| 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 | ||||||||
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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
4-trimethylammoniobutanoate + NADH + 2 HThe 3 substrates of this enzyme are 4-trimethylammoniobutanal, NAD, and H2O, whereas its 3 products are 4-trimethylammoniobutanoate, 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.
| Aldehyde/oxo oxidoreductases (EC 1.2) | |
|---|---|
| 1.2.1: NAD or NADP | |
| 1.2.2: cytochrome | |
| 1.2.3: oxygen | |
| 1.2.4: disulfide | |
| 1.2.7: iron–sulfur protein | |
| Enzymes | |
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| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
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