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
✓
A.
Cofactor mediated catalysis
✓
D.
General acid catalysis
✓
A.
The enzyme is denatured
✓
B.
Product concentration becomes zero
✓
C.
Further increase in substrate concentration fails to increase the reaction rate
✓
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.
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.
Lines intersecting on the x axis
✓
B.
Parallel lines at varying substrate concentrations
✓
C.
A single straight line
✓
A.
A completely uniform charge distribution
✓
B.
A significantly lowered dielectric constant that enhances electrostatic interactions
✓
C.
A pH always equal to 7.0
✓
D.
An unlimited supply of free water molecules
✓
A.
Random substrate binding
✓
B.
Both substrates bind before any product is released, in a compulsory order
✓
C.
Product leaves before all substrates bind
✓
D.
Reaction rate is independent of the second substrate
✓
A.
Quaternary structure
✓
B.
Amino acid side chains arranged in the active site
✓
B.
Hydrophobic and non polar
✓
C.
Rich in lysine residues
✓
A.
Substrate inhibits product
✓
B.
One product is released before all substrates bind
✓
C.
Cooperative binding occurs
✓
D.
Non competitive inhibition occurs
✓
A.
Sequential ordered mechanism
✓
B.
Sequential random mechanism
✓
C.
Ping pong double displacement mechanism
✓
D.
Concerted acid base mechanism
✓
A.
Release of the unaltered second substrate
✓
B.
Binding of a water molecule and its nucleophilic attack on the acyl enzyme intermediate
✓
C.
Binding of an allosteric inhibitor
✓
D.
Auto degradation of the enzyme
✓
A.
Denaturing the substrate
✓
B.
Binding two substrates close together to increase their effective concentration
✓
C.
Lowering the pH of the solution
✓
D.
Using a metal ion to generate hydroxyl radicals
✓
B.
Histidine acting as a general base
✓
C.
Aspartate donating a proton
✓
D.
Formation of a disulfide bond
✓
A.
Directly break substrate bonds
✓
B.
Increase activation energy
✓
C.
Lower activation energy by stabilizing the transition state
✓
D.
Dissociate the enzyme cofactor complex
✓
