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Updated: Aug 18, 2026

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
Divergency of structure and function of vertebrate xanthine:NAD+ oxidoreductase
1Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw.
Abstract:
Selection pressure for increasing metabolic flux through a define metabolic pathway affects the enzyme levels, enzyme structure and their kinetic properties. These aspects exemplified by xanthine oxidoreductase from vertebrates of various type of nitrogen excretion are discussed. Two trends in evolutionary kinetic changes of oxypurine hydroxylating activity could be distinguished. Changes in the subunit structure and kinetic properties suggest that the domain catalysing oxypurine hydroxylation and the one cooperating with NAD+ evolved through separate pathways.
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