4-trimethylammoniobutyraldehyde dehydrogenase
| 4-trimethylammoniobutyraldehyde dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.2.1.47 | ||||||||
| CAS no. | 73361-01-0 | ||||||||
| 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 4-trimethylammoniobutyraldehyde dehydrogenase (EC 1.2.1.47) is an enzyme that catalyzes the chemical reaction
- 4-trimethylammoniobutanal + NAD+ + H2O 4-trimethylammoniobutanoate + NADH + 2 H+
The 3 substrates of this enzyme are , NAD+, and H2O, whereas its 3 products are , NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-trimethylammoniobutanal:NAD+ 1-oxidoreductase. Other names in common use include 4-trimethylaminobutyraldehyde dehydrogenase, and 4-N-trimethylaminobutyraldehyde dehydrogenase. This enzyme participates in lysine degradation and carnitine biosynthesis.
See also[]
References[]
- Rebouche CJ, Engel AG (1980). "Tissue distribution of carnitine biosynthetic enzymes in man". Biochim. Biophys. Acta. 630 (1): 22–9. doi:10.1016/0304-4165(80)90133-6. PMID 6770910.
Categories:
- EC 1.2.1
- NADH-dependent enzymes
- Enzymes of unknown structure
- EC 1.2 stubs