A.
A hydrophobic pocket
✓
B.
A positively charged metal ion or lysine residue
✓
C.
A negatively charged aspartate residue
✓
D.
A neutral cysteine residue
✓
A.
Dissolving the enzyme in membranes
✓
B.
Driving substrate binding into the hydrophobic active site
✓
C.
Preventing substrate entry
✓
D.
Causing enzyme denaturation
✓
A.
General acid catalysis
✓
B.
Specific acid catalysis
✓
A.
Lines intersecting on the x axis
✓
B.
Parallel lines at varying substrate concentrations
✓
C.
A single straight line
✓
A.
Protects the enzyme from phosphorylation
✓
B.
Provides a large flat surface for adsorption
✓
C.
Sequesters the substrate from bulk solvent and creates a specialized environment
✓
D.
Allows simultaneous binding to DNA and proteins
✓
A.
Random sequential binding
✓
B.
Rate limiting formation of a covalent enzyme substrate intermediate
✓
C.
Rate limiting release of the first product
✓
D.
Slow activation of the free enzyme
✓
A.
The enzyme is denatured
✓
B.
Product concentration becomes zero
✓
C.
Further increase in substrate concentration fails to increase the reaction rate
✓
A.
Cofactor mediated catalysis
✓
D.
General acid catalysis
✓
A.
Change its own stereochemistry
✓
B.
Produce racemic products
✓
C.
Distinguish between optical isomers and act on only one
✓
D.
Convert every substrate into its optical isomer
✓
