Trimethylamine-oxide aldolase
| trimethylamine-oxide aldolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.2.32 | ||||||||
| CAS no. | 72561-08-1 | ||||||||
| 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, a trimethylamine-oxide aldolase (EC 4.1.2.32) is an enzyme that catalyzes the chemical reaction
- trimethylamine N-oxide dimethylamine + formaldehyde
Hence, this enzyme has one substrate, trimethylamine N-oxide, and two products, dimethylamine and formaldehyde.
This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is trimethylamine-N-oxide formaldehyde-lyase (dimethylamine-forming). Other names in common use include trimethylamine N-oxide formaldehyde-lyase, trimethylamine N-oxide aldolase, trimethylamine N-oxide demethylase, and trimethylamine-N-oxide formaldehyde-lyase. This enzyme participates in methane metabolism.
References
- Large PJ (1971). "Non-oxidative demethylation of trimethylamine N-oxide by Pseudomonas aminovorans". FEBS Lett. 18 (2): 297–300. doi:10.1016/0014-5793(71)80470-2. PMID 11946146.
- Myers PA, Zatman LJ (1971). "The metabolism of trimethylamine N-oxide by Bacillus PM6". Biochem. J. 121 (1): 10P. PMC 1176517. PMID 5116524.
