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Lecture 1 - enzyme kinetics

The amount of enzyme e affects the maximum reaction

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Unformatted text preview: he maximum reaction rate. To better compare enzymes, we should normalize Vmax to the amount of enzyme (amount of catalytic sites) present. Vmax [E] = kcat Enzyme Kinetics! Effects of [Enzyme] on Reaction Rates! Summary •  Vmax is directly proportional to the molecules of enzyme present in a reaction •  The catalytic constant (kcat) of an enzyme describes the time it takes one molecule of enzyme to convert one molecule of substrate to product under saturating conditions (all active sites bound) kcat = turnover time; kcat= turnover time Enzyme Kinetics! Case Study - Genetic Engineering of Subtilisin! Subtilisin: Extracellular proteolytic enzyme synthesized by Grampositive bacteria eg. Bacillus subtilis. 6519 P roduction of a n Oxidatively Resistant Subtilisin iew of t he from B . a me (Wright et \ eled include a spartate32 i ad typical of ed is methioue identified es t o be oxiP 02 with refera nd Etson, t he N t o C cleft extendt o lower left TABLE I kc/ Wild Type { mef -222 v r \ ground secreted protease activity from these two major secreted proteases. Furthermore, possible recombination betw...
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