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Appl Environ Microbiol. 1977 March; 33(3): 725-727
Copyright © 1977 American Society for Microbiology. All Rights Reserved.

Extradiol Cleavage of 3-Methylcatechol by Catechol 1,2-Dioxygenase from Various Microorganisms

C. T. Hou, R. Patel and M. O. Lillard

Corporate 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.

Appl Environ Microbiol. 1977 March; 33(3): 725-727
Copyright © 1977 American Society for Microbiology. All Rights Reserved.





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Copyright © 1977 by the American Society for Microbiology. All rights reserved.