2,3-Dihydroxybenzoate 3,4-oxygenase from Pseudomonas fluorescens—Oxidation of a substrate analog

2,3-Dihydroxybenzoate is oxidized by extracts of Pseudomonas fluorescens to α-hydroxymuconic semialdehyde and CO 2. A noninducing substrate analog, 2,3-dihydroxy- p-toluate, has now been used to determine the site of ring cleavage. 2,3-Dihydroxy- p-toluate is oxidized quantitatively with the consump...

Full description

Saved in:
Bibliographic Details
Published inArchives of biochemistry and biophysics Vol. 138; no. 2; pp. 557 - 565
Main Authors Ribbons, D.W., Senior, P.J.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.06.1970
Subjects
Benzoates - metabolism
Chemical Phenomena
Chemistry
Enzyme Induction
Oxidation-Reduction
Oxidoreductases - metabolism
Oxygen
Pseudomonas - enzymology
Quaternary Ammonium Compounds
Online AccessGet full text

Cover

More Information
Summary:2,3-Dihydroxybenzoate is oxidized by extracts of Pseudomonas fluorescens to α-hydroxymuconic semialdehyde and CO 2. A noninducing substrate analog, 2,3-dihydroxy- p-toluate, has now been used to determine the site of ring cleavage. 2,3-Dihydroxy- p-toluate is oxidized quantitatively with the consumption of 1 mole of O 2, evolution of 1 mole of CO 2, and the accumulation of 2,6-diketoheptenoate. The product was characterized by (1) spectral analysis of the isolated acid, (2) ring closure in the presence of NH 4 + to form 6-methylpicolinate, and (3) its ready conversion to acetate in 76% yield, by extracts of Ps. aeruginosa T1. It is concluded that enzymic cleavage of the benzenoid nucleus by this oxygenase is between carbon atoms 3 and 4, and the enzyme has been named 2,3-dihydroxybenzoate 3,4-oxygenase.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0003-9861
1096-0384
DOI:10.1016/0003-9861(70)90381-4