220.127.116.11 - Aspartate-semialdehyde dehydrogenase
- ASA dehydrogenase.
- L-aspartate-beta-semialdehyde dehydrogenase.
- Aspartic semialdehyde dehydrogenase.
L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH
There are no Cofactors for this Enzyme
Aspartate-beta-semialdehyde dehydrogenase (ASADH) lies at the first branch point in the biosynthetic pathway that converts L-aspartic acid to lysine, isoleucine, methionine, threonine and metabolic intermediates such as diaminopimelic acid. The reaction catalysed is the reductive dephosphorylation of L-beta-aspartyl phosphate to L-aspartate-beta-semialdehyde, in the presence of NADPH. ASADH occurs in plants, most bacteria and fungi.
The mechanism of ASADH is thought to be very similar to that of Glyceraldehyde-3-phosphate dehydrogenase. In the suggested mechanism the cysteine thiolate attacks the substrate carbonyl to form a thioester intermediate. This is followed by the transfer of a hydride to NADP to form NADPH. The oxygen anion of a bound inorganic phosphate attacks the thioester intermediate to expel the cysteine thiolate and to form the phosphorylated product.
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There are no kinetic parameters information for this Enzyme
- Structural characterization of aspartate-semialdehyde dehydrogenase from Pseudomonas aeruginosa and Neisseria gonorrhoeae.
- Evaluation of a novel inhibitor of aspartate semialdehyde dehydrogenase as a potent antitubercular agent against Mycobacterium tuberculosis.
- IMB-XMA0038, a new inhibitor targeting aspartate-semialdehyde dehydrogenase of Mycobacterium tuberculosis.
- Molecular evolution, binding site interpretation and functional divergence of aspartate semialdehyde dehydrogenase.
- In silico anti-fungal efficacy and the mechanism of binding of some Syzygium aromaticum ingredient compounds to aspartate semialdehyde dehydrogenase, 6C8W and 6C85, enzymes from Blastomyces dermatitidis.
- Aspartate semialdehyde dehydrogenase inhibition suppresses the growth of the pathogenic fungus Candida albicans.
- Structural insights into inhibitor binding to a fungal ortholog of aspartate semialdehyde dehydrogenase.
- Structure of a fungal form of aspartate-semialdehyde dehydrogenase from Aspergillus fumigatus.
- Identification of anti-filarial leads against aspartate semialdehyde dehydrogenase of Wolbachia endosymbiont of Brugia malayi: combined molecular docking and molecular dynamics approaches.
- Structure of a fungal form of aspartate semialdehyde dehydrogenase from Cryptococcus neoformans.
- Elaboration of a fragment library hit produces potent and selective aspartate semialdehyde dehydrogenase inhibitors.