CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.309 | Aldehyde Dehydrogenase; Chain A, domain 2 |
|
3.40.309.10 | Aldehyde Dehydrogenase; Chain A, domain 2 |
Domain Context
CATH Clusters
| Superfamily | Aldehyde Dehydrogenase; Chain A, domain 2 |
| Functional Family | 4-trimethylaminobutyraldehyde dehydrogenase isoform X1 |
Enzyme Information
| 1.2.1.3 |
Aldehyde dehydrogenase (NAD(+)).
based on mapping to UniProt P49189
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.
|
| 1.2.1.19 |
Aminobutyraldehyde dehydrogenase.
based on mapping to UniProt P49189
4-aminobutanal + NAD(+) + H(2)O = 4-aminobutanoate + NADH.
-!- The enzyme from some species exhibits broad substrate specificity and has a marked preference for straight-chain aldehydes (up to 7 carbon atoms) as substrates. -!- The plant enzyme also acts on 4-guanidinobutanal (cf. EC 1.2.1.54). -!- As 1-pyrroline and 4-aminobutanal are in equilibrium and can be interconverted spontaneously, 1-pyrroline may act as the starting substrate. -!- Formerly EC 1.5.1.35.
|
| 1.2.1.47 |
4-trimethylammoniobutyraldehyde dehydrogenase.
based on mapping to UniProt P49189
4-trimethylammoniobutanal + NAD(+) + H(2)O = 4-trimethylammoniobutanoate + NADH.
|
UniProtKB Entries (1)
| P49189 |
AL9A1_HUMAN
Homo sapiens
4-trimethylaminobutyraldehyde dehydrogenase
|
PDB Structure
| PDB | 6QAO |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Kinetic and structural analysis of human ALDH9A1.
Biosci.Rep.
|
