lec 15 a - BL/CH 401 Lecture #15A - Introduction to Enzyme...

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BL/CH 401 Lecture #15A -- Introduction to Enzyme Mechanisms Part I. Features of Enzymatic Catalysis. Enzymes cause rate increases in reactions that are 10 times to 10,000 times greater than the best chemical catalysts. Enzymes, since they are proteins and must maintain their folded shape or conformation, operate under mild conditions (37°C/pH 7) and have high specificity. Enzymes achieve specificity via geometric and physical complementarity between the active site and the substrate. Figure 1. 3-D Geometric Fit of Substrate to Enzyme's Active Site. Of course, it is somewhat obvious that both the substrate and the enzyme are 3-D and that the shape of the substrate must fit the shape of the active site for the substrate to bind to the enzyme and the E-S complex to form. But an important aspect of this reality is that the enzyme and its active site are both asymmetric in the chemical sense that they are chiral. Amino acids are chiral and so the enzyme and its active site are formed by chiral structures and are themselves chiral. So if the substrate has an degree of chirality (ie either it has a chiral center or even one partially chiral - usually called pro-chiral, then the enzyme will bind the one form or stereo-isomer of the substrate. Let's take the example of an amino acid which is present in both the D- and L-forms, the enzyme will bind only one of these forms, which in most cases will be the L-form of the
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This note was uploaded on 09/02/2009 for the course BIO BL 401 taught by Professor Wilbur during the Spring '07 term at Michigan Technological University.

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lec 15 a - BL/CH 401 Lecture #15A - Introduction to Enzyme...

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