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In enzymology, 2-aminomuconate deaminase (EC 3.5.99.5) (also known as amnd) is an enzyme that catalyzes the chemical reaction

2-aminomuconate + H₂O ${\displaystyle \rightleftharpoons }$ 4-oxalocrotonate + NH₃

Thus, the two substrates of this enzyme are 2-aminomuconate and H₂O, whereas its two products are 4-oxalocrotonate and NH₃.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is 2-aminomuconate aminohydrolase. This enzyme participates in tryptophan metabolism.

References

• He Z, Spain JC (1998). "A novel 2-aminomuconate deaminase in the nitrobenzene degradation pathway of Pseudomonas pseudoalcaligenes JS45". J. Bacteriol. 180 (9): 2502–6. PMC 107194. PMID 9573204.
• He Z, Spain JC (1997). "Studies of the catabolic pathway of degradation of nitrobenzene by Pseudomonas pseudoalcaligenes JS45: removal of the amino group from 2-aminomuconic semialdehyde". Appl. Environ. Microbiol. 63 (12): 4839–43. PMC 168809. PMID 9471964.

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