The Enzyme Database

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Accepted name: homoserine dehydrogenase
Reaction: L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
For diagram of threonine biosynthesis, click here
Other name(s): HSDH; HSD
Systematic name: L-homoserine:NAD(P)+ oxidoreductase
Comments: The yeast enzyme acts most rapidly with NAD+; the Neurospora enzyme with NADP+. The enzyme from Escherichia coli is a multi-functional protein, which also catalyses the reaction of EC (aspartate kinase).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-13-1
1.  Black, S. and Wright, N.G. Homoserine dehydrogenase. J. Biol. Chem. 213 (1955) 51–60. [PMID: 14353905]
2.  Starnes, W.L., Munk, P., Maul, S.B., Cunningham, G.N., Cox, D.J. and Shive, W. Threonine-sensitive aspartokinase-homoserine dehydrogenase complex, amino acid composition, molecular weight, and subunit composition of the complex. Biochemistry 11 (1972) 677–687. [PMID: 4551091]
3.  Véron, M., Falcoz-Kelly, F. and Cohen, G.N. 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 (1972) 520–527. [DOI] [PMID: 4562990]
[EC created 1961, modified 1976]

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