Week 6, Etc.

Front 1

what is the enzyme complementary to?

Back 1

the transition state

Front 2

what's the favorable interaction between enzyme and substrate called?

Back 2

binding energy

Front 3

describe a transition state analog?

Back 3

mimics the substrate in transition state

Front 4

what do serine proteases do?

Back 4

cleave the peptides

Front 5

what is the catalytic triad and what does each one do?

Back 5

ƒ Ser ‐ reactive, forms a temporary covalent bond with substrate
       ‐ Provides a specific pathway for the reaction
ƒ His ‐ acts as a base (later as an acid)
      ‐ accepts proton from OH of Ser to facilitate covalent bond formation
      ‐ Helps form covalent tetrahedral transition state/stabilizes negatively
         charged transition state
ƒ Asp ‐ stabilizes positive charge of His
        ‐ acts as temporary proton acceptor

Front 6

what does the oxyanion hole do?

Back 6

stabilize transition state through h-bonding

Front 7

what's the specificity pocket?

Back 7

binds to specific AA side chains

Front 8

What happens when each thing is damaged?

Back 8

loss of catalytic activity, mostly in serine

Front 9

3 ways to regulate enzymes?

Back 9

allosteric control, proteolytic cleavage, covalent modification

Front 10

what happens in allosteric control?

Back 10

reversible non-covalent modification, distal from the site

Front 11

what happens in covalent modification?

Back 11

modification on 1 or more residues that can alter an enzyme

Front 12

what happens in proteolytic activation?

Back 12

irreversible modification, conformational change