2.4 lecture Flashcards
What do enzymes do?
-They act as catalysts and lower activation energy
-equilibrium is reached faster
What don’t enzymes do?
-does not change equilibrium points for reactions
-does not shift equilibrium toward more product
Mechanisms enzymes use to lower activation energy?
1.catalytically active groups (polar/charged)
2.properly aligning groups
3.more weak intermolecular reactions are formed between enzyme and transition state
Proteases
Cleave peptide bonds in the backbone of proteins
Chymotrypsin structure
- 2 anti parallel beta barrel domains that sandwich together
What are the structural requirements for chymotrypsin activity
- catalytic triad
- oxyanion hole
- substrate binding pocket
- specificity pocket
catalytic triad
- Serine (Ser)
- Histidine (His)
- Aspartate (Asp)
Serine 95: catalytic triad
forms alkoxide ion that acts as a nucleophile and covalently bonds w/ the substrate
Histidine 57: catalytic triad
acts as a general base to ionize the serine side chain and turns it into nucleophilic alkoxide
Aspartate 102: catalytic triad
Stabilizes the positively charged histidine
Oxyanion hole
formation of tetrahedral state
Substrate binding pocket
binds peptide chains regardless of amino acid content
Specificity pocket: Chymotrypsin
cuts after a bulky residue (F,Y,W)
Specificity pocket: Trypsin
cuts after a positively charged residue (K, R)
Specificity pocket: Elastase
cuts after small hydrophobic amino acids (A, V, G)