Thomas D Hurley PhD

OBJECTIVES

  • To introduce the basic concepts of steady-state kinetics
  • To understand the significance of the Michaelis-Menton equation
  • To introduce the concept of multisubstrate systems
  • To develop the concept of enzyme inhibition
  • To introduce cooperative interactions and regulation of enzymes
  • To illustrate control mechanisms of enzyme activity

OUTLINE

  1. 1 Steady-State Kinetics 58
  2. 2 Enzyme Inhibition 72
  3. 3 Cooperative Behavior in Enzymes 78
  4. 4 Covalent Regulation of Enzyme Activity 81

Enzymes are biological catalysts that enable thousands of biological reactions that occur every second within cells. The kinetics of enzymatic reactions is important for the spatial and temporal regulation of cell processes and its measurement is used for diagnosis of diseases. Biochemical engineers manipulate biological processes with the use of enzymes in order to produce the desired products.

By and large, enzymes are the engines that drive the metabolic functions that underlie cellular functions. Enzymes are extraordinary catalysts, often accelerating chemical reactions by more than 108 times over the rates of the uncatalyzed reactions and they do so at relatively low temperature (37°C) and low pressure (~1 atm). They achieve their remarkable rate enhancements without sacrificing their selectivity for particular substrates, and these rates can be regulated through numerous mechanisms, providing the cell with precise control over what reactions to catalyze and the rate at which those reactions will occur. In this chapter, we will explore the manner in which enzymes interact with their substrates and how these reactions may be controlled through both noncovalent and covalent modifying agents.

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