            - global hormones and nuclear receptors

Lecture 13: Membranes

  • Phospholipids bilayers
    • As long as there are enough then Self assemble
    • membrane permeability needs ion channels

Molecule Permeability

Small nonpolar molecules pass easily

Glycerophospholipids

- polar head structure ece
- inner fatty tail leaflet

Pip2 Signaling

    - phospholipids sitting laterally in inner leaflet, they are laterally diffusing (moving around)
    - can bump into Pi3K
            - signals and adds phosphate to pi

Sphingolipids

- Polar head outter leaflet end
 - Fatty acid Tail with scaffold and hydrophobic end

Phospholipid Diffusion

Transverse Diffusion lateral diffusion

Transverse and Lateral Diffusion

  • flips from outer leaflet
  • nonpolar enviornment
  • simply moves from the leaflet

Diffusion Assymetry

    - Cell membranes actively maintain distribution
- Cell membranes that are different in composition
  • electric enviornmnets for structure
  • if ps seen outside means targted for something

Maintaining Assymetry

Flippase: to inside Floppase: to outside Scarmble Indiscrimant to inside

Saturation and Temperature

Saturation: rigid Insaturation: fluid Regulation

ABOVE: heat saturated BELOW: Cold unsaturated

  • choleseterol moderates fludiity and creates bonding

  • lipid anchors exist on the surface of the cell membreane covalente

  • helps associate proteins to the membreane

Lecture 14: Enzymes

  • Oxidation of glucose with enzymes is highly exergonic
  • Catalysis for protein

Comparentailization

  • Bio comparents that have processing efficency increases metabolites and have correct enyzme

Catalyst

  • Catalyst lowers actovation enegry becoming products
  • activation energy is high when the reaction has to go pass through transitions

Enzyme Sites

  • Binding or catalytic +Substrate +geometric and binding

Regulatory

  • Binding molecules
  • change efficiencies
  • prodes a third ayer

Characteristics

Alloestery changes activity spaces that are small complentariy

Design Challenge

  • binds to target - bings w solution - soltion to stable target

The Enyzmatic Process

  • Sometimes has reaction but can also go back for uncatylzed and catlyzed
  • two indermediates where recycled which es > e+s is always driven which is why it works

Starts with Enymes

  • always has one end - regenerated in a process - peptid

Transition

  • stabilizes
  • binds to product

Polypeptide

  • Amino acids residues are chain Hole: Change from o has strong bond

Destaizling

  • decreases activation w two ways to do it
  • deastablzies

Steric Hindrandce

  • binds
  • hinders
  • analogs w inhibitors models

Stererospecific

Steric bond with shape

  • effect with systems

Reaction Specicity

limits to subsrtrrate all product types

Temperature Specifity

Temp = 37

  • starts and denatures, the protein structure will be the type
  • in low temp the lower effeicncy of the enzyme is in the lower amunt of sufficient molucukes from the energy
  • denaturation can a lter the active site too

PH

optimal ranges with the right acitvity at 5

Enzymes

  • oxidoreductases which move electron and reduces atom
    • lactate
  • Transferases where groups go from molecule
  • functional groups where transferse
  • hydrolases
    • single water usage pep tide = hydro

Lyases

  • bond forms through remval

  • lyase is used forms product from subtrtes bond formation

  • isomerases where structures rearrange

Enzymes have orientation

Acidity

with rna through catalysis

  • acid catalysis which donwates and stbalzie
  • basic catalsis which allows high funaction

can be used to form a teiad

Covalant catalysis

  • where active often forms bonds
  • by nulciophile
  • chanvges new

can be eleectric to chnage stabalziaiton.

metals

used cations for structre stabilization

RNaase

  • non specfici cuts uracil

Histindie

acts to stable. catalylsi the reaction while lys is the phosphate. the h makes the O bcome a much better catalysr

Proeteae

use of catalysts to attack.

base:

high strengths charges where acid is present.

chymotrpysin

recognitions used to cleave peptide

Catalytic

  • His stabaizlsed

  • ser attacks ser is there bond oxyianion is stabilzed and hydrogen bonding

  • Carbonyl bond formed

  • histindone makes group water active with stabilizeation with Hist hist with base hydorcide with act stabilizeed aminos is there ser stabilizon and carbyul

all dissociates and origan

Kintetics Of Enzymes"

lecture: michel

Key facts

  • enzymes used in reaction
  • products and how it work
  • prodices are true in the reacyion
  • reaction

Assemptions

  • fast and slow
  • prodcuts are 0

State : whats measured for easy

what equals out from it is from system find vmx which equation

  • how it affects and does it effect the product
  • it increases and affects product

Linewave

we use to linear with enzyme

  • turnovber rater, and to find product

Inhibition of Enymes

  • interfere with subsrte
  • reversubke by binding an ehzyme

What kind of Inhibition are you Non allusteric, Km up Alluesteroc Km doan Mixed Allusteric P. km

  • Competitive with KM up
  • Mixed is to Km

Noncompetitive Inhibition

mechanism as mixed inhibitors and can bind the same to all E or es. Km is the inhibitor disassociation

  • decreases the dissociation to km and the maximum is not affevtced Mixed: a site that e bmds it is for or es.

What binds to

  • COmp: e and s. uncompetition:
  • e+ and s
  • Non competiton bounds to both
  • Mixed can eiter

Cometpeivi vs non. All steric effects Km and vMxa with el, i and es i

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