Extradiol cleavage of 3-methylcatechol by catechol 1,2-dioxygenase from various microorganisms
C T Hou1, R Patel, M O Lillard
1Corporate Research Laboratories, EXXON Research and Engineering Company, Linden, New Jersey 07036.
Abstract:
The isofunctional enzymes of catechol 1,2-dioxygenase from species of Acinetobacter, Pseudomonas, Nocardia, Alcaligenes, and Corynebacterium oxidize 3-methylcatechol according to both the intradiol and extradiol cleavage patterns. However, the enzyme preparations from Brevibacterium and Arthrobacter have only the intradiol cleavage activity. Comparison of substrate specificity among these isofunctional dioxygenases shows striking differences in the oxidation of 3-methylcatechol, 4-methylcatechol and pyrogallol.
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