Enzymes
| UniProtKB help_outline | 1 proteins |
| Enzyme class help_outline |
|
Reaction participants Show >> << Hide
- Name help_outline 1-carboxybiuret Identifier CHEBI:142864 Charge -1 Formula C3H4N3O4 InChIKeyhelp_outline HAKPEUOAOGGSPC-UHFFFAOYSA-M SMILEShelp_outline NC(NC(NC([O-])=O)=O)=O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NH4+ Identifier CHEBI:28938 (CAS: 14798-03-9) help_outline Charge 1 Formula H4N InChIKeyhelp_outline QGZKDVFQNNGYKY-UHFFFAOYSA-O SMILEShelp_outline [H][N+]([H])([H])[H] 2D coordinates Mol file for the small molecule Search links Involved in 528 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline urea-1,3-dicarboxylate Identifier CHEBI:142865 Charge -2 Formula C3H2N2O5 InChIKeyhelp_outline OBMKNHGTYMWONF-UHFFFAOYSA-L SMILEShelp_outline [O-]C(NC(NC([O-])=O)=O)=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:58900 | RHEA:58901 | RHEA:58902 | RHEA:58903 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
|||
| EC numbers help_outline | ||||
| MetaCyc help_outline |
Publications
-
An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme.
Esquirol L., Peat T.S., Wilding M., Liu J.W., French N.G., Hartley C.J., Onagi H., Nebl T., Easton C.J., Newman J., Scott C.
Cyanuric acid is a metabolic intermediate of <i>s</i>-triazines, such as atrazine (a common herbicide) and melamine (used in resins and plastics). Cyanuric acid is mineralized to ammonia and carbon dioxide by the soil bacterium <i>Pseudomonas</i> sp. strain ADP via three hydrolytic enzymes (AtzD, ... >> More
Cyanuric acid is a metabolic intermediate of <i>s</i>-triazines, such as atrazine (a common herbicide) and melamine (used in resins and plastics). Cyanuric acid is mineralized to ammonia and carbon dioxide by the soil bacterium <i>Pseudomonas</i> sp. strain ADP via three hydrolytic enzymes (AtzD, AtzE, and AtzF). Here, we report the purification and biochemical and structural characterization of AtzE. Contrary to previous reports, we found that AtzE is not a biuret amidohydrolase, but instead it catalyzes the hydrolytic deamination of 1-carboxybiuret. X-ray crystal structures of apo AtzE and AtzE bound with the suicide inhibitor phenyl phosphorodiamidate revealed that the AtzE enzyme complex consists of two independent molecules in the asymmetric unit. We also show that AtzE forms an α2β2 heterotetramer with a previously unidentified 68-amino acid-long protein (AtzG) encoded in the cyanuric acid mineralization operon from <i>Pseudomonas</i> sp. strain ADP. Moreover, we observed that AtzG is essential for the production of soluble, active AtzE and that this obligate interaction is a vestige of their shared evolutionary origin. We propose that AtzEG was likely recruited into the cyanuric acid-mineralizing pathway from an ancestral glutamine transamidosome that required protein-protein interactions to enforce the exclusion of solvent from the transamidation reaction. << Less
J. Biol. Chem. 293:7880-7891(2018) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.