Describes the enzyme known as pyruvate decarboxylase.
Written in 2006; 1,907 words; 9 sources; MLA; $ 60.95
Paper Summary:
This paper describes the functions, structure and activity of pyruvate decarboxylase. The paper also explains that the enzyme is very stable, and extremely easy to purify as well as its kinetic property and the oxidation processes for the enzyme. Additionally, the paper describes the anaerobic conditions of pyruvate decarboxylase and the three stages of aerobic respiration. Numerous figures are provided throughout the paper to help explain the topic.
From the Paper:
"The curve for v[S], the same as pryuvate decarboxylase, shows that catalytic activity inside of the enzyme has to be regulated by a substrate. The inactive enzyme can only be activated by 2-oxo acids and 2-oxo acid amides. These cannot be a substrate inside of the enzyme. The actual dissociation constant completely depends on electrophilic nature of a carbonyl group, the structure of the activator molecules are completely independent from the saturation concentration of the catalytic activity."
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