Betaine-aldehyde dehydrogenase
| 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.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1A4S, 1BPW, 1WNB, and 1WND.
References
- ^ Enzyme 1.2.1.8 at KEGG Pathway Database.
- ^ Eklund H; El-Ahmad, M; Ramaswamy, S; Hjelmqvist, L; Jörnvall, H; Eklund, H (1998). "Structure of betaine aldehyde dehydrogenase at 2.1 A resolution". Protein Sci. 7 (10): 2106–17. doi:10.1002/pro.5560071007. PMC 2143847. PMID 9792097.
- ^ Tsutui N, Hirasawa E (2003). "Purification and properties of betaine aldehyde dehydrogenase from Avena sativa". J. Plant Res. 116 (2): 133–40. Bibcode:2003JPlR..116..133L. doi:10.1007/s10265-003-0077-7. PMID 12736784. S2CID 23668905.
- ^ L; González-Segura, L; Mújica-Jiménez, C; Contreras-Díaz, L (2003). "Ligand-induced conformational changes of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa and Amaranthus hypochondriacus L. leaves affecting the reactivity of the catalytic thiol". Chem. Biol. Interact. 143–144: 129–37. Bibcode:2003CBI...143..129M. doi:10.1016/S0009-2797(02)00197-7. PMID 12604197.
- ^ Takabe T; Tanaka, Y; Aoki, K; Hibino, T; Jikuya, H; Takano, J; Takabe, T; Takabe, T (2003). "Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica". J. Biol. Chem. 278 (7): 4932–42. doi:10.1074/jbc.M210970200. PMID 12466265.
