Biology Exam 2 Flashcards
Ligase
Formation of c-c, c-o, c-s, or c-n bonds using ATP cleavage
Synthetases
Transferase
Transfer of functional groups
Kinases, Transaminases
Lyase
Cleavage of c-c, c-o, c-n and other bonds by means other than hydrolysis or oxidation
Decarboxylases
Hydrolase
Formation of two products by hydrolyzing a substrate
peptides
Isomerase
Intramolecular rearrangements, transfer of groups within molecules
Mutases
Acid/Base
name from the perspective of enzyme
General: AA fun group
Specific: H2O (acceptor or donor)
Addition or loss of proton to make enzyme a better nucleophile or electrophile.
Electrostatic
The presence of opposite charges to stabilize the transition state of the substrate
Salt Bridge
Proximity and Orientation
Substrate first bind in the enzyme active site in the correct position
Always happens first
Oxidoreductase
Oxidation – Reduction
Transfer of H or O atoms
Oxidases (NAD+, NADH)
Metal Ion
The presence of inorganic material to stabilizes the transition state of the substrate.
Covalent
Formation of transilent covalent Bond
Formation of bond to stabalize the transition state of the substrate in the enzyme pocket.
What are the non-covalent interactions that could be made?
Vandaar waals
Hydrogen
Ionic
Ka
Association constant going to PL
Kd
Dissasociation constant going to P+L
Fractional Saturation
Occupied binding sites/Total binding sites
Protein-ligand interactions
-Reversible binding of P/L non-covalent interactions.
-Ligand binding induces conformational change.
-Equilibrium can be altered by effector molecules, can bind to protein and induce structure change.
Unbound
T-State, Tense
