In
enzymology, a
homoserine dehydrogenase is an
enzyme that
catalyzes the
chemical reaction- L-homoserine + NAD(P)+ 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.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
- BLACK S, WRIGHT NG "Homoserine dehydrogenase". J. Biol. Chem. 213 51–60.
- Starnes WL, Munk P, Maul SB, Cunningham GN, Cox DJ, Shive W "Threonine-sensitive aspartokinase-homoserine dehydrogenase complex, amino acid composition, molecular weight, and subunit composition of the complex". Biochemistry. 11 677–87.
- Veron M, Falcoz-Kelly F, Cohen GN "The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. The two catalytic activities are carried by two independent regions of the polypeptide chain". Eur. J. Biochem. 28 520–7.
External links
- The CAS registry number for this enzyme class is .
Gene Ontology (GO) codes