Enzyme_Kinetics_concepts_review

Enzyme_Kinetics_concepts_review - Enzyme Kinetics...

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Enzyme Kinetics Influences on Enzyme Activity | Oxidation-Reduction Reactions | Introduction to Metabolism Influences on Enzyme Activity Substrate concentration Vmax is the maximal reaction velocity and is achieved when the substrate saturates the enzyme. Km is defined as the [substrate] needed to produce one half the maximal velocity of the reaction. Km reflects the affinity of an enzyme for its substrate; the smaller the value of Km the greater the affinity an enzymes has for its substrate. [substrate] in the cell is often equal to or less than its Km. This allows the enzyme to respond to small changes in [substrate] because it is still on the steep part of the curve. Enzyme concentration if the enzyme is saturated with substrate, increasing the [enzyme] increases the reaction velocity. Thus, Vmax is proportional to the [enzyme]. Temperature reaction rates increase with temperature increase; however, too high of a temperature causes protein breakdown. the Q10 describes the fold increase in the reaction rate that occurs with a 10 °C increase. pH most enzymes are pH sensitive and operate effectively only within a narrow pH range. Competitive/Noncompetitive inhibitors competitive inhibitors are chemically similar to the substrate making them able to bind to the enzymes. By doing so, they occupy the binding site, thus competing with the substrate for the active site on the enzyme. noncompetitive inhibitors do not resemble the substrate nor bind to the active site. However, it binds elsewhere on the enzyme which reduces the effectiveness of the enzyme Cofactors many enzymes require cofactors such as metal ions (e.g., Mg2+, Mn2+, Ca2+) or other coenzymes
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This note was uploaded on 03/27/2011 for the course BIO 2912 taught by Professor Waring/rappaport during the Spring '11 term at Temple.

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Enzyme_Kinetics_concepts_review - Enzyme Kinetics...

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