Lec 4 - When α = α ’, then we also speak of...

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Metabolic Biochemistry BIBC 102 Winter 2007 Lecture 4, January 17, 2007
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k 1 k 2 E + S ES Products k -1 CHAPTER 6 Enzymes and Enzyme Kinetics Michaelis-Menten (1912-1916)
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k -1 + k 2 K m = k 1 k 2 [E] T [S] V o = K m + [S]
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Fig. 6-11 when K m = [S], then v o = 1/2 v max
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1 K m 1 1 = x + v o v max [S] v max y = ax + b
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Lineweaver-Burk Plot Double Reciprocal Plot box. 6-1
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Reactions with more than one substrate (more typical) Overall reaction : S 1 + S 2 P 1 + P 2
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Fig. 6-13
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LNC 6-14 a Lines intersect: ternary complex is formed in the reaction
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LNC 6-14 a Lines intersect: ternary complex is formed in the reaction 1/[S 1 ]
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LNC 6-13 b This case is also referred to as the Ping-Pong or double displacement mechanism
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LNC 6-14 b Lines do not intersect: no ternary complex is formed 1/[S 1 ]
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Enzyme Inhibitors
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Fig. 6-15a
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Competitive Inhibition α = 1 + [I] / K I box. 6-2.1 1/[S 1 ]
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Fig. 6-15b
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Uncompetitive Inhibition α ’ = 1 + [I] / K I box. 6-2.2 1/[S 1 ]
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Fig. 6-15c
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Mixed Inhibition
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Unformatted text preview: When α = α ’, then we also speak of noncompetitive inhibition box 6-2.3 1/[S 1 ] LNC 6-28 FEEDBACK INHIBITION Typically, the product at the end of a pathway inhibits an enzyme early in the pathway Purpose/rationale: the precursor is saved to be used for other reactions Allosteric Regulation of Enzymes LNC 6-26 C – catalytic subunit R – regulatory subunit LNC 6-27 ASPARTATE TRANSCARBAMYLASE two stacked catalytic clusters each with 3 catalytic subunits and 3 regulatory clusters (two polypeptides) LNC 6-29a homotropic enzyme: substrate is positive modulator (e.g. hemoglobin) LNC 6-29b No change in v max , but change in K m LNC 6-29c Both v max and K m change Part III Bioenergetics and Metabolism Chapter 13 in LNC urea End of Lecture 4, January 17, 2007...
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This note was uploaded on 02/25/2010 for the course BIBC na taught by Professor Schfler during the Spring '10 term at UCSD.

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Lec 4 - When α = α ’, then we also speak of...

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