Biology:Trimethylamine-oxide aldolase
From HandWiki
| trimethylamine-oxide aldolase | |||||||||
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| Identifiers | |||||||||
| EC number | 4.1.2.32 | ||||||||
| CAS number | 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 | ||||||||
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The enzyme trimethylamine-oxide aldolase (EC 4.1.2.32) catalyzes the chemical reaction
- trimethylamine N-oxide [math]\displaystyle{ \rightleftharpoons }[/math] dimethylamine + 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.
- "The metabolism of trimethylamine N-oxide by Bacillus PM6". Biochem. J. 121 (1): 10P. 1971. PMID 5116524.
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