Protein-Enzyme Flashcards
What are Enzymes?
Are biological catalysts - they speed up the rate of chemical reactions without being used up →lower the activation energy required
What is the active site?
-A specific shape to fit a specific substrate - they are complementary
Why do enzymes have complementary shape?
Is determined by the tertiary structure of protein that makes up the enzyme
What is an enzyme-substrate complex?
- forms when an enzyme and its substrate join together
-The enzyme-substrate complex is only formed temporarily, before the enzyme catalyses the reaction and the product(s) are released
What is a Catabolic reactions?
Involve the breakdown of complex molecules into simpler products
What is a Anabolic reactions?
Involve the building of complex molecules from simpler ones
How do enzymes lower the activation energy?
Enzymes speed up this process by making bond-breaking & bond-forming occur more readily → lowers the activation energy
What is the The lock-and-key hypothesis?
Based on the idea that the shape of enzymes are highly specific & fixed structures
The induced-fit hypothesis
The enzyme and its active site (and sometimes the substrate) can change shape slightly as the substrate molecule enters the enzyme - these are called conformational changes
Limiting Factors Affecting Enzymes: Temperature
Bonds (e.g., hydrogen bonds) holding the enzyme molecules together start to break
Tertiary structure of the protein (enzyme) changes
Active site becomes damaged → substrate cannot bind → enzyme becomes denatured
Limiting Factors Affecting Enzymes: pH
Too acidic solutions (H+ ions) or alkaline solutions (OH- ions) can cause hydrogen & ionic bonds to break
Shape of the active site changes → enzyme-substrate complexes form less easily - enzyme denatures
Limiting Factors Affecting Enzymes: Enzyme concentration
Higher the enzyme conc. → greater number of active sites available → greater likelihood of enzyme-substrate complex formation
This relationship is linear until the amount of substrate becomes limited …
… any further increase in enzyme concentration will not increase the rate of reaction - substrate becomes the limiting factor
Limiting Factors Affecting Enzymes: Substrate concentration
Greater the substrate concentration → greater likelihood of enzyme-substrate complex formation → higher the rate of reaction
When all active sites are saturated (full), no more enzyme-substrate complexes can form → rate of reaction plateaus
Competitive inhibitors
Have a similar shape to substrate molecules → compete with the substrate for the active site
Non-competitive inhibitors
Bind to the enzyme at an alternative site → alters the shape of the active site → prevents the substrate from binding to it