Enzymes Flashcards
(32 cards)
Activation Energy
The minimum amount of energy needed for a reaction to happen
Active Site
A specific region on an enzyme where the substrate binds and the reaction takes place
Amylase
An enzyme that catalyses the extracellular breakdown of starch
catalase
An enzyme that catalyses the intracellular breakdown of hydrogen peroxide into oxygen and water
Coenzyme
A type of cofactor that is bound loosely o an enzyme with weak interactions
Cofactors
A non-protein molecule that is needed for the effective functioning of an enzyme
Competitive Inhibitor
A molecule which binds to the active site of an enzyme and prevents the substrate from binding
End Product inhibition
A method of enzyme inhibition where the product f an enzyme controlled reaction can bind to the enzyme and prevent it from workin
Enzyme
A biological catalyst used to speed up the rate of biochemical reactions without being used up or permanently altered
Enzyme-Product Complex
The temporary complex formed after the enzyme has catalysed the reaction but before the products have left the active site of the enzyme
Enzyme Substrate Complex
The temporary complex formed when th substrate binds to the active site of the enzyme
Extracellular reaction
A reaction that occurs outside of cells
Inactive Precursor
An inactive form of an enzyme that cannot carry out its function until it is activated
Induced fit hypothesis
A model of enzyme action that describes how once a specific substrate binds to the active site; the enzyme undergoes subtle conformational changes to fit the substrate better
Intracellular Reaction
A reaction that occurs inside the cells
Lock and Key hypothesis
A model of enzyme action that describes how the enzyme will only fit a substrate that has the correct complimentary shape to the active site
Metabolism
The sum of all the chemical reactions taking place in a cell
Non-Competitive Inhibitor
An inhibitor which binds to a different part of an enzyme known as the allosteric site and prevents the enzyme from functioning
Prosthetic group
A type of cofactor that is bound tightly to an enzyme with strong interactions
Substrate Specificity
The ability of an enzyme to catalyse only a specific reaction or set of reactions which have substrates complementary to the active site of the enzyme
Trypsin
An enzyme that catalyses the extracellular breakdown of proteins
Enzymes Notes
- Biological catalysts
- Globular proteins
- have a specific tertiary structure
- Catalyses metabolic reactions
- Lowers the activation energy of reaction
Effect of Temperature on Enzymes
As the temperature increases the kinetic energy does to. This means the substrate and the enzymes move around faster. The substrate and active site collide more often so Enzyme Substrate Complexes form which increases the rate of reaction.
Heat makes the molecules vibrate so the the weaker and ionic bonds break. The tertiary structure of the enzyme and active site changes shape so the substrate no longer first then the enzyme denatures
Effect of PH on Enzymes
Enzymes have an optimum PH,where the rate of reaction is highest. The hydrogen and ionic bonds that hold the tertiary structure in place get broken. This alters the tertiary structure which denatures the enzyme since the substrate no longer fits the site and the enzyme substrate complex cannot form