EC Number   |
General Information |
Reference |
|---|
    1.2.1.3 | evolution |
enzyme ALDHTt belongs to the ALDH superfamily |
-, 763724 |
| 1.2.1.3 | evolution |
the enzyme belongs to the aldehyde dehydrogenase (ALDH) superfamily. Enzyme ALDH16 has an extra C-terminal domain of unknown function and shows absence of the essential catalytic cysteine residue in certain non-bacterial ALDH16 sequences |
763362 |
| 1.2.1.3 | evolution |
the enzyme belongs to the aldehyde dehydrogenase (ALDH) superfamily. Enzyme ALDH16 has an extra C-terminal domain of unknown function and shows absence of the essential catalytic cysteine residue in certain non-bacterial ALDH16 sequences. The Loktanella ALDH16 structure may be considered to be the archetype of the ALDH16 family |
763362 |
| 1.2.1.3 | evolution |
the enzyme is a member of Arabidopsis thaliana ALDH family 3 |
763728 |
| 1.2.1.3 | evolution |
the enzyme is a member of Arabidopsis thaliana ALDH family 7 |
763728 |
| 1.2.1.3 | malfunction |
ALDH2 inhibition suppresses cocaine self-administration and seeking behavior and prevents cocaine- or cue-induced reinstatement in a rat model of cocaine relapse-like behavior |
713089 |
| 1.2.1.3 | malfunction |
ALDH7A1 knockdown sensitizes human renal proximal tubular epithelial cells and CHO cells to hyperosmotic stress |
712435 |
| 1.2.1.3 | malfunction |
decreased ALDH3A1 activity is associated with pathologic corneas (cataract development) |
711635 |
| 1.2.1.3 | malfunction |
endosperms from aldh7 null mutants accumulate brown pigments (melanoidin) during desiccation and storage |
713308 |
| 1.2.1.3 | malfunction |
enzyme residues Ala505 and Gln506 interact with the conserved aldehyde anchor loop structure in the closed state. The apparent involvement of these residues in catalysis is significant because they are replaced by Pro505 and Lys506 in a genetic deletion (c.1512delG) that causes pyridoxine-dependent epilepsy, a rare autosomal recessive disorder that typically presents with seizures in the first days of life. Compromised ALDH7A1 activity leads to increased levels of alpha-aminoadipate semialdehyde and DELTA1-piperideine-6-carboxylic acid (P6C), the cyclized form of alpha-aminoadipate semialdehyde. P6C reacts with a ubiquitous cofactor, pyridoxal 5'-phosphate, and the resulting adduct is incapable as an enzyme cofactor. Site-directed single mutations A505P and Q506K and double mutation A505P/Q506K as well as the C-terminal truncation mutant DELTA504-511, which lacks residues 504-511, are analyzed with steady-state kinetics assays and analytical ultracentrifugation. The mutant enzymes exhibit a common phenotype characterized by a very high Km for alpha-aminoadipate semialdehyde (AASAL) and a perturbed self-association equilibrium |
744371 |
