Most likely on exam

Lec 16

• Creatine is used for only a short burst of energy

• During DD, never at any time are the two substrates on the enzyme at the same time

Lec 17

• Enzymes do NOT go through an intermediate

• What is the transition state?

• Difference between specificity and affinity

  • Specificity is what the enzyme CAN take

  • Affinity falls under specificity and is what the enzyme PREFERS

• A lot of molecules will take advantage of electrostatis (slide 8-9)

• TSA’s bind better than comp. inhibitors bc they look like the transition state

• What will move enzyme catalysis along?

• Prosthetic groups are coenzymes (NAD, FAD, and heme are examples)

• Trypsin does covalent modification

• Water and His can act as acid & base (proto=acid depro=base)

• Primary aa!!!! Who is in the active site

Lec 18

• 4 different mechanisms of catalysis

Lec 19

• Catalytic triads: Asp, His, Ser (?)

• Slide 9 (pockets for trypsin, chymo, and elastase)

• You can have high affinity and low specificity and vice-versa

• Specificity is dictated by the active site

• Serine protease mechanism (14 & 15)

• All triads will have an acid, base, and a nucleophile

• Aspartic proteases have no covalent catalysis

• LBHB’s play a role in aspartic proteases (proteases have a tetrahedral intermediate).

Lec 20/21/22

• All 5 enzyme regulation methods

• MWC doesn’t explain negative cooperativity bc you’re all or none

• Hemoglobin is NOT an enzyme but it still uses the KNF model

• Bohr effect is a really good example of cooperativity

From Rabiya

• Slide 30 lecture 22

• Slide 28 lecture 20/21

• Slide 6 lecture 16

• Slide 13 lecture 17

• Slide 12 lecture 16

• Slide 8 lecture 19

• Generally all of the examples (and maybe not the examples in the tables)