4-trimethylammoniobutyraldehyde dehydrogenase

4-trimethylammoniobutyraldehyde dehydrogenase
Identifiers
EC no.1.2.1.47
CAS no.73361-01-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a 4-trimethylammoniobutyraldehyde dehydrogenase (EC 1.2.1.47) is an enzyme that catalyzes the chemical reaction

4-trimethylammoniobutanal
+ NAD+
 
 
H2O
H+
H2O
H+
 
4-trimethylammoniobutanoate
 

The three substrates of this enzyme are 4-trimethylammoniobutanal, oxidised nicotinamide adenine dinucleotide (NAD+), and water. Its products are 4-trimethylammoniobutanoate, reduced NADH, and a proton.[1][2]

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

  1. ^ Enzyme 1.2.1.47 at KEGG Pathway Database.
  2. ^ 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.