2-Aminomuconic acid

2-Aminomuconic acid
	Skeletal formula of 2-aminomuconic acid
	Ball-and-stick model of 2-aminomuconic acid
Names
	Preferred IUPAC name (2Z,4E)-2-Aminohexa-2,4-dienedioic acid
Identifiers
CAS Number	4548-99-6 ;
3D model (JSmol)	Interactive image ;
ChEBI	CHEBI:16886 ;
ChemSpider	4573610 ;
PubChem CID	5459864 ;
UNII	9PX3G8GFQ7 ;
CompTox Dashboard (EPA)	DTXSID70274256 ;
	InChI InChI=1S/C6H7NO4/c7-4(6(10)11)2-1-3-5(8)9/h1-3H,7H2,(H,8,9)(H,10,11)/b3-1+,4-2- Key: ZRHONLCTYUYMIQ-TZFCGSKZSA-N ;
	SMILES C(=C\C(=O)O)/C=C(/C(=O)O)\N;
Properties
Chemical formula	C6H7NO4
Molar mass	157.12 g/mol
Density	1.461 g/mL
Boiling point	368.4 °C (695.1 °F; 641.5 K)
	Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). verify (what is ?) Infobox references

Last updated September 23, 2025

2-Aminomuconic acid (also known as 2-aminomuconate) is an unsaturated dicarboxylic amino acid. It serves as a biochemical intermediate in the microbial degradation of various aromatic compounds and is involved in the oxidative cleavage steps of the kynurenine pathway of tryptophan catabolism.

Structure and basic properties

2-Aminomuconic acid is a six-carbon molecule bearing two carboxyl groups, two conjugated double bonds, and a primary amino substituent at carbon 2. The neutral formula is C₆H₇NO₄. The molecule is commonly encountered in its ionized form, 2-aminomuconate, under physiological and environmental aqueous conditions.^[1]

Specific physical constants such as pKa values, solubility, and spectroscopic data are not comprehensively tabulated in the primary literature and should be added only with a verified source.

Occurrence and metabolic context

2-Aminomuconic acid is observed in two general biological contexts:

In microbial biodegradation of aromatic xenobiotics, for example certain nitroaromatic compounds, where ring-cleavage pathways produce aminomuconic intermediates prior to further downstream processing. The compound appears as a catabolic intermediate in several bacterial strains studied under laboratory conditions.^[1]

In the oxidative degradation of tryptophan via the kynurenine pathway, intermediates with structural relation to aminomuconate are formed during enzymatic ring opening and aldehyde oxidation steps.^[2]

Wherever it appears, the ionized form 2-aminomuconate is typically the biologically relevant species.^{[ citation needed ]}

Biosynthesis and enzymology

In enzymatic schemes described in the literature:

The immediate precursor known in many pathways is 2-aminomuconate semialdehyde, which can be oxidized to 2-aminomuconate by aldehyde dehydrogenase activity. Human ALDH8A1 has been reported to accept related substrates in the kynurenine pathway context.^[2]

Bacterial pathways include enzymes that catalyze ring cleavage and subsequent deamination or dehydrogenation reactions. A 2-aminomuconate deaminase activity has been reported in bacterial isolates that degrade nitrobenzene derivatives; this enzyme converts 2-aminomuconate to downstream catabolites such as 4-oxalocrotonate, releasing ammonium in the process.

Details such as kinetic constants, mechanism and gene names vary by organism and strain and should be cited from the primary enzymology literature for each specific claim.

Environmental and applied relevance

In environmental microbiology, pathways involving 2-aminomuconate are part of bacterial systems that allow mineralization of aromatic pollutants, converting recalcitrant compounds into metabolites that join central carbon metabolism. Such pathways are of interest for biodegradation and bioremediation research.^[1]

Safety and handling

This article does not provide laboratory protocols. Any experimental work involving chemical intermediates or microbial strains should follow institutional biosafety and chemical safety guidelines and consult primary sources for concentrations, conditions and hazard classifications.

References

1 2 3 He, Z.; Nishino, S. F. (1997). "Complete mineralization of 2,4,6-trinitrotoluene in liquid medium by a bacterial consortium". Applied and Environmental Microbiology. 63 (7): 2704–2709. doi:10.1128/aem.63.7.2925-2927.1997. PMC 168588 . PMID 16535658.
1 2 Davis, T. A.; Han, Q.; Christman, R.; Huang, Y.; Li, J. (2018). "Structural and functional insights into the evolution of aldehyde dehydrogenases in tryptophan metabolism". Journal of Biological Chemistry. 293 (22): 8577–8589. doi: 10.1074/jbc.RA118.002274 (inactive 21 September 2025). PMC 6005452 . PMID 29650623.{{cite journal}}: CS1 maint: DOI inactive as of September 2025 (link)