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Lecture

BIOCH 200 (March 10, 2014) - Enzymes

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Department
Biochemistry
Course
BIOCH200
Professor
Walter Dixon
Semester
Winter

Description
BIOCH 200 Enzyme (March 10, 2014) • *The higher the [S] needed for V max/2 to be reached, the lower the affinity the enzyme has for the substrate • **V max(plateau region) represents when all the enzyme active sites are saturated… this plateau does NOT mean that all the substrate has been converted to product because V is the speed at which the reaction is occurring. If the reaction is still occurring, that means that there is still substrate present in the solution that hasn’t been converted!!! • *Mechanisms for Regulation Enzyme Activity o *Competitive inhibition  *Competitive inhibitors bind reversibly to active sites (acts as physical block)  compete for the same site on the enzyme • May resemble the substrate OR transition state o *If it resembles the transition state, it is an even better inhibitor because the substrate is more favourable and will therefore be less likely to partake in reaction. • More competitive inhibitors bound  less active sites available  increase in Km (more substrate needed to reach V max/2) • *Inhibition can be overcome by increasing substrate concentration [S] (remember, it’s a competition. If there is more substrate available there is a higher chance for them to bind to the substrate than inhibitory molecules) o *There is no change in V maxvalue… it just takes longer for it to be reached = higher Km value  *Competitive inhibitors decrease the apparent affinity (K ) between M enzyme and substrate shown on a graph as a higher K valum o Allostery (activator/inhibitor)  Many enzymes are oligomeric (multi-subunit)  *Reaction rate (velocity) and substrate concentration graph will
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