Chapter 1: Biological Molecules Flashcards
1.5 Enzymes
An enzyme is a ____ protein
Globular
1.5 Enzymes
What are the key characteristics of an enzyme?
- Globular proteins
- Water soluble
- Act as biological catalysts (speed up reactions without being used up themselves)
- Highly specific
- Have an ‘active site’
- Activitiy is usually affected by pH and temperature
1.5 Enzymes
What is the primary structure of an enzyme?
Their primary structure is the initial chain of AA’s.
1.5 Enzymes
What is secondary structure of an enzyme?
The secondary structure is the initial folding.
1.5 Enzymes
What is tertiary structure of an enzyme?
Tertiary structure is its functional shape with hydrophobic groups in the middle and hydrophilic groups surrounding them on the outside.
1.5 Enzymes
Draw a diagram for enzyme action
1.5 Enzymes
1.5 Enzymes
What is lock and theory model?
The enzymes specifically shaped active site will only allow one kind of substrate to fit in.
The substrate has to have a complimentary shape to the active site therefore can fit in.
1.5 Enzymes
What is the induced fit hypothesis?
Once in the active site the substrate is broken down, this process is aided by the ‘induced-fit hypothesis’. This suggests that the enzyme active site is malleable to fit the shape of the substrate. The enzyme will change shape slightly to hold the substrate in place, this change puts stress on the substrate further speeding up the process
1.5 Enzymes
Draw the enzyme action activation energy curve
1.5 Enzymes
Why does pH affect enzyme action?
A hydrogen (H+) ion carries a positive charge so is attracted to negative charges. And likewise repelled by positive charges.
Hydrogen and ionic bonds are responsible for maintaining the tertiary structure and repulsion or attraction may alter tertiary structure.
Some ‘R’ groups are slightly charged and therefore will be attracted/repelled by the presence of H+ ions.
1.5 Enzymes
The intial rate is always…
…the highest.Maximum number of active sites available when compared to number of substrates.
1.5 Enzymes
Draw the three types of enzyme Inhibtion
1.5 Enzymes
Describe competitive inhibition
**The inhibitor competes with the substrate for the active site of the enzyme. **
Inhibitor is structurally similar to the substrate, binding to the active site. When the inhibitor binds, substrate cant bind, decreasing RoR
The presence of a competitive inhibitor can be overcome by increasing the concentration of the substrate. As more substrate molecules are available, they are more likely to outcompete the inhibitor
1.5 Enzymes
Describe non competitive inhibition
**In non-competitive inhibition, the inhibitor binds to a different site on the enzyme, not the active site. This other site is called the allosteric site.
**
Inhibitor binds to the allosteric site, causing a conformational change in the enzyme. This change can either reduce the enzyme’s ability to bind to the substrate or lower the catalytic activity
- this MAY permenantly alter the enzymes shape making it inactive
Cant be overcome by increasing concentration of substrates