CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.605 | Aldehyde Dehydrogenase; Chain A, domain 1 |
|
3.40.605.10 | Aldehyde Dehydrogenase; Chain A, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Aldehyde Dehydrogenase; Chain A, domain 1 |
| Functional Family | alpha-aminoadipic semialdehyde dehydrogenase |
Enzyme Information
| 1.2.1.8 |
Betaine-aldehyde dehydrogenase.
based on mapping to UniProt P49419
Betaine aldehyde + NAD(+) + H(2)O = betaine + NADH.
-!- In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. -!- This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria. -!- In contrast, different enzymes are involved in the first reaction. -!- In plants, this reaction is catalyzed by EC 1.14.15.7, whereas in animals and many bacteria, it is catalyzed by either membrane-bound EC 1.1.99.1 or soluble EC 1.1.3.17. -!- In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 and EC 2.1.1.157.
|
| 1.2.1.31 |
L-aminoadipate-semialdehyde dehydrogenase.
based on mapping to UniProt P49419
(S)-2-amino-6-oxohexanoate + NAD(P)(+) + H(2)O = L-2-aminoadipate + NAD(P)H.
-!- (S)-2-amino-6-oxohexanoate undergoes a spontaneous dehydration forming the cyclic (S)-2,3,4,5-tetrahydropyridine-2-carboxylate, which serves as a substrate for the hydrogenation reaction.
|
| 1.2.1.3 |
Aldehyde dehydrogenase (NAD(+)).
based on mapping to UniProt P49419
An aldehyde + NAD(+) + H(2)O = a carboxylate + NADH.
-!- Wide specificity, including oxidation of D-glucuronolactone to D-glucarate. -!- Formerly EC 1.1.1.70.
|
UniProtKB Entries (1)
| P49419 |
AL7A1_HUMAN
Homo sapiens
Alpha-aminoadipic semialdehyde dehydrogenase
|
PDB Structure
| PDB | 2J6L |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Aldehyde Dehydrogenase 7A1 (Aldh7A1) is a Novel Enzyme Involved in Cellular Defense Against Hyperosmotic Stress.
J.Biol.Chem.
|
