330-10 JP 16

330-10 JP 16 - BISC 330L Sp2010 Lect JP 16 Friday 19 Feb...

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Unformatted text preview: BISC 330L Sp2010 Lect JP 16.ppt Friday, 19 Feb 2010 Petruska Lecture 15 (M-M Equation, Linear Plots, and Reversible Inhibition Model) Cont’d Lect. 16: Classical Inhibitors & Catalytic Strategies Reference: BTS (6th ed.) Chap. 8, 9 Summary of Equations in M-M Enzyme Kinetics he velocity equation, v = d[P]/dt, can be expressed as follows under steady-state conditions. a) v = k 2 [ES], the starting equation. At steady-state: [ES] = [E][S]/K M b) v = (k 2 /K M )[E][S], where (k 2 /K M ) indicates enzyme efficiency , when compared with k 1 . c) v = k 2 [E T ][S]/(K M +[S]) = V max [S]/(K M +[S]), = k 2 [E T ] = K D + ( k 2 / k 1 ) Curve of v vs. [S], a rectangular hyperbola predicted by Michelis-Menten model. v = V max [S]/( K M + [S]) 1 8 Fig . 13.9 (Lineweaver-Burk Linear Eq., called “double-reciprocal” plot of M-M Eq.) 8 4 1 {Note crowding of points 4 to 8) Hanes-Woolf Linear Eq. is more reliable. Fig. 13.10 1 4 8 (Note points 1-8 evenly spaced, in same order as original M-M plot of v vs . [S].) If the M-M model fits and V max is determined by catalysis (not by product release), then if enzyme is pure and [E T ] is known, k 2 = k cat = V max /[E T ] k cat , the turnover number, is the number of substrate molecules converted to produc per enzyme molecule per unit of time, when enzyme is saturated with substrate, i.e., when [ES] = [E T ]....
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This note was uploaded on 08/30/2010 for the course BIO 320 taught by Professor Wu during the Spring '10 term at USC.

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330-10 JP 16 - BISC 330L Sp2010 Lect JP 16 Friday 19 Feb...

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