2.1.4 - Enzymes (set A - Enzyme Action) Flashcards

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1
Q

Why are enzymes important?

A

Most of the processes necessary to life involve chemical reactions which need to happen very fast - they would demand very high temperatures and pressures which are not possible in living cells (would damage them)

  • catalysts provide an alternate reaction pathway
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2
Q

What are enzymes?

A

Globular proteins which act as biological catalysts for intra and extracellular reactions - interact with substrate molecules forming an enzyme-substrate complex which lowers activation energy for metabolic reactions

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3
Q

Explain the role of enzymes?

A

Enzymes catalyse anabolic (building up) reactions and catabolic (breaking down) reactions - overall important for growth (forming tissues ext) and releasing energy

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4
Q

Explain why temperature and pressure increases enzyme action?

A

Molecules in a solution move and collide randomly - they need to collide in the right origination to form an enzyme substrate complex, increasing temperature and pressure increases the likelihood of more successful collisions (therefore rate of reactions)

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5
Q

Outline the meaning of enzyme specificity?

A

Enzymes are specific to only one substrate and only that substrate fits into the enzyme active site and forms an enzyme-substrate complex

  • each enzyme only catalyses one biochemical reaction
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6
Q

Outline enzymes affect on activation energy?

A

Energy needs to be supplied to start most reactions - sometimes the activation energy is too large, so enzymes help the molecules collide more successfully, reducing energy required for reaction to start

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7
Q

Give the two hypotheses for how enzymes lower activation energy?

A
  • lock and key theory
  • induced-fit hypothesis
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8
Q

Outline the lock and key theory?

A

Tertiary structure on enzyme has complementary shape for a specific substrate (active site), only specific substrate fits into enzymes active site - forms an enzyme-substrate complex lowers activation energy, substrate react forming the products which are then released due to weak bonds

  • enzyme is unchanged and free to form another complex
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9
Q

Outline in depth the binding of the enzyme-substrate complex - with focus on the lock and key hypothesis?

A

Substrate held in way that the complementary atom-groups are close enough to react - R-groups of amino acid within enzymes active site also interact with the substrate

  • forms temporary bonds - which put strain on the bonds within the substrate, helps the reaction
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10
Q

Outline the induced-fit hypothesis?

A

Modified versions of lock and key

Idea AS changes slightly not completely complementary

initial interaction between the enzyme and substrate is relatively weak - however interactions rapidly induce changes in the enzyme’s tertiary structure that strengthen binding, putting strain on the substrate molecule

Weakens bonds in substrate, lowering the activation energy for reaction

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11
Q

explain how activation energy is lowered, explain with focus on the induced-fit?

A

Initial interaction between enzyme and substrate is relatively weak - weak interactions rapidly induce changes in enzymes tertiary structure - puts strain on the substrate molecule

  • weakens bonds in the substrate, lowering activation energy
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12
Q

Outline what intracellular enzymes are - give an example of an enzyme that catalyses intracellular reactions?

A

Enzymes which act within cells

  • catalase - catalyses decomposition of hydrogen peroxide into water and oxygen (found in plants and animals)
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13
Q

Outline what extracellular enzymes are - give an example of an enzyme that catalyses extracellular reactions?

A

Enzymes which work outside the cell that made them - released by the cell to break down large nutrient molecules into smaller molecules (process of digestion) which can enter cell
through the cell-surface membrane

  • eg amylase and trypsin (involved in human digestion)
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14
Q

Give 2 examples of enzyme that catalyse extracellular reaction, state location they function?

A
  • amylase - carbohydrate catalyses digestion of starch to maltose (in saliva and small intestine lumen)
  • trypsin - type of protease (breaks down protein) catalyses hydrolysis of peptide bonds (in small intestine lumen)
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15
Q

Outline the digestion of starch?

A

1) Starch polymers partially broken down into maltose (disaccharide) reaction catalysed by amylase (produce in salivary glands and pancreas)

2) maltose broken down into glucose (monosaccharide) - enzyme maltase present in small intestine catalyses the reaction

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16
Q

Give the names of both enzymes involved in the digestion of starch state where they are produced?

A
  • amylase -produced in the salivary gland and pancreas - released into saliva in the mouth and in pancreatic juice in small intestines
  • maltase - present in small intestines
17
Q

Outline the digestion of proteins?

A

Trypsin is a type of protease which catalyses the digestion of proteins into smaller peptides - can be further broken down into amino acids by other protease

  • amino acids than absorbed into cells lining the digestive system and then absorbed into the bloodstream
18
Q

Explain where trypsin is produced and where it acts?

A

Produced in pancreas - where its released with pancreatic juice into the small intestine to act on proteins