Homoserine dehydrogenase

From Wikipedia, the free encyclopedia

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

L-homoserine + NAD(P)+ $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

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

[edit] References

IUBMB entry for 1.1.1.3
BRENDA references for 1.1.1.3 (Recommended.)
PubMed references for 1.1.1.3
PubMed Central references for 1.1.1.3
Google Scholar references for 1.1.1.3
BLACK S, WRIGHT NG (1955). "Homoserine dehydrogenase". J. Biol. Chem. 213: 51–60. PMID 14353905.
Starnes WL, Munk P, Maul SB, Cunningham GN, Cox DJ, Shive W (1972). "Threonine-sensitive aspartokinase-homoserine dehydrogenase complex, amino acid composition, molecular weight, and subunit composition of the complex". Biochemistry. 11: 677–87. doi:10.1021/bi00755a003. PMID 4551091.
Veron M, Falcoz-Kelly F, Cohen GN (1972). "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. doi:10.1111/j.1432-1033.1972.tb01939.x. PMID 4562990.