| betaine-aldehyde dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Betaine aldehyde dehydrogenase tetramer, Staphylococcus aureus | |||||||||
| Identifiers | |||||||||
| EC no. | 1.2.1.8 | ||||||||
| CAS no. | 9028-90-4 | ||||||||
| 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, betaine-aldehyde dehydrogenase (EC 1.2.1.8) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are glycine betaine aldehyde, oxidised nicotinamide adenine dinucleotide (NAD+), and water. Its products are trimethylglycine, reduced NADH, and a proton. [1] [2] [3] [4] [5]
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 betaine-aldehyde:NAD+ oxidoreductase. Other names in common use include betaine aldehyde oxidase, BADH, betaine aldehyde dehydrogenase, and BetB. This enzyme participates in glycine, serine and threonine metabolism.
As of late 2007 [update] , 4 structures have been solved for this class of enzymes, with PDB accession codes 1A4S, 1BPW, 1WNB, and 1WND.