| 2-aminomuconate deaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.99.5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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 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.
This page was last edited on 26 August 2023, at 12:25