BIOCHEM TEST 4

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Anonymous
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152194
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BIOCHEM TEST 4
Updated:
2012-05-04 17:41:07
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Biochemistry
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PLEASE DO NOT FAIL THIS TEST EVAN!!! YOU CAN DO THIS!!!
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  1. What is a zymogen?
    An inactive enzyme precursor.
  2. Name the irreversible enzyme that we learned about in class, and name the zymogen that regulates it.
    • Trypsin
    • Trypsinogen.
  3. Name the enzyme that activates Trypsin
    Enteropeptidase
  4. What condition occurs when enzymes are activated prematurely?
    Pancreatitis
  5. What do Kinases do?
    Enzymes that phosphorylate various substrates.
  6. What do phosphatases do?
    Remove phospate from substrate
  7. Name one enzyme that is only active via lose of phosphate.
    Pyruvate DH
  8. Which AA can have Phosphates attached to them?
    Serine, Threonine, Tyrosine.
  9. What is "The Proximity Effect"?
    Substrates kept close to eachother have higher rates than substrates not kept in proximity. Help explain how enzymes work.
  10. What state are enzymes complementary to?
    Transition
  11. What is Koshland's induced fit model?
    Enzymes change shape once bound to substrate.
  12. What are Aspartate & Glutamates functions in catalytic reactions?
    Proton Transfer & Cation Binding.
  13. What are Cysteine and Serines funcitons in catalytic reactions?
    Covalent binding of Acyl groups.
  14. What is histidines role in catalytic binding?
    Proton transfer
  15. What is tyrosines role in catalytic reactions?
    Hydrogen bonding to ligands
  16. What are lysines and aginines roles in catalytic reactions?
    • Lysine (Proton Transfer & Anion Binding)
    • Arginine (Anion Binding)
  17. What is a bronsted acid?
    Proton Donor (Loses H)
  18. What is a Bronsted Base?
    Proton Acceptor (gains H)
  19. What is covalent catalysis?
    • Enzyme is covalently attached to substrate.
    • Enzyme transfers substrate to second substrate.
  20. What are the best competitive inhibitors of enzymatic reactions?
    Transition State Analogs
  21. Which AA's in triosephosphate isomerase are primarly used?
    Histidine and Glutamate.
  22. What are the two types of Coenzymes?
    Cosubstrates & Prostethic Groups
  23. Two types of essential ions
    Metal Ions. Activator Ions.
  24. How do cosubstrates work?
    Bind to active site, diffuse away, and are then regenerated by a second enzyme.
  25. Name some common cosubstrates
    NAD, NADP, ATP, Coenzyme A
  26. What is the role of metal ions in enzymes?
    Lewis Acid
  27. What are vitamins?
    Organic Micronutrients
  28. What are the functions of vitamins?
    Hormones, antioxidents, Cell signalling, precursors of coenzymes/cofactors.
  29. Which enzymes are derivized from Niacin?
    • NAD & NADP
    • Nicitanimide Adenine Dinucleotide (Phosphate)
  30. What are the roles of NAD & NADH?
    Oxidation & Reduction reactions involving two electron transfers.
  31. What enzyme gives us FMN and FAD?
    Riboflavin
  32. What are FMN and FAD?
    Flavin mononucleotide and flavin adenine dinucleotide.
  33. What enzymes are derivitized from Riboflavin?
    Flavin mononucleotide and flavine adenine dinucleotide.
  34. What is Pantothenate?
    Vitamin used to derivitize CoA (Coenzyme A)
  35. What is CoA
    Coenzyme A
  36. What vitamin is used to produce CoA?
    Pantothenate

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