Evidence map›Paper›PMID 14617643›Full record

ArticleJournal of bacteriology2003

New bacterial pathway for 4- and 5-chlorosalicylate degradation via 4-chlorocatechol and maleylacetate in Pseudomonas sp. strain MT1.

Patricia Nikodem, Volker Hecht, Michael Schlömann, Dietmar H Pieper

Open access · greenAbstract readComparative Study
In one paragraph

Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.2field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 49 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Patricia NikodemDepartment of Environmental Microbiology, GBF-German Research Center for Biotechnology, D-38124 Braunschweig, Germany.
Volker Hecht
Michael Schlömann
Dietmar H Pieper
German Center for Infection Research · DETU Bergakademie Freiberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pseudomonas sp. strain MT1 is capable of degrading 4- and 5-chlorosalicylates via 4-chlorocatechol, 3-chloromuconate, and maleylacetate by a novel pathway. 3-Chloromuconate is transformed by muconate cycloisomerase of MT1 into protoanemonin, a dominant reaction product, as previously shown for other muconate cycloisomerases. However, kinetic data indicate that the muconate cycloisomerase of MT1 is specialized for 3-chloromuconate conversion and is not able to form cis-dienelactone. Protoanemonin is obviously a dead-end product of the pathway. A trans-dienelactone hydrolase (trans-DLH) was induced during growth on chlorosalicylates. Even though the purified enzyme did not act on either 3-chloromuconate or protoanemonin, the presence of muconate cylcoisomerase and trans-DLH together resulted in considerably lower protoanemonin concentrations but larger amounts of maleylacetate formed from 3-chloromuconate than the presence of muconate cycloisomerase alone resulted in. As trans-DLH also acts on 4-fluoromuconolactone, forming maleylacetate, we suggest that this enzyme acts on 4-chloromuconolactone as an intermediate in the muconate cycloisomerase-catalyzed transformation of 3-chloromuconate, thus preventing protoanemonin formation and favoring maleylacetate formation. The maleylacetate formed in this way is reduced by maleylacetate reductase. Chlorosalicylate degradation in MT1 thus occurs by a new pathway consisting of a patchwork of reactions catalyzed by enzymes from the 3-oxoadipate pathway (catechol 1,2-dioxygenase, muconate cycloisomerase) and the chlorocatechol pathway (maleylacetate reductase) and a trans-DLH.

Indexed as

DioxygenasesAmino Acid SequenceCarboxylic Ester HydrolasesCatechol 1,2-DioxygenaseCatecholsFuransGenome, BacterialIntramolecular LyasesMaleatesMolecular Sequence DataMultienzyme ComplexesOxidoreductases Acting on CH-CH Group DonorsOxygenasesPseudomonasSalicylatesSequence Homology, Amino Acid4-chlorocatechol4-chlorosalicylic acid5-chlorosalicylic acidCarboxylic Ester HydrolasescarboxymethylenebutenolidaseCatechol 1,2-DioxygenaseCatecholsDioxygenasesFuransIntramolecular LyasesMaleatesmaleoylacetic acidmaleylacetate reductasemuconate cycloisomeraseMultienzyme ComplexesOxidoreductases Acting on CH-CH Group DonorsOxygenasesprotoanemoninSalicylatesXenobiotics

Identifiers

PMID14617643
PMCPMC262710
OpenAlexW2092193412

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.