Practical Significance of Kinetic Constants
The study of enzyme kinetics is important for two basic reasons. Firstly,
it helps explain how enzymes work, and secondly, it helps predict how
enzymes behave in living organisms. The kinetic constants defined
above, KM and Vmax, are critical to attempts to understand how
enzymes work together to control metabolism.
Making these predictions is not trivial, even for simple systems. For
example, oxaloacetate is formed by malate dehydrogenase within the
mitochondrion. Oxaloacetate can then be consumed by citrate
synthase, phosphoenolpyruvate carboxykinase or aspartate
aminotransferase, feeding into the citric acid cycle, gluconeogenesis or
aspartic acid biosynthesis, respectively. Being able to predict how much
oxaloacetate goes into which pathway requires knowledge of the
concentration of oxaloacetate as well as the concentration and kinetics
of each of these enzymes.
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