Homoserine dehydrogenase

In enzymology, a homoserine dehydrogenase (EC number|1.1.1.3) is an enzyme that catalyzes the chemical reaction

:L-homoserine + NAD(P)+ $ightleftharpoons$ L-aspartate 4-semialdehyde + NAD(P)H + H⁺

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

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-homoserine:NAD(P)+ oxidoreductase. Other names in common use include HSDH, and HSD. This enzyme participates in glycine, serine and threonine metabolism and lysine biosynthesis.

tructural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes PDB link|1EBF, PDB link|1EBU, PDB link|1Q7G, and PDB link|1TVE.

References

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External links

::"The CAS registry number for this enzyme class is CAS registry|9028-13-1."

Gene Ontology (GO) codes