BCHM 307 Exam I

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Author:
MRK
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235383
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BCHM 307 Exam I
Updated:
2013-09-29 15:51:38
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Enzymes Carbohydrates
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Enzyme Kinetics
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  1. Michaelis-Menten equation
    • gives initial rate velocity at any concentration of substrate
  2. K1 - K3 defined
  3. Km
    • Michaelis Constant
    • Km = 1/2 Vmax
  4. Standard Hypobolic Graph of V
    axis labels
    Km
    Vmax
  5. Allosteric V plot
    • Sigmoidal
    • the more are attached the easier to attach more
  6. Double Reciprocal Plot/ Lineweaver-Burk Plot
    • y = 1/V
    • x = 1/[S]
    • m = Km/Vmax
  7. Types of Inhibitors
    • Reversable
    • - comperitive
    • - non-competitive
    • - un-competitive
    • Irreversible
    • - Suicide
  8. Competitive Inhibiton
    KM & Vmax
    • KM =increase b/c decreases affinity¬†
    • Vmax = stays the same because [S] eventually going to increase if [I] stays the same
  9. Non-Competitive Inhibition
    KM & Vmax
    • Binds to a site other than the active site
    • Km = stays the same b/c substrate can still bind
    • Vmax = decrease can't make product (can't be overcome by [S] increase
  10. Un-competitive Inhibition
    • bind to a site other than the active site but only when the substrate is bound
    • Km = decreases because there is more affinity to the substrate
    • Vmax = decreases b/c substrate can't out compete the inhibitor
    • Can't be over come with increased [S]
  11. Irreversible Inhibition
    • Enzyme is covalently modified from inhibitor
    • Enzyme is no longer a catalyst
    • Insecticide and nerve gas
    • Organoflurorophospates & acetylcholinesterase
  12. Nerve gases
    • irreversible inhibitors
    • stops nerve trigger from being deactivated = prolonged firing
    • Atropine is an antidote- it is a competitive inhibitor of acetylcholine
  13. Enzyme Mechanisms
    • R-groups are used in catalysis
    • Asp, Glu- Acid
    • His, Lys- Base
    • Ser, Cys, Tyr- alcohol
    • Catalysis coocurs when substrate is immobilized around active site
  14. Why is a specific aa targeted for derivatization?
    • Adjacent aa's make it more reactive
    • eg. cataylitic triads
  15. When R-group can't preform the Rxn
    Use co enzymes and prosthetic groups
  16. Coenzyme
    • metals or small organic molecules
    • not covalently bound to protien
    • often function as co-substrates
    • precursors are often vitamins
  17. Prosthetic groups
    • small organic molecules
    • covalently linked protien
  18. Classes of Carbohydrates
    • Monosaccharides
    • Disaccharides
    • Trisaccharides
    • Oligosaccharides
    • Polysacchardies
  19. Monosaccharide Nomenclature
    • Aldoses or Ketoses
    • tri, tetro, pento, hexo, (number of C)

    = aldohexose
    • aldose
    • because O= on end
    • Ketose
    • because O= in middle
  20. Fischer Projections
    • Most oxidized carbon at top
    • vertical extend behind
    • horizontal extend in front
    • carbons are numbered from the top
  21. Name D or L
    • on penultimate carbon- second to last
    • if OH to right = D
    • if OH to left = L
  22. Diastereomers
    stereoisomers that are not mirror images
  23. D-Glucose Fischer Projection
  24. hemiacetals
    Hemiketals
    • Form and breakdown randomly
    • C-5 hydroxyl interacts with C-1 of aldohexose
    • C-5 hydroxyl interacts with C-2 of Ketohexose
    • Into a ring- 90% of the time in solution
  25. Haworth Projections
    • Furanose (5 member rings)- rarer
    • Pyranose (6 member rings)
    • alpha if hydroxyl below
    • beta if hydroxyl above
  26. Draw alpha-D-Glucophyranose ß-D-Glucophranose
  27. Disaccharide bond
    • a glycosidic bond formed between monosaccharides
    • involves anomeric carbon
    • what is lost
    • in either alpha or beta configuration
  28. Disaccharides bond nomenclature
    alpha (1->4)
    • alpha= configuration of anomeric carbon
    • 1 = number of anomeric carbon
    • ->4 = denotes other carbon involved in glycosidic bond
  29. glucose-ß(1->4)-glucose
  30. Polysaccharides
    • Starch (amylose)
    • Glycogen and amylopectin
    • Cellulose
  31. Starch (amylose)
    • alpha(1->4) linked polymer of glucose
    • forms helical structure
    • amylase- hydrolyzes the bond to degrade it
  32. Glycogen and amylopectin
    • like Starch alpha (1->4) glucose polymers
    • but have alpha (1->6) branches
    • for storage
    • Easier to break down
    • in liver
  33. Cellulose
    • beta(1->4) linked polymer of glucose
    • forms planer, crystalline structure with H-Bonds
  34. Lipids
    • Hydrophobic/amphiphilic
    • insoluble in water
    • soluble in organic solvents
    • soluble in lipids
  35. Saponifiable Lipids
    • from soap making
    • have ester bond the releases a fatty acid chain
    • Polar head group
    • Triacylclycerols
    • phosphoacylglycerols
    • sphingolipids
    • glycolipids
  36. Fatty Acids
    • long chain carboxylic acids
    • 12-20 carbons (even #)
    • No H-bonding functional groups= hydrophobic
    • often have double bonds
    • saturated = no double bonds
    • Unsaturated = a double bond
    • polyunsaturated = more than one double
  37. fatty acid melting Point
    • Longer the chain more solid
    • less double bonds more solid
  38. Triacylglycerols
    • storage form of fatty acids
    • ester linked fatty acids
    • fats and oils
    • non-polar
    • rich energy
    • highly reduced C
    • not hydrated = denser
  39. Triacylglycerols
  40. Hydrogenation of Oils
    • used to produce solid triacylglycerols
    • reduces Cis-double bonds
    • sometimes makes trans- bonds (not as good)
  41. Glycerophosphoplipid
  42. Phosphoacylglycerols
    • membrane lipids
    • Phosphatidic acid core
    • Has a hydrophilic head group w/ P
    • therefore amphiphilic
  43. Sphingosine basic structure
  44. Sphigosine charateristics
    • membrane lipids
    • long chain amino alcohol core
    • amphiplilic
    • Has its own hyrdocarbon chain
    • Amide is hydrophilic
  45. Non-saponifiable Lipids
    • no ester linkage
    • sterols
    • cholesterol
    • hormones
  46. Cholesterol
    • very hydrophobic
    • OH is a hydrophilic group
    • planner in nature and makes membrane less rigid.
  47. Membrane Function
    • Separate cytoplasm from enviroment
    • provide system for uptake of compounds
    • mediate interactions with enviroment
    • provide environment for catalysis
  48. Membranes
    • Fluid mosaic- flow and change shape
    • around chloroplasts and mitochondria
    • lipid bilayer
  49. Fluidity Lipid Bilayer
    • Saturated are rigid
    • unsaturated are more fluid
  50. Integral: Membrane Protiens
    • hydrophobic aa interact with middle
    • held in place better
    • need detergent (SDS) to remove
    • topologies- anchored via membrane-spanning alpha helix
  51. Peripheral Membrane Protiens
    • attached with H-bonding on head group or integral protiens
    • not in membrane
    • removed with mild agent (salt)

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