Extradiol Cleavage of 3-Methylcatechol by Catechol 1,2-Dioxygenase from Various Microorganisms-Reference-Cited by-同舟云学术

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

Published:1977-03 Issue:3 Volume:33 Page:725-727
ISSN:0099-2240
Container-title:Applied and Environmental Microbiology
language:en
Short-container-title:Appl Environ Microbiol

Author:

Hou C. T.¹,Patel R.¹,Lillard M. O.¹

Affiliation:

1. 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.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

Link

https://journals.asm.org/doi/pdf/10.1128/aem.33.3.725-727.1977

Reference14 articles.

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3. Circular dichroism ofholo- and apoprotocatechuate 3,4-dioxygenase form Pseudomonas aeruginosa;Hou C. T.;Biochemistry,1975

4. Immunological properties of protocatechuate 3,4-dioxygenase isofunctional enzymes;Hou C.;J. Bacteriol.,1976

5. Protocatechuate 3,4-dioxygenase from Acinetobacter calcoaceticus;Hou C. T.;Biochemistry,1976

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