Aspartate-semialdehyde dehydrogenase

In enzymology, an aspartate-semialdehyde dehydrogenase is an enzyme that catalyzes the chemical reaction


 * L-aspartate 4-semialdehyde + phosphate + NADP+ $$\rightleftharpoons$$ L-4-aspartyl phosphate + NADPH + H+

The 3 substrates of this enzyme are L-aspartate 4-semialdehyde, phosphate, and NADP+, whereas its 3 products are L-4-aspartyl phosphate, NADPH, and H+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-aspartate-4-semialdehyde:NADP+ oxidoreductase (phosphorylating). Other names in common use include aspartate semialdehyde dehydrogenase, aspartic semialdehyde dehydrogenase, L-aspartate-beta-semialdehyde:NADP+ oxidoreductase, (phosphorylating), aspartic beta-semialdehyde dehydrogenase, and ASA dehydrogenase. This enzyme participates in glycine, serine and threonine metabolism and lysine biosynthesis.

Structural studies
As of late 2007, 24 structures have been solved for this class of enzymes, with PDB accession codes, , , , , , , , , , , , , , , , , , , , , , , and.