EC Number   |
General Information |
Reference |
|---|
    1.2.1.31 | malfunction |
alpha-AASA dehydrogenase deficiency results in the accumulation of pathognomonic alpha-aminoadipic semialdehyde (in cerebrospinal fluid, plasma and urine) and pipecolic acid (cerebrospinal fluid and plasma) in affected patients |
712017 |
| 1.2.1.31 | malfunction |
enzyme deficiency causes pyridoxine-dependent epilepsy |
763341 |
| 1.2.1.31 | malfunction |
mutations in the ALDH7A1 gene can cause the autosomal recessive metabolic disease pyridoxine-dependent epilepsy (PDE), which is characterized by seizure activity within days of birth. Although PDE symptoms can be mitigated with high doses of pyridoxine (vitamin B6) and a lysine-restricted diet, many patients have long-lasting and untreatable cognitive disability. The molecular basis of PDE is thought to be due to a buildup of DELTA1-piperideine-6-carboxylate, the cyclic form of the aldehyde substrate of ALDH7A1 |
763029 |
| 1.2.1.31 | metabolism |
human aldehyde dehydrogenase 7A1 (ALDH7A1) catalyzes the final step in lysine catabolism, the NAD+-dependent oxidation of alpha-aminoadipate semialdehyde to alpha-aminoadipate |
763029 |
| 1.2.1.31 | metabolism |
key enzyme in lysine oxidation |
763341 |
| 1.2.1.31 | physiological function |
the catalytically active oligomer of ALDH7A1 is assembled on demand in response to cofactor availability |
763029 |
