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. 1977 Mar;33(3):725–727. doi: 10.1128/aem.33.3.725-727.1977

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

C T Hou 1, R Patel 1, M O Lillard 1
PMCID: PMC170750  PMID: 16345232

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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Selected References

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  1. Fujiwara M., Golovleva L. A., Saeki Y., Nozaki M., Hayaishi O. Extradiol cleavage of 3-substituted catechols by an intradiol dioxygenase, pyrocatechase, from a Pseudomonad. J Biol Chem. 1975 Jul 10;250(13):4848–4855. [PubMed] [Google Scholar]
  2. Hou C. T. Circular dichroism of holo- and apoprotocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa. Biochemistry. 1975 Aug 26;14(17):3899–3902. doi: 10.1021/bi00688a025. [DOI] [PubMed] [Google Scholar]
  3. Hou C. T., Lillard M. O. Immunological properties of protocatechuate 3, 4-dioxygenase isofunctional enzymes. J Bacteriol. 1976 Apr;126(1):516–519. doi: 10.1128/jb.126.1.516-519.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Hou C. T., Lillard M. O., Schwartz R. D. Protocatechuate 3, 4-dioxygenase from Acinetobacter calcoaceticus. Biochemistry. 1976 Feb 10;15(3):582–588. doi: 10.1021/bi00648a020. [DOI] [PubMed] [Google Scholar]
  5. ICHIYAMA A., NAKAMURA S., KAWAI H., HONJO T., NISHIZUKA Y., HAYAISHI O., SENOH S. STUDIES ON THE METABOLISM OF THE BENZENE RING OF TRYPTOPHAN IN MAMMALIAN TISSUES. II. ENZYMIC FORMATION OF ALPHA-AMINOMUCONIC ACID FROM 3-HYDROXYANTHRANILIC ACID. J Biol Chem. 1965 Feb;240:740–749. [PubMed] [Google Scholar]
  6. Kojima Y., Fujisawa H., Nakazawa A., Nakazawa T., Kanetsuna F., Taniuchi H., Nozaki M., Hayaishi O. Studies on pyrocatechase. I. Purification and spectral properties. J Biol Chem. 1967 Jul 25;242(14):3270–3278. [PubMed] [Google Scholar]
  7. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  8. NAKAGAWA H., INOUE H., TAKEDA Y. CHARACTERISTICS OF CATECHOL OXYGENASE FROM BREVIBACTERIUM FUSCUM. J Biochem. 1963 Jul;54:65–74. doi: 10.1093/oxfordjournals.jbchem.a127748. [DOI] [PubMed] [Google Scholar]
  9. Nakazawa A., Nakazawa T., Kotani S., Nozaki M., Hayaishi O. Studies on pyrocatechase. 3. Circular dichroism and optical rotatory dispersion. J Biol Chem. 1969 Mar 25;244(6):1527–1532. [PubMed] [Google Scholar]
  10. Nakazawa T., Nozaki M., Hayaishi O., Yamano T. Sttudies on pyrocatechase. II. Electron spin resonance and other properties of iron in the active center. J Biol Chem. 1969 Jan 10;244(1):119–125. [PubMed] [Google Scholar]
  11. Patel R. N., Hou C. T., Felix A., Lillard M. O. Catechol 1,2-dioxygenase from Acinetobacter calcoaceticus: purification and properties. J Bacteriol. 1976 Jul;127(1):536–544. doi: 10.1128/jb.127.1.536-544.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Zaborsky O. R., Ogletree J., Hou C. T. Circular dichroism of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa. Biochim Biophys Acta. 1975 Mar 28;386(1):18–25. doi: 10.1016/0005-2795(75)90241-x. [DOI] [PubMed] [Google Scholar]

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