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Biochem J. Dec 15, 1982; 208(3): 679–684.
PMCID: PMC1154018

The degradative pathway of the s-triazine melamine. The steps to ring cleavage.

Abstract

1. The degradative pathway of melamine (1,3,5-triazine-2,4,6-triamine) was examined in Pseudomonas sp. strain A. 2. The bacterium grew with melamine, ammeline, ammelide, cyanuric acid or NH+4 as sole source of nitrogen, and each substrate was entirely metabolized. Utilization of ammeline, ammelide, cyanuric acid or NH+4 was concomitant with growth. But with melamine as substrate, a transient intermediate was detected, which was identified as ammeline by three methods. 3. Enzymes from strain A were separated by chromatography on DEAE-cellulose, and four activities were examined. 4. Melamine was converted stoichiometrically into equimolar amounts of ammeline and NH+4. 5. Ammeline was converted stoichiometrically into equimolar amounts of ammelide and NH+4; ammelide was identified by four methods. 6. Ammelide was converted stoichiometrically into equimolar amounts of cyanuric acid and NH+4; cyanuric acid was identified by four methods. 7. Cyanuric acid was converted by an enzyme preparation into an unidentified product with negligible release of NH+4. 8. The specific activities of the degradative enzymes (greater than or equal to 0.3 mkat/kg of protein) were high enough to explain the growth rate of the organism. 9. The bacterium converted 0.4 mM-melamine anaerobically into 2.3 mM-NH+4. 10. Two other pseudomonads and two strains of Klebsiella pneumoniae were also examined, with similar results. 11. The degradative pathway of melamine appears to be hydrolytic, and proceeds by three successive deaminations to cyanuric acid, which is further metabolized.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Harvey NL, Fewson CA, Holms WH. Apparatus for batch culture of micro-organisms. Lab Pract. 1968 Oct;17(10):1134–1136. [PubMed]
  • Kennedy SI, Fewson CA. Enzymes of the mandelate pathway in Bacterium N.C.I.B. 8250. Biochem J. 1968 Apr;107(4):497–506. [PMC free article] [PubMed]

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