Enzymes Flashcards
Give function and examples of oxidoreductases.
- Move electrons
- NADH, NADPH, FADH2, FMNH
Give function and examples of Transferases.
- Move a functional group
- ATP, SAM, Pyridoxal phosphate, 5’-deoxy…, tetrahydrofolate
Give function hydrolases.
- Break chemical bonds via hydrolysis
Give function of isomerase.
Rearrange order of atoms in a molecule
Give function of lyases.
Break a chemical bond w/out water
Give function and examples of ligases .
- Make chemical bond using ATP
- TPP, CoASH, Lipoamide, biotin
What are characteristics of an active site?
- Is only a few residues out of the protein
- Is a 3-D cleft/crevice/pocket, creating a unique microenvironment
- Determines substrate specificity by size and charge complementarity 4. Contacts with the substrate through noncovalent interactions
What is characteristic of allosteric binding?
- Does NOT occur at the active site, but follows the same interaction rules as an active site
- Involves a second substrate, which can be an activator or an inhibitor
Compare and contrast Apo and Holoenzymes
Apoenzymes:
• Incomplete
• Inactive
• Lack cofactor/coenzyme
Holoenzymes: • Whole • Active • Contain cofactor/coenzyme • Require allosteric activation!
What is Y and how is it calculated?? What are possible values for Y and what they mean?
Fractional saturation Y = [E-S]/[E]+[E-S]
= [S]/KD+[S]
Y = 0 - no ligand bound Y = 0.5 - half saturated Y = 1 - saturated
What is cooperativety?
Binding of each subsequent ligand influences the affinity (strength of interaction) of the next ligand to bind an active site
How do we interpret cooperativity?
In terms of cooperativity, we interpret Hill Coefficients in the following way:
• nH = 1 means nocooperativity
(sites are independent)
• nH > 1 means positivecooperativity
(affinity increases)
• 0 < nH < 1 means negativecooperativity
(affinity decreases)