ENZYMES

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Author:
Anonymous
ID:
305201
Filename:
ENZYMES
Updated:
2015-07-14 16:58:59
Tags:
enzymes biochemistry
Folders:
Biochemistry
Description:
Chapter 3: Enzymes
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  1. specialized protein with catalytic properties
    enzymes
  2. exception of proteins with catalytic properties
    ribozymes
  3. RNA's with catalytic activity (transcription)
    ribozymes
  4. properties of enzymes
    • efficient/ effective
    • very specific/ very selective in action
    • location
  5. Types of specificity
    • stereochemical
    • broad
    • absolute
    • linkage
  6. E act only on one particular isomer
    stereochemical specificity
  7. E acts on a group of structurally related compounds
    Broad
  8. acts on only one substrate
    absolute specificity
  9. act only on one king of bind or linkage
    linkage specificity
  10. peptidase -----> 1
    carbohydrase -----> 2
    esterase -----> 3
    phosphatase -----> 4
    • 1 peptide bond
    • 2 glycosidic bond
    • 3 ester bond
    • 4 phosphate ester bond
  11. activities of this enzyme can be controlled or modulated by allosteric effectors
    allosteric enzymes
  12. reason why enzymes are used as a clinical markers for certain disease
    bec. they are found in specific sites/ organelles within the cell
  13. decrease the rate of reaction
    lowering the ACTIVATION ENERGY
  14. initial input of energy
    activation energy
  15. gives alternate route, one with lower energy of activation
    catalyst
  16. place where substrate binds to enzyme
    enzyme active site
  17. formed due to folding and bending of the protein
    enzyme active site
  18. usually a "crevice like" location in the enzyme
    enzyme active site
  19. two groups of Active Site
    catalytic and binding sites
  20. where enzyme attaches
    cleft or pocket
  21. additional non protein molecule needed by some enzymes to help reaction
    cofactor
  22. tightly boung cofactor
    prosthetic group
  23. organic co factors that are bound and released easily are called ________
    coenzyme
  24. types of cofactor
    • coenzyme
    • metal ion
  25. protein part of an enzyme that is inactive. requires cofactor to be activated
    apoenzyme
  26. the complete catalytically active enzyme
    holoenzyme
  27. enzyme requiring metal ion as cofactor
    metalloenzyme
  28. transport substrates from port of generation to port of utilization
    coenzyme
  29. most common metal ion
    Co Cu Mg Mn Zn
  30. example of prosthetic group
    PP FAD TPP Biotin
  31. thiamin pryophosphate
    Thimamine/ B1
  32. FAD, FMN
    Riboflavin/ B2
  33. NAD+ and NADP+
    Nicotinic acid/ niacin/ B3
  34. PLP
    Pyridoxine/ B6
  35. coenzyme A
    Pantothenic acid/ B5
  36. Biotin
    Biocytin
  37. THF, tetrahydrofolate
    Folic acid
  38. deoxyadenoxyl cobalamine
    B12
  39. lipoate
    Lipoic acid
  40. substrate of an enzyme
    reactant
  41. 2 theories about active site
    • Lock & key hypothesis
    • Induced Fit theory
  42. fit betweeen the substrate and the active site of enzyme is exact
    Lock & key hypothesis
  43. specificity of Lock & key hypothesis
    absolute specificity
  44. specificity explained by induced fit hypothesis
    broad specificity
  45. some proteins can change their shape
    induced fit hypothesis
  46. example of oxidoreductse
    dehydrogenase, oxidase
  47. example of transferase
    kinase, amino transferase/trans aminase
  48. example of hydrolase
    esterase, glycosidase, peptidase, phosphatase, phospholopase
  49. example of lysase
    decarboxylase, synthase
  50. example of ligase
    synthatase, carboxylase
  51. example of isomerase
    epimerase, mutase

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