释义 |
- Structural studies
- References
{{enzyme | Name = betaine-aldehyde dehydrogenase | EC_number = 1.2.1.8 | CAS_number = 9028-90-4 | IUBMB_EC_number = 1/2/1/8 | GO_code = 0008802 | image = 4q92.jpg | width = 270 | caption = Betaine aldehyde dehydrogenase tetramer, Staphylococcus aureus }}In enzymology, a betaine-aldehyde dehydrogenase ({{EC number|1.2.1.8}}) is an enzyme that catalyzes the chemical reaction betaine aldehyde + NAD+ + H2O betaine + NADH + 2 H+ The 3 substrates of this enzyme are betaine aldehyde, NAD+, and H2O, whereas its 3 products are betaine, 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 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|2007|alt=As of late 2007}}, 4 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1A4S}}, {{PDB link|1BPW}}, {{PDB link|1WNB}}, and {{PDB link|1WND}}.References- {{cite journal |vauthors=ROTHSCHILD HA, BARRON ES | date = 1954 | title = The oxidation of betaine aldehyde by betaine aldehyde dehydrogenase | journal = J. Biol. Chem. | volume = 209 | pages = 511–23 | pmid = 13192104 | issue = 2 }}
- {{cite journal |vauthors=Tsutui N, Hirasawa E | date = 2003 | title = Purification and properties of betaine aldehyde dehydrogenase from Avena sativa | journal = J. Plant. Res. | volume = 116 | pages = 133–40 | pmid = 12736784 | doi = 10.1007/s10265-003-0077-7 | issue = 2 }}
- {{cite journal | author = L | date = 2003 | title = Ligand-induced conformational changes of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa and Amaranthus hypochondriacus L. leaves affecting the reactivity of the catalytic thiol | journal = Chem. Biol. Interact. | volume = 143-144 | pages = 129–37 | pmid = 12604197 | doi = 10.1016/S0009-2797(02)00197-7 | last2 = González-Segura | first2 = L | last3 = Mújica-Jiménez | first3 = C | last4 = Contreras-Díaz | first4 = L }}
- {{cite journal | author = Eklund H | date = 1998 | title = Structure of betaine aldehyde dehydrogenase at 2.1 A resolution | journal = Protein Sci. | volume = 7 | pages = 2106–17 | pmid = 9792097 | last2 = El-Ahmad | first2 = M | last3 = Ramaswamy | first3 = S | last4 = Hjelmqvist | first4 = L | last5 = Jörnvall | first5 = H | last6 = Eklund | first6 = H | issue = 10 | pmc = 2143847 | doi = 10.1002/pro.5560071007 }}
- {{cite journal | author = Takabe T | date = 2003 | title = Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica | journal = J. Biol. Chem. | volume = 278 | pages = 4932–42 | pmid = 12466265 | doi = 10.1074/jbc.M210970200 | last2 = Tanaka | first2 = Y | last3 = Aoki | first3 = K | last4 = Hibino | first4 = T | last5 = Jikuya | first5 = H | last6 = Takano | first6 = J | last7 = Takabe | first7 = T | last8 = Takabe | first8 = T | issue = 7 }}
{{Aldehyde/Oxo oxidoreductases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{1.2-enzyme-stub}} 3 : EC 1.2.1|NADH-dependent enzymes|Enzymes of known structure |