BCH210H1 Chapter 15: R15

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

Document Summary

When introducing an ei complex, we are essentially removing es complexes from the. Observing competitive inhibition: graph: as the concentration of inhibitors increase, the y-intercept remains the same therefore, vmax is unchanged, the x-intercept decreases (smaller value) therefore, the km value increases. Succinate dehydrogenase: a classic example of competitive inhibition, type of enzyme activity, co-enzyme, substrate: Malonate: both succinate and malonate are found in the krebs"s cycle, succinate will be oxidized to form fumarate (double bond forming between c2,c3, malonate has similar structure to succinate, only missing 1 ch2. Therefore, it will fit within the active site, binds non-covalently, and can"t undergo catalysis because a double bond can"t form between c2 and c3. Observing non competitive inhibition: graph: as the concentration of inhibitors increase, the y-intercept increases (larger values) therefore, Vmax value decreases: the x-intercept remains the same therefore, the.