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Flashcards

Enzymes

Ellie august Biology Inglês 15 flashcards

Flashcards do conjunto (15)

  1. 1Enzymesenzymes lower the activation energy of a reaction
  2. 2Enzymes- in anabolic reactions enzymes bring the substrate molecules together
    - in catabolic reactions the enzyme active site affects the bonds in substrates so they are easier to break
    e.g. transferase, ligase and hydrolase
  3. 3Specificity- absolute specificity: the enzyme will catalyse only one reaction
    - group specificity: the enzyme will act only on molecules that have a particular functional group e.g. amino acids
    - linkage specificity: the enzyme will act on a particular chemical bond
    - stereochemical specificity: the enzyme will act on a specific steric isomer
  4. 4Lock and Keyassumes the active site of an enzyme is rigid in its shape
  5. 5The Induced Fitthe active site is flexible + only assumes it catalytic conformation after the substrate molecules bind to the site
    when the product leaves the enzyme, the active site returns to its inactive state
  6. 6Globular proteins- active site has a specific shape due to tertiary shape of the protein
    - a change in shape of the protein effects the shape of the active site and the function of the enzyme
  7. 7Characteristics of Enzymesrate of enzyme action is dependent on the number of substrate molecules present
  8. 8Denaturation- changes in the shape of the enzyme
    - temperature
    - pH
    - radiation
    - salt
  9. 9Shape- enzymes must be folded into the right 3D shape to function
    - enzymes are suited to function best with a certain temperature, pH ect
    - denaturation is a process in which proteins lose their quarternary, tertiary and secondary structure
    - this is caused by application of external stress
    - if proteins are denatured cell activity is disrupted
  10. 10Enzyme regulation- enzymes can be regulated to promote or reduce activity
    - sometimes an inhibitor molecule is similar enough to a substrate that it can bind to the active site and act as a block
    - other times the inhibitor binds to the allosteric site
    - some inhibitors can change the shape of the enzyme so the substrate is less likely to bind.
  11. 11Competitive Inhibitors- work by preventing the formation of enzyme-substrate complexes as they have a similar shape to the substrate
    - they fit in the active site but remain unreacted . this causes the reaction rate to decrease
    - usually temporary
  12. 12Non-competitive Inhibitors- bind to the allosteric site causing the structure to distort
    - not affected by substrate concentration
    - many are irreversible and permanent
    - non-permanent ones are responsible for controlling metabolic functions
  13. 13Regulation- many enzymes do not work optimally unless bound to a non-specific helper molecule
    - temporary bond: ionic or hydrogen bonds
    - permanent bond: covalent bond
  14. 14Cofactorinorganic ions
  15. 15Coenymesorganic helper molecules (basic atomic structure)

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Biology FlashCards sobre Enzymes, criado por Ellie august em 25-10-2025.
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Ellie august
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