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