BCH210H1 Lecture Notes - Lecture 20: Cyclooxygenase, Maud Menten, Nonsteroidal Anti-Inflammatory Drug

• School: UTSG
• Department: Biochemistry
• Course: BCH210H1
• Professor: Stavroula Andreopoulos

Document Summary

Under saturated conditions, we get a maximum velocity. The enzyme cant work any faster than the vmax. They said that enzyme + substrate goes to enzyme + product. It goes e + s = es = e + p. going from e+s to es is k1, going backwards is k-1. Going from es to e+p is k2, and k2 is the rate limiting step. Going forward only depends n how much substrase we have. Theres a canadian connection for maud menten, she went to uoft and became a physician, but since. Ca(cid:374)ada did(cid:374)"t let girls do resear(cid:272)h she (cid:449)e(cid:374)t to e(cid:374)gla(cid:374)d a(cid:374)d (cid:449)rked i(cid:374) leo(cid:374)or mi(cid:272)haelis la(cid:271). The rate of es formation is equal to the rate of es breakdown, which resulted in the steady state function, meaning its not changing. After 3 substitutions, we arrive at the michaelis menten equation. Km is a substrate concentration at the point where you have 50% of the max velocity of the enzyme.