Characterization of isofunctional ring-cleaving enzymes in aniline and 3-chloroaniline degradation by Pseudomonas acidovorans CA28.
During degradation of aniline and 3-chloroaniline, respectively, by Pseudomonas acidovorans CA28, selective induction of two catechol 1,2-dioxygenases (C12O) was observed. C12O I activity was the sole ring-cleaving enzyme detectable in cell-free extracts after growth on aniline, while C12O II was exclusively found after growth on 3-chloroaniline. Both enzymes were clearly differentiated by their elution behaviour on DEAE-cellulose and their substrate specificities. For C12O I high activity was demonstrable only with unsubstituted catechol, while C12O II showed preference for and high affinity towards chlorinated catechols. Therefore, evidence of different ortho-cleavage enzymes in Pseudomonas acidovorans CA28 involved in aniline and 3-chloroaniline metabolism, respectively, is indicated.
Hinteregger
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Abteilung für Umweltmikrobiologie, Technische Universität Wien, Vienna, Austria.
Loidl
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Streichsbier
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D000814:Aniline Compounds / Q000378:metabolism*; D050548:Catechol 1,2-Dioxygenase; D049308:Dioxygenases; D004790:Enzyme Induction; D010105:Oxygenases / Q000096:biosynthesis* / Q000737:chemistry / Q000302:isolation & purification; D011549:Pseudomonas / Q000201:enzymology* / Q000378:metabolism
D000814:Aniline Compounds; C031392:3-chloroaniline; D010105:Oxygenases; D049308:Dioxygenases; D050548:Catechol 1,2-Dioxygenase; C023650:aniline