Bacterial degradation of N-cyclopropylmelamine : the steps to ring cleavage


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COOK, Alasdair M., Hugo GROSSENBACHER, Ralf HÜTTER, 1984. Bacterial degradation of N-cyclopropylmelamine : the steps to ring cleavage. In: Biochemical Journal. 222(2), pp. 315-320. ISSN 0264-6021. eISSN 1470-8728. Available under: doi: 10.1042/bj2220315

@article{Cook1984Bacte-6749, title={Bacterial degradation of N-cyclopropylmelamine : the steps to ring cleavage}, year={1984}, doi={10.1042/bj2220315}, number={2}, volume={222}, issn={0264-6021}, journal={Biochemical Journal}, pages={315--320}, author={Cook, Alasdair M. and Grossenbacher, Hugo and Hütter, Ralf} }

<rdf:RDF xmlns:dcterms="" xmlns:dc="" xmlns:rdf="" xmlns:bibo="" xmlns:dspace="" xmlns:foaf="" xmlns:void="" xmlns:xsd="" > <rdf:Description rdf:about=""> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dcterms:issued>1984</dcterms:issued> <dc:contributor>Hütter, Ralf</dc:contributor> <dc:language>eng</dc:language> <dcterms:abstract xml:lang="eng">The s-triazine cyclopropylmelamine (N-cyclopropyl-1,3,5-triazine-2,4,6-triamine) was degraded to about 6 mol of NH4+/mol of substrate by a mixture of two bacteria (strains A and D, both Pseudomonas spp.) Only strain A grew with cyclopropylmelamine as sole and limiting source of nitrogen. The organism obtained 2 mol of nitrogen/mol of substrate and excreted a product that was identified as cyclopropylammelide [6-cyclopropylamino-1,3,5-triazine-2,4(1 H,3 H)-dione]. Proteins in extracts from strain A were separated on a Sephadex G-200 column. Cyclopropylmelamine was found to be deaminated in two separable steps to cyclopropylammelide via cyclopropylammeline [4-amino-6-cyclopropylamino-1,3,5-triazine-2(1 H)-one], which was identified. Strain D could not utilize cyclopropylmelamine or cyclopropylammeline, but could utilize cyclopropylammelide (or homologue) as sole and limiting source of nitrogen and obtain about 4 mol of nitrogen/mol of substrate. Proteins in cell extracts from strain D were separated on a DEAE-cellulose column. Alkylammelides were degraded quantitatively by one enzyme fraction to 1 mol of cyanuric acid plus 1 mol of alkylamine/mol of substrate. The specific activities of enzymes in extracts of the two strains were as high as the activities observed during growth. The three activities studied in the two strains were all active under aerobic and oxygen-free conditions. The reactions appear to be hydrolytic, yielding 2 mol of NH4+ plus 1 mol of cyclopropylamine and 1 mol of cyanuric acid/mol of substrate.</dcterms:abstract> <dcterms:isPartOf rdf:resource=""/> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dcterms:title>Bacterial degradation of N-cyclopropylmelamine : the steps to ring cleavage</dcterms:title> <dcterms:bibliographicCitation>First publ. in: Biochemical Journal 222 (1984), 2, pp. 315 320</dcterms:bibliographicCitation> <dcterms:rights rdf:resource=""/> <dc:contributor>Grossenbacher, Hugo</dc:contributor> <dcterms:hasPart rdf:resource=""/> <dc:date rdf:datatype="">2011-03-24T17:28:55Z</dc:date> <dspace:isPartOfCollection rdf:resource=""/> <dspace:hasBitstream rdf:resource=""/> <dc:creator>Cook, Alasdair M.</dc:creator> <bibo:uri rdf:resource=""/> <dc:contributor>Cook, Alasdair M.</dc:contributor> <dc:format>application/pdf</dc:format> <dc:rights>terms-of-use</dc:rights> <dc:creator>Grossenbacher, Hugo</dc:creator> <dcterms:available rdf:datatype="">2011-03-24T17:28:55Z</dcterms:available> <dc:creator>Hütter, Ralf</dc:creator> </rdf:Description> </rdf:RDF>

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