Please use this identifier to cite or link to this item:
http://dx.doi.org/10.18419/opus-8021
Authors: | Pieper, Dietmar H. Reineke, Walter Engesser, Karl-Heinrich Knackmuss, Hans-Joachim |
Title: | Metabolism of 2,4-dichlorophenoxyacetic acid, 4-chloro-2-methylphenoxyacetic acid and 2-methylphenoxyacetic acid by Alcaligenes eutrophus JMP 134 |
Issue Date: | 1988 |
metadata.ubs.publikation.typ: | Zeitschriftenartikel |
metadata.ubs.publikation.source: | Archives of microbiology 150 (1988), S. 95-102. URL http://dx.doi.org./10.1007/BF00409724 |
URI: | http://nbn-resolving.de/urn:nbn:de:bsz:93-opus-76540 http://elib.uni-stuttgart.de/handle/11682/8038 http://dx.doi.org/10.18419/opus-8021 |
Abstract: | Of eleven substituted phenoxyacetic acids tested, only three (2,4-dichloro-, 4-chloro-2-methyl- and 2-methylphenoxyacetic acid) served as growth substrates for Alcaligenes eutrophus JMP 134. Whereas only one enzyme seems to be responsible for the initial cleavage of the ether bond, there was evidence for the presence of three different phenol hydroxylases in this strain. 3,5-Dichlorocatechol and 5-chloro-3-methylcatechol, metabolites of the degradation of 2,4-dichlorophenoxyacetic acid and 4-chloro-2-methylphenoxyacetic acid, respectively, were exclusively metabolized via the ortho-cleavage pathway. 2-Methylphenoxyacetic acid-grown cells showed simultaneous induction of meta- and ortho-cleavage enzymes. Two catechol 1,2-dioxygenases responsible for ortho-cleavage of the intermediate catechols were partially purified and characterized. One of these enzymes converted 3,5-dichlorocatechol considerably faster than catechol or 3-chlorocatechol. A new enzyme for the cycloisomerisation of muconates was found, which exhibited high activity against the ring-cleavage products of 3,5-dichlorocatechol and 4-chlorocatechol, but low activities against 2-chloromuconate and muconate. |
Appears in Collections: | 15 Fakultätsübergreifend / Sonstige Einrichtung |
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